Table for the 87,826 triples in graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt

SubjectPredicateObject
drug:'5'-O-(N-(L-Alanyl)-Sulfamoyl)Adenosinedrugbank:description" experimental This compound belongs to the purine nucleosides and analogues. These are compounds comprising a purine base attached to a sugar. Purine Nucleosides and Analogues Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Glycosyl Compounds Glycoamino Acids and Derivatives Alpha Amino Acid Amides Pentoses Purines and Purine Derivatives Aminopyrimidines and Derivatives N-substituted Imidazoles Primary Aromatic Amines Oxolanes Sulfuric Acid Amide Esters Tetrahydrofurans Organic Sulfites 1,2-Diols Secondary Alcohols Carboxylic Acid Amides Enolates Polyamines Ethers Monoalkylamines alpha-amino acid amide alpha-amino acid or derivative pentose monosaccharide purine imidazopyrimidine aminopyrimidine pyrimidine primary aromatic amine monosaccharide sulfuric acid amide ester n-substituted imidazole sulfuric acid derivative tetrahydrofuran imidazole azole organic sulfite oxolane carboxamide group 1,2-diol secondary alcohol carboxylic acid derivative ether enolate polyamine amine alcohol primary amine organonitrogen compound primary aliphatic amine logP -1.4 ALOGPS logS -2 ALOGPS Water Solubility 4.58e+00 g/l ALOGPS logP -3.9 ChemAxon IUPAC Name (2S)-2-amino-1-[({[(2S,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}sulfonyl)amino]propan-1-one ChemAxon Traditional IUPAC Name (2S)-2-amino-1-({[(2S,3R,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxysulfonyl}amino)propan-1-one ChemAxon Molecular Weight 417.398 ChemAxon Monoisotopic Weight 417.106666687 ChemAxon SMILES C[C@H](N)C(=O)NS(=O)(=O)OC[C@@H]1O[C@H]([C@H](O)[C@H]1O)N1C=NC2=C1N=CN=C2N ChemAxon Molecular Formula C13H19N7O7S ChemAxon InChI InChI=1S/C13H19N7O7S/c1-5(14)12(23)19-28(24,25)26-2-6-8(21)9(22)13(27-6)20-4-18-7-10(15)16-3-17-11(7)20/h3-6,8-9,13,21-22H,2,14H2,1H3,(H,19,23)(H2,15,16,17)/t5-,6-,8-,9+,13+/m0/s1 ChemAxon InChIKey InChIKey=CWWYMWDIYBJVLP-KOMLLWLHSA-N ChemAxon Polar Surface Area (PSA) 217.8 ChemAxon Refractivity 92.14 ChemAxon Polarizability 38.21 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 12 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 2.75 ChemAxon pKa (strongest basic) 6.76 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 0 ChemAxon PubChem Compound 46936655 PubChem Substance 46509106 PDB A5A BE0000188 Bifunctional glutamate/proline--tRNA ligase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Bifunctional glutamate/proline--tRNA ligase Translation, ribosomal structure and biogenesis EPRS 1q41-q42 None 7.75 163028.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3418 GenAtlas EPRS GeneCards EPRS GenBank Gene Database X54326 GenBank Protein Database 31958 UniProtKB P07814 UniProt Accession SYEP_HUMAN EC 6.1.1.15 EC 6.1.1.17 Glutamate--tRNA ligase Prolyl-tRNA synthetase >Bifunctional aminoacyl-tRNA synthetase [Includes: Glutamyl-tRNA synthetase MEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNA AWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPG AEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVI LEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHR KNPIEKNLQMWEEMKKGSQFGHSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYN VYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTV LSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKI WAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFI EGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKFNLENKDYKKTTKVTWLAE TTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQL QRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPF KERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYK EKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINE AVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQG EVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKS EKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVI TKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKT HVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVR WEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTE KEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNS WGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRR RLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTV AENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEID CEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY >4323 bp ATGGAACATACTGAGATTGATCACTGGTTGGAGTTCAGTGCTACAAAATTATCTTCATGT GATTCCTTTACTTCTACAATTAATGAACTCAATCATTGCCTGTCTCTGAGAACATACTTA GTTGGAAACTCCTTGAGTTTAGCAGATTTATGTGTTTGGGCCACCCTAAAAGGAAATGCT GCCTGGCAAGAACAGTTGAAACAGAAGAAAGCTCCAGTTCATGTAAAACGTTGGTTTGGC TTTCTTGAAGCCCAGCAGGCCTTCCAGTCAGTAGGTACCAAGTGGGATGTTTCAACAACC AAAGCTCGAGTGGCACCTGAGAAAAAGCAAGATGTTGGGAAATTTGTTGAGCTTCCAGGT GCGGAGATGGGAAAGGTTACCGTCAGATTTCCTCCAGAGGCCAGTGGTTACTTACACATT GGGCATGCAAAAGCTGCTCTTCTGAACCAGCACTACCAGGTTAACTTTAAAGGGAAACTG ATCATGAGATTTGATGACACAAATCCTGAAAAAGAAAAGGAAGATTTTGAGAAGGTTATC TTGGAAGATGTTGCAATGTTGCATATCAAACCAGATCAATTTACTTATACTTCGGATCAT TTTGAAACTATAATGAAGTATGCAGAGAAGCTAATTCAAGAAGGGAAGGCTTATGTGGAT GATACTCCTGCTGAACAGATGAAAGCAGAACGTGAGCAGAGGATAGAATCTAAACATAGA AAAAACCCTATTGAGAAGAATCTACAAATGTGGGAAGAAATGAAAAAAGGGAGCCAGTTT GGTCACTCCTGTTGTTTGCGAGCAAAAATTGACATGAGTAGTAACAATGGATGCATGAGA GATCCAACCCTTTATCGCTGCAAAATTCAACCACATCCAAGAACTGGAAATAAATACAAT GTTTATCCAACATATGATTTTGCCTGCCCCATAGTTGACAGCATCGAAGGTGTTACACAT GCCCTGAGAACAACAGAATACCATGACAGAGATGAGCAGTTTTACTGGATTATTGAAGCT TTAGGCATAAGAAAACCATATATTTGGGAATATAGTCGGCTAAATCTCAACAACACAGTG CTATCCAAAAGAAAACTCACATGGTTTGTCAATGAAGGACTAGTAGATGGATGGGATGAC CCAAGATTTCCTACGGTTCGTGGTGTACTGAGAAGAGGGATGACAGTTGAAGGACTGAAA CAGTTTATTGCTGCTCAGGGCTCCTCACGTTCAGTCGTGAACATGGAGTGGGACAAAATC TGGGCGTTTAACAAAAAGGTTATTGACCCAGTGGCTCCACGATATGTTGCATTACTGAAG AAAGAAGTGATCCCAGTGAATGTACCTGAAGCTCAGGAGGAGATGAAAGAAGTAGCCAAA CACCCAAAGAATCCTGAGGTTGGCTTGAAGCCTGTGTGGTATAGTCCCAAAGTTTTCATT GAAGGTGCTGATGCAGAGACTTTTTCGGAGGGTGAGATGGTTACATTTATAAATTGGGGC AACCTCAACATTACAAAAATACACAAAAATGCAGATGGAAAAATCATATCTCTTGATGCA AAGTTTAATTTGGAAAACAAAGACTACAAGAAAACCACTAAGGTCACTTGGCTTGCAGAG ACTACACATGCTCTTCCTATTCCAGTAATCTGTGTCACTTATGAGCACTTGATCACAAAG CCAGTGCTAGGAAAAGACGAGGACTTTAAGCAGTATGTCAACAAGAACAGTAAGCATGAA GAGCTAATGCTAGGGGATCCCTGCCTTAAGGATTTGAAAAAAGGAGATATTATACAACTC CAGAGAAGAGGATTCTTCATATGTGATCAACCTTATGAACCTGTTAGCCCATATAGTTGC AAGGAAGCCCCGTGTGTTTTGATATACATTCCTGATGGGCACACAAAGGAAATGCCAACA TCAGGGTCAAAGGAAAAGACCAAAGTAGAAGCCACAAAAAATGAGACCTCTGCTCCTTTT AAGGAAAGACCAACACCTTCTCTGAATAATAATTGTACTACATCTGAGGATTCCTTGGTC CTTTACAATAGAGTGGCTGTTCAAGGAGATGTGGTTCGTGAATTAAAAGCCAAGAAAGCA CCAAAGGAAGATGTAGATGCAGCTGTAAAACAGCTTTTGTCTTTGAAAGCTGAATATAAG GAGAAAACTGGCCAGGAATATAAACCTGGAAACCCTCCTGCTGAAATAGGACAGAATATT TCTTCTAATTCCTCAGCAAGTATTCTGGAAAGTAAATCTCTGTATGATGAAGTTGCTGCA CAAGGGGAGGTGGTTCGTAAGCTAAAAGCTGAAAAATCCCCTAAGGCTAAAATAAATGAA GCTGTAGAATGCTTACTGTCCCTGAAGGCTCAGTATAAAGAAAAAACTGGGAAGGAGTAC ATACCTGGTCAGCCCCCATTATCTCAAAGTTCGGATTCAAGCCCAACCAGAAATTCTGAA CCTGCTGGTTTAGAAACACCAGAAGCGAAAGTACTTTTTGACAAAGTAGCTTCTCAAGGG GAAGTAGTTCGGAAACTTAAAACTGAAAAAGCCCCTAAGGATCAAGTAGATATAGCTGTT CAAGAACTCCTTCAGCTAAAGGCACAGTACAAGTCTTTGATAGGAGTAGAGTATAAGCCT GTGTCGGCCACTGGAGCTGAGGACAAAGATAAGAAGAAGAAAGAAAAAGAAAATAAATCT GAAAAGCAGAATAAGCCTCAGAAACAAAATGATGGCCAAAGGAAAGACCCTTCTAAAAAC CAAGGAGGTGGGCTCTCATCAAGTGGAGCAGGAGAAGGGCAGGGGCCTAAGAAACAGACC AGGTTGGGTCTTGAGGCAAAAAAAGAAGAAAATCTTGCTGATTGGTATTCTCAGGTCATC ACAAAGTCAGAAATGATTGAATACCATGACATAAGTGGCTGTTATATTCTTCGTCCCTGG GCCTATGCCATTTGGGAAGCCATCAAGGACTTTTTTGATGCTGAGATCAAGAAACTTGGT GTTGAAAACTGCTACTTCCCCATGTTTGTGTCTCAAAGTGCATTAGAGAAAGAGAAGACT CATGTTGCTGACTTTGCCCCAGAGGTTGCTTGGGTTACAAGATCTGGCAAAACCGAGCTG GCAGAACCAATTGCCATTCGTCCTACTAGTGAAACAGTAATGTATCCTGCATATGCAAAA TGGGTACAATCACACAGAGACCTGCCCATCAAGCTCAATCAGTGGTGCAATGTGGTGCGT TGGGAATTCAAGCATCCTCAGCCTTTCCTACGTACTCGTGAATTTCTTTGGCAGGAAGGG CACAGTGCTTTTGCTACCATGGAAGAGGCAGCGGAAGAGGTCTTGCAGATACTTGACTTA TATGCTCAGGTATATGAAGAACTCCTGGCAATTCCTGTTGTTAAAGGAAGAAAGACGGAA AAGGAAAAATTTGCAGGAGGAGACTATACAACTACAATAGAAGCATTTATATCTGCTAGT GGAAGAGCTATCCAGGGAGGAACATCACATCATTTAGGGCAGAATTTTTCCAAAATGTTT GAAATCGTTTTTGAAGATCCAAAGATACCAGGAGAGAAGCAATTTGCCTATCAAAACTCC TGGGGCCTGACAACTCGAACTATTGGTGTTATGACCATGGTTCATGGGGACAACATGGGT TTAGTATTACCACCCCGTGTAGCATGTGTTCAGGTGGTGATTATTCCTTGTGGCATTACC AATGCACTTTCTGAAGAAGACAAAGAAGCGCTGATTGCAAAATGCAATGATTATCGAAGG CGATTACTCAGTGTTAACATCCGCGTTAGAGCTGATTTACGAGATAATTATTCTCCAGGT TGGAAATTCAATCACTGGGAGCTCAAGGGAGTTCCCATTAGACTTGAAGTTGGGCCACGT GATATGAAGAGCTGTCAGTTTGTAGCCGTCAGACGAGATACTGGAGAAAAGCTGACAGTT GCTGAAAATGAGGCAGAGACTAAACTTCAAGCTATTTTGGAAGACATCCAGGTCACCCTT TTCACAAGGGCTTCTGAAGACCTTAAGACTCATATGGTTGTGGCTAATACAATGGAAGAC TTTCAGAAGATACTAGATTCTGGAAAGATTGTTCAGATTCCATTCTGTGGGGAAATTGAC TGTGAGGACTGGATCAAAAAGACCACTGCCAGGGATCAAGATCTTGAACCTGGTGCTCCA TCCATGGGAGCTAAAAGCCTTTGCATCCCCTTCAAACCACTCTGTGAACTGCAGCCTGGA GCCAAATGTGTCTGTGGCAAGAACCCTGCCAAGTACTACACCTTATTTGGTCGCAGCTAC TGA PF00587 tRNA-synt_2b PF03129 HGTP_anticodon PF00749 tRNA-synt_1c PF03950 tRNA-synt_1c_C PF00458 WHEP-TRS component cell component intracellular component cytoplasm function nucleotide binding function ligase activity, forming phosphoric ester bonds function purine nucleotide binding function RNA ligase activity function adenyl nucleotide binding function tRNA ligase activity function binding function ATP binding function catalytic activity function proline-tRNA ligase activity function glutamate-tRNA ligase activity function ligase activity process RNA metabolism process tRNA metabolism process tRNA aminoacylation process physiological process process tRNA aminoacylation for protein translation process macromolecule biosynthesis process metabolism process protein biosynthesis process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process prolyl-tRNA aminoacylation process macromolecule metabolism process glutamyl-tRNA aminoacylation "
drug:'5'-O-(N-(L-Alanyl)-Sulfamoyl)Adenosinerdfs:label"'5'-O-(N-(L-Alanyl)-Sulfamoyl)Adenosine"
drug:'5'-O-(N-(L-Alanyl)-Sulfamoyl)Adenosineowl:sameAsdrug:EXPT00374
drug:'5'-O-(N-(L-Alanyl)-Sulfamoyl)Adenosinerdf:typedrugbank:drugs
drug:'5'-O-(N-(L-Prolyl)-Sulfamoyl)Adenosinedrugbank:description" experimental This compound belongs to the purine nucleosides and analogues. These are compounds comprising a purine base attached to a sugar. Purine Nucleosides and Analogues Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Glycosyl Compounds Alpha Amino Acid Amides Pentoses Purines and Purine Derivatives Pyrrolidinecarboxamides Aminopyrimidines and Derivatives Primary Aromatic Amines N-substituted Imidazoles Tetrahydrofurans Sulfuric Acid Amide Esters Organic Sulfites Oxolanes 1,2-Diols Secondary Alcohols Carboxylic Acid Amides Dialkylamines Polyamines Enolates Ethers alpha-amino acid amide pentose monosaccharide imidazopyrimidine purine pyrrolidine-2-carboxamide pyrrolidine carboxylic acid or derivative aminopyrimidine monosaccharide sulfuric acid amide ester pyrimidine n-substituted imidazole primary aromatic amine organic sulfite azole imidazole tetrahydrofuran sulfuric acid derivative oxolane pyrrolidine carboxamide group secondary alcohol 1,2-diol enolate carboxylic acid derivative polyamine secondary amine secondary aliphatic amine ether organonitrogen compound amine alcohol primary amine logP -1.5 ALOGPS logS -2 ALOGPS Water Solubility 4.09e+00 g/l ALOGPS logP -3.6 ChemAxon IUPAC Name [({[(2S,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}sulfonyl)amino](2S)-pyrrolidin-2-ylmethanone ChemAxon Traditional IUPAC Name ({[(2S,3R,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxysulfonyl}amino)(2S)-pyrrolidin-2-ylmethanone ChemAxon Molecular Weight 443.435 ChemAxon Monoisotopic Weight 443.122316751 ChemAxon SMILES NC1=NC=NC2=C1N=CN2[C@@H]1O[C@@H](COS(=O)(=O)NC(=O)[C@@H]2CCCN2)[C@H](O)[C@H]1O ChemAxon Molecular Formula C15H21N7O7S ChemAxon InChI InChI=1S/C15H21N7O7S/c16-12-9-13(19-5-18-12)22(6-20-9)15-11(24)10(23)8(29-15)4-28-30(26,27)21-14(25)7-2-1-3-17-7/h5-8,10-11,15,17,23-24H,1-4H2,(H,21,25)(H2,16,18,19)/t7-,8-,10-,11+,15+/m0/s1 ChemAxon InChIKey InChIKey=LKVJEMXWEODCAY-WTOVGXSXSA-N ChemAxon Polar Surface Area (PSA) 203.81 ChemAxon Refractivity 99.71 ChemAxon Polarizability 41.76 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 12 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 2.73 ChemAxon pKa (strongest basic) 9.4 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 0 ChemAxon PubChem Compound 46936411 PubChem Substance 46506105 ChemSpider 2532941 PDB P5A BE0000188 Bifunctional glutamate/proline--tRNA ligase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Bifunctional glutamate/proline--tRNA ligase Translation, ribosomal structure and biogenesis EPRS 1q41-q42 None 7.75 163028.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3418 GenAtlas EPRS GeneCards EPRS GenBank Gene Database X54326 GenBank Protein Database 31958 UniProtKB P07814 UniProt Accession SYEP_HUMAN EC 6.1.1.15 EC 6.1.1.17 Glutamate--tRNA ligase Prolyl-tRNA synthetase >Bifunctional aminoacyl-tRNA synthetase [Includes: Glutamyl-tRNA synthetase MEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNA AWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPG AEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVI LEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHR KNPIEKNLQMWEEMKKGSQFGHSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYN VYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTV LSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKI WAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFI EGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKFNLENKDYKKTTKVTWLAE TTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQL QRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPF KERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYK EKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINE AVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQG EVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKS EKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVI TKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKT HVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVR WEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTE KEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNS WGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRR RLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTV AENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEID CEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY >4323 bp ATGGAACATACTGAGATTGATCACTGGTTGGAGTTCAGTGCTACAAAATTATCTTCATGT GATTCCTTTACTTCTACAATTAATGAACTCAATCATTGCCTGTCTCTGAGAACATACTTA GTTGGAAACTCCTTGAGTTTAGCAGATTTATGTGTTTGGGCCACCCTAAAAGGAAATGCT GCCTGGCAAGAACAGTTGAAACAGAAGAAAGCTCCAGTTCATGTAAAACGTTGGTTTGGC TTTCTTGAAGCCCAGCAGGCCTTCCAGTCAGTAGGTACCAAGTGGGATGTTTCAACAACC AAAGCTCGAGTGGCACCTGAGAAAAAGCAAGATGTTGGGAAATTTGTTGAGCTTCCAGGT GCGGAGATGGGAAAGGTTACCGTCAGATTTCCTCCAGAGGCCAGTGGTTACTTACACATT GGGCATGCAAAAGCTGCTCTTCTGAACCAGCACTACCAGGTTAACTTTAAAGGGAAACTG ATCATGAGATTTGATGACACAAATCCTGAAAAAGAAAAGGAAGATTTTGAGAAGGTTATC TTGGAAGATGTTGCAATGTTGCATATCAAACCAGATCAATTTACTTATACTTCGGATCAT TTTGAAACTATAATGAAGTATGCAGAGAAGCTAATTCAAGAAGGGAAGGCTTATGTGGAT GATACTCCTGCTGAACAGATGAAAGCAGAACGTGAGCAGAGGATAGAATCTAAACATAGA AAAAACCCTATTGAGAAGAATCTACAAATGTGGGAAGAAATGAAAAAAGGGAGCCAGTTT GGTCACTCCTGTTGTTTGCGAGCAAAAATTGACATGAGTAGTAACAATGGATGCATGAGA GATCCAACCCTTTATCGCTGCAAAATTCAACCACATCCAAGAACTGGAAATAAATACAAT GTTTATCCAACATATGATTTTGCCTGCCCCATAGTTGACAGCATCGAAGGTGTTACACAT GCCCTGAGAACAACAGAATACCATGACAGAGATGAGCAGTTTTACTGGATTATTGAAGCT TTAGGCATAAGAAAACCATATATTTGGGAATATAGTCGGCTAAATCTCAACAACACAGTG CTATCCAAAAGAAAACTCACATGGTTTGTCAATGAAGGACTAGTAGATGGATGGGATGAC CCAAGATTTCCTACGGTTCGTGGTGTACTGAGAAGAGGGATGACAGTTGAAGGACTGAAA CAGTTTATTGCTGCTCAGGGCTCCTCACGTTCAGTCGTGAACATGGAGTGGGACAAAATC TGGGCGTTTAACAAAAAGGTTATTGACCCAGTGGCTCCACGATATGTTGCATTACTGAAG AAAGAAGTGATCCCAGTGAATGTACCTGAAGCTCAGGAGGAGATGAAAGAAGTAGCCAAA CACCCAAAGAATCCTGAGGTTGGCTTGAAGCCTGTGTGGTATAGTCCCAAAGTTTTCATT GAAGGTGCTGATGCAGAGACTTTTTCGGAGGGTGAGATGGTTACATTTATAAATTGGGGC AACCTCAACATTACAAAAATACACAAAAATGCAGATGGAAAAATCATATCTCTTGATGCA AAGTTTAATTTGGAAAACAAAGACTACAAGAAAACCACTAAGGTCACTTGGCTTGCAGAG ACTACACATGCTCTTCCTATTCCAGTAATCTGTGTCACTTATGAGCACTTGATCACAAAG CCAGTGCTAGGAAAAGACGAGGACTTTAAGCAGTATGTCAACAAGAACAGTAAGCATGAA GAGCTAATGCTAGGGGATCCCTGCCTTAAGGATTTGAAAAAAGGAGATATTATACAACTC CAGAGAAGAGGATTCTTCATATGTGATCAACCTTATGAACCTGTTAGCCCATATAGTTGC AAGGAAGCCCCGTGTGTTTTGATATACATTCCTGATGGGCACACAAAGGAAATGCCAACA TCAGGGTCAAAGGAAAAGACCAAAGTAGAAGCCACAAAAAATGAGACCTCTGCTCCTTTT AAGGAAAGACCAACACCTTCTCTGAATAATAATTGTACTACATCTGAGGATTCCTTGGTC CTTTACAATAGAGTGGCTGTTCAAGGAGATGTGGTTCGTGAATTAAAAGCCAAGAAAGCA CCAAAGGAAGATGTAGATGCAGCTGTAAAACAGCTTTTGTCTTTGAAAGCTGAATATAAG GAGAAAACTGGCCAGGAATATAAACCTGGAAACCCTCCTGCTGAAATAGGACAGAATATT TCTTCTAATTCCTCAGCAAGTATTCTGGAAAGTAAATCTCTGTATGATGAAGTTGCTGCA CAAGGGGAGGTGGTTCGTAAGCTAAAAGCTGAAAAATCCCCTAAGGCTAAAATAAATGAA GCTGTAGAATGCTTACTGTCCCTGAAGGCTCAGTATAAAGAAAAAACTGGGAAGGAGTAC ATACCTGGTCAGCCCCCATTATCTCAAAGTTCGGATTCAAGCCCAACCAGAAATTCTGAA CCTGCTGGTTTAGAAACACCAGAAGCGAAAGTACTTTTTGACAAAGTAGCTTCTCAAGGG GAAGTAGTTCGGAAACTTAAAACTGAAAAAGCCCCTAAGGATCAAGTAGATATAGCTGTT CAAGAACTCCTTCAGCTAAAGGCACAGTACAAGTCTTTGATAGGAGTAGAGTATAAGCCT GTGTCGGCCACTGGAGCTGAGGACAAAGATAAGAAGAAGAAAGAAAAAGAAAATAAATCT GAAAAGCAGAATAAGCCTCAGAAACAAAATGATGGCCAAAGGAAAGACCCTTCTAAAAAC CAAGGAGGTGGGCTCTCATCAAGTGGAGCAGGAGAAGGGCAGGGGCCTAAGAAACAGACC AGGTTGGGTCTTGAGGCAAAAAAAGAAGAAAATCTTGCTGATTGGTATTCTCAGGTCATC ACAAAGTCAGAAATGATTGAATACCATGACATAAGTGGCTGTTATATTCTTCGTCCCTGG GCCTATGCCATTTGGGAAGCCATCAAGGACTTTTTTGATGCTGAGATCAAGAAACTTGGT GTTGAAAACTGCTACTTCCCCATGTTTGTGTCTCAAAGTGCATTAGAGAAAGAGAAGACT CATGTTGCTGACTTTGCCCCAGAGGTTGCTTGGGTTACAAGATCTGGCAAAACCGAGCTG GCAGAACCAATTGCCATTCGTCCTACTAGTGAAACAGTAATGTATCCTGCATATGCAAAA TGGGTACAATCACACAGAGACCTGCCCATCAAGCTCAATCAGTGGTGCAATGTGGTGCGT TGGGAATTCAAGCATCCTCAGCCTTTCCTACGTACTCGTGAATTTCTTTGGCAGGAAGGG CACAGTGCTTTTGCTACCATGGAAGAGGCAGCGGAAGAGGTCTTGCAGATACTTGACTTA TATGCTCAGGTATATGAAGAACTCCTGGCAATTCCTGTTGTTAAAGGAAGAAAGACGGAA AAGGAAAAATTTGCAGGAGGAGACTATACAACTACAATAGAAGCATTTATATCTGCTAGT GGAAGAGCTATCCAGGGAGGAACATCACATCATTTAGGGCAGAATTTTTCCAAAATGTTT GAAATCGTTTTTGAAGATCCAAAGATACCAGGAGAGAAGCAATTTGCCTATCAAAACTCC TGGGGCCTGACAACTCGAACTATTGGTGTTATGACCATGGTTCATGGGGACAACATGGGT TTAGTATTACCACCCCGTGTAGCATGTGTTCAGGTGGTGATTATTCCTTGTGGCATTACC AATGCACTTTCTGAAGAAGACAAAGAAGCGCTGATTGCAAAATGCAATGATTATCGAAGG CGATTACTCAGTGTTAACATCCGCGTTAGAGCTGATTTACGAGATAATTATTCTCCAGGT TGGAAATTCAATCACTGGGAGCTCAAGGGAGTTCCCATTAGACTTGAAGTTGGGCCACGT GATATGAAGAGCTGTCAGTTTGTAGCCGTCAGACGAGATACTGGAGAAAAGCTGACAGTT GCTGAAAATGAGGCAGAGACTAAACTTCAAGCTATTTTGGAAGACATCCAGGTCACCCTT TTCACAAGGGCTTCTGAAGACCTTAAGACTCATATGGTTGTGGCTAATACAATGGAAGAC TTTCAGAAGATACTAGATTCTGGAAAGATTGTTCAGATTCCATTCTGTGGGGAAATTGAC TGTGAGGACTGGATCAAAAAGACCACTGCCAGGGATCAAGATCTTGAACCTGGTGCTCCA TCCATGGGAGCTAAAAGCCTTTGCATCCCCTTCAAACCACTCTGTGAACTGCAGCCTGGA GCCAAATGTGTCTGTGGCAAGAACCCTGCCAAGTACTACACCTTATTTGGTCGCAGCTAC TGA PF00587 tRNA-synt_2b PF03129 HGTP_anticodon PF00749 tRNA-synt_1c PF03950 tRNA-synt_1c_C PF00458 WHEP-TRS component cell component intracellular component cytoplasm function catalytic activity function proline-tRNA ligase activity function glutamate-tRNA ligase activity function ligase activity function nucleotide binding function ligase activity, forming phosphoric ester bonds function purine nucleotide binding function RNA ligase activity function adenyl nucleotide binding function tRNA ligase activity function binding function ATP binding process macromolecule biosynthesis process metabolism process protein biosynthesis process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process prolyl-tRNA aminoacylation process macromolecule metabolism process glutamyl-tRNA aminoacylation process RNA metabolism process tRNA metabolism process tRNA aminoacylation process physiological process process tRNA aminoacylation for protein translation "
drug:'5'-O-(N-(L-Prolyl)-Sulfamoyl)Adenosinerdfs:label"'5'-O-(N-(L-Prolyl)-Sulfamoyl)Adenosine"
drug:'5'-O-(N-(L-Prolyl)-Sulfamoyl)Adenosineowl:sameAsdrug:EXPT02481
drug:'5'-O-(N-(L-Prolyl)-Sulfamoyl)Adenosinerdf:typedrugbank:drugs
drug:((2r,3s,5r)-3-Hydroxy-5-(4-Hydroxy-2-Oxo-3,4-Dihydropyrimidin-1(2h)-Yl)-Tetrahydrofuran-2-Yl)Methyldihydrogen Phosphatedrugbank:description" experimental This compound belongs to the pyrimidine 2'-deoxyribonucleoside monophosphates. These are pyrimidine nucleotides with a monophosphate group linked to the ribose moiety lacking an hydroxyl group at position 2. Pyrimidine 2'-deoxyribonucleoside Monophosphates Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Glycosyl Compounds Ureides Pyrimidones Organic Phosphoric Acids Organophosphate Esters Hydropyrimidines Tetrahydrofurans Oxolanes Secondary Alcohols Tertiary Amines Polyamines Ethers Enamines pyrimidone ureide phosphoric acid ester organic phosphate pyrimidine hydropyrimidine oxolane tetrahydrofuran secondary alcohol tertiary amine polyamine enamine ether alcohol organonitrogen compound amine logP -2.3 ALOGPS logS -1.5 ALOGPS Water Solubility 9.82e+00 g/l ALOGPS logP -1.9 ChemAxon IUPAC Name {[(2S,3R,5R)-3-hydroxy-5-[(4S)-4-hydroxy-2-oxo-1,2,3,4-tetrahydropyrimidin-1-yl]oxolan-2-yl]methoxy}phosphonic acid ChemAxon Traditional IUPAC Name [(2S,3R,5R)-3-hydroxy-5-[(4S)-4-hydroxy-2-oxo-3,4-dihydropyrimidin-1-yl]oxolan-2-yl]methoxyphosphonic acid ChemAxon Molecular Weight 310.1978 ChemAxon Monoisotopic Weight 310.056601978 ChemAxon SMILES O[C@@H]1C[C@@H](O[C@H]1COP(O)(O)=O)N1C=C[C@H](O)NC1=O ChemAxon Molecular Formula C9H15N2O8P ChemAxon InChI InChI=1S/C9H15N2O8P/c12-5-3-8(11-2-1-7(13)10-9(11)14)19-6(5)4-18-20(15,16)17/h1-2,5-8,12-13H,3-4H2,(H,10,14)(H2,15,16,17)/t5-,6+,7+,8-/m1/s1 ChemAxon InChIKey InChIKey=ILSIYJVILUIVPM-VGRMVHKJSA-N ChemAxon Polar Surface Area (PSA) 148.79 ChemAxon Refractivity 62.8 ChemAxon Polarizability 26.03 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 1.23 ChemAxon pKa (strongest basic) -3.2 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 46936941 PubChem Substance 46505026 PDB DDN BE0001709 Deoxycytidylate deaminase Enterobacteria phage T4 # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Deoxycytidylate deaminase Nucleotide transport and metabolism Supplies the nucleotide substrate for thymidylate synthetase CD Cytoplasmic None 7.94 21198.0 Enterobacteria phage T4 GenBank Gene Database J05172 GenBank Protein Database 215838 UniProtKB P16006 UniProt Accession DCTD_BPT4 dCD dCMP deaminase EC 3.5.4.12 >Deoxycytidylate deaminase MKASTVLQIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNGSPAGGVNCCDYAAEQGWLL NKPKHAIIQGHKPECVSFGSTDRFVLAKEHRSAHSEWSSKNEIHAELNAILFAARNGSSI EGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDKNKPGWDDILRNAGIEVFNVPKKNLN KLNWENINEFCGE >582 bp ATGAAAGCGAGTACAGTACTTCAAATTGCATATTTAGTATCGCAGGAATCAAAATGTTGC TCCTGGAAGGTAGGAGCAGTAATTGAAAAGAATGGACGTATTATTTCTACTGGGTATAAT GGTTCACCCGCAGGGGGTGTGAACTGTTGTGATTATGCTGCTGAGCAAGGATGGTTGTTG AATAAGCCTAAACATGCTATCATTCAAGGTCATAAGCCTGAATGCGTATCATTTGGTTCA ACTGATCGTTTTGTTTTGGCGAAAGAACATCGTAGTGCTCACTCGGAATGGTCATCTAAA AATGAAATTCATGCTGAACTAAATGCAATTTTGTTTGCTGCACGAAATGGTTCTTCTATT GAAGGTGCTACTATGTATGTAACACTTTCTCCTTGTCCAGATTGCGCAAAAGCGATAGCT CAATCTGGTATTAAAAAGCTGGTTTATTGTGAAACATACGACAAAAATAAACCCGGTTGG GATGATATTCTGCGAAATGCAGGTATTGAAGTGTTTAATGTTCCTAAGAAAAACTTGAAT AAGTTAAACTGGGAAAATATCAACGAATTCTGTGGTGAATAA PF00383 dCMP_cyt_deam_1 function binding function catalytic activity function hydrolase activity function ion binding function cation binding function transition metal ion binding function zinc ion binding "
drug:((2r,3s,5r)-3-Hydroxy-5-(4-Hydroxy-2-Oxo-3,4-Dihydropyrimidin-1(2h)-Yl)-Tetrahydrofuran-2-Yl)Methyldihydrogen Phosphaterdfs:label"((2r,3s,5r)-3-Hydroxy-5-(4-Hydroxy-2-Oxo-3,4-Dihydropyrimidin-1(2h)-Yl)-Tetrahydrofuran-2-Yl)Methyldihydrogen Phosphate"
drug:((2r,3s,5r)-3-Hydroxy-5-(4-Hydroxy-2-Oxo-3,4-Dihydropyrimidin-1(2h)-Yl)-Tetrahydrofuran-2-Yl)Methyldihydrogen Phosphateowl:sameAsdrug:EXPT01146
drug:((2r,3s,5r)-3-Hydroxy-5-(4-Hydroxy-2-Oxo-3,4-Dihydropyrimidin-1(2h)-Yl)-Tetrahydrofuran-2-Yl)Methyldihydrogen Phosphaterdf:typedrugbank:drugs
drug:(1'r,2's)-9-(2-Hydroxy-3'-Keto-Cyclopenten-1-Yl)Adeninedrugbank:description" experimental This compound belongs to the purines and purine derivatives. These are aromatic heterocyclic compounds containing a purine moiety, which is formed a pyrimidine-ring ring fused to an imidazole ring. Purines and Purine Derivatives Organic Compounds Heterocyclic Compounds Imidazopyrimidines Purines and Purine Derivatives Aminopyrimidines and Derivatives Primary Aromatic Amines N-substituted Imidazoles Secondary Alcohols Cyclic Alcohols and Derivatives 1,2-Diols Polyamines aminopyrimidine pyrimidine n-substituted imidazole primary aromatic amine azole imidazole cyclic alcohol 1,2-diol secondary alcohol polyamine amine alcohol primary amine organonitrogen compound logP -0.63 ALOGPS logS -1.5 ALOGPS Water Solubility 6.86e+00 g/l ALOGPS logP -1.2 ChemAxon IUPAC Name (1S,2S,5R)-5-(6-amino-9H-purin-9-yl)cyclopent-3-ene-1,2-diol ChemAxon Traditional IUPAC Name (1S,2S,5R)-5-(6-aminopurin-9-yl)cyclopent-3-ene-1,2-diol ChemAxon Molecular Weight 233.2266 ChemAxon Monoisotopic Weight 233.091274621 ChemAxon SMILES NC1=NC=NC2=C1N=CN2[C@@H]1C=C[C@H](O)[C@H]1O ChemAxon Molecular Formula C10H11N5O2 ChemAxon InChI InChI=1S/C10H11N5O2/c11-9-7-10(13-3-12-9)15(4-14-7)5-1-2-6(16)8(5)17/h1-6,8,16-17H,(H2,11,12,13)/t5-,6+,8+/m1/s1 ChemAxon InChIKey InChIKey=RQPALADHFYHEHK-CHKWXVPMSA-N ChemAxon Polar Surface Area (PSA) 110.08 ChemAxon Refractivity 61.44 ChemAxon Polarizability 22.39 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 13.19 ChemAxon pKa (strongest basic) 5.09 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 5287610 PubChem Substance 46505345 ChemSpider 1424 PDB ADC BE0001684 Adenosylhomocysteinase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Adenosylhomocysteinase Coenzyme transport and metabolism Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine AHCY 20cen-q13.1 Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to None 6.29 47717.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:343 GenAtlas AHCY GeneCards AHCY GenBank Gene Database M61831 GenBank Protein Database 178277 UniProtKB P23526 UniProt Accession SAHH_HUMAN AdoHcyase EC 3.3.1.1 S-adenosyl-L-homocysteine hydrolase >Adenosylhomocysteinase MSDKLPYKVADIGLAAWGRKALDIAENEMPGLMRMRERYSASKPLKGARIAGCLHMTVET AVLIETLVTLGAEVQWSSCNIFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYF KDGPLNMILDDGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVI ITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCIDIILGRHFEQMKDDAIVCNIG HFDVEIDVKWLNENAVEKVNIKPQVDRYRLKNGRRIILLAEGRLVNLGCAMGHPSFVMSN SFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMS CDGPFKPDHYRY >1299 bp ATGTCTGACAAACTGCCCTACAAAGTCGCCGACATCGGCCTGGCTGCCTGGGGACGCAAG GCCCTGGACATTGCTGAGAACGAGATGCCGGGCCTGATGCGTATGCGGGAGCGGTACTCG GCCTCCAAGCCACTGAAGGGCGCCCGCATCGCTGGCTGCCTGCACATGACCGTGGAGACG GCCGTCCTCATTGAGACCCTCGTCACCCTGGGTGCTGAGGTGCAGTGGTCCAGCTGCAAC ATCTTCTCCACCCAGAACCATGCGGCGGCTGCCATTGCCAAGGCTGGCATTCCGGTGTAT GCCTGGAAGGGCGAAACGGACGAGGAGTACCTGTGGTGCATTGAGCAGACCCTGTACTTC AAGGACGGGCCCCTCAACATGATTCTGGACGACGGGGGCGACCTCACCAACCTCATCCAC ACCAAGTACCCGCAGCTTCTGCCAGGCATCCGAGGCATCTCTGAGGAGACCACGACTGGG GTCCACAACCTCTACAAGATGATGGCCAATGGGATCCTCAAGGTGCCTGCCATCAATGTC AATGACTCCGTCACCAAGAGCAAGTTTGACAACCTCTATGGCTGCCGGGAGTCCCTCATA GATGGCATCAAGCGGGCCACAGATGTGATGATTGCCGGCAAGGTAGCGGTGGTAGCAGGC TATGGTGATGTGGGCAAGGGCTGTGCCCAGGCCCTGCGGGGTTTCGGAGCCCGCGTCATC ATCACCGAGATTGACCCCATCAACGCACTGCAGGCTGCCATGGAGGGCTATGAGGTGACC ACCATGGATGAGGCCTGTCAGGAGGGCAACATCTTTGTCACCACCACAGGCTGTATTGAC ATCATCCTTGGCCGGCACTTTGAGCAGATGAAGGATGATGCCATTGTGTGTAACATTGGA CACTTTGACGTGGAGATCGATGTCAAGTGGCTCAACGAGAACGCCGTGGAGAAGGTGAAC ATCAAGCCGCAGGTGGACCGGTATCGGTTGAAGAATGGGCGCCGCATCATCCTGCTGGCC GAGGGTCGGCTGGTCAACCTGGGTTGTGCCATGGGCCACCCCAGCTTCGTGATGAGTAAC TCCTTCACCAACCAGGTGATGGCGCAGATCGAGCTGTGGACCCATCCAGACAAGTACCCC GTTGGGGTTCATTTCCTGCCCAAGAAGCTGGATGAGGCAGTGGCTGAAGCCCACCTGGGC AAGCTGAATGTGAAGTTGACCAAGCTAACTGAGAAGCAAGCCCAGTACCTGGGCATGTCC TGTGATGGCCCCTTCAAGCCGGATCACTACCGCTACTGA PF05221 AdoHcyase PF00670 AdoHcyase_NAD function hydrolase activity, acting on ether bonds function trialkylsulfonium hydrolase activity function adenosylhomocysteinase activity function catalytic activity function hydrolase activity process physiological process process metabolism process cellular metabolism process one-carbon compound metabolism "
drug:(1'r,2's)-9-(2-Hydroxy-3'-Keto-Cyclopenten-1-Yl)Adeninerdfs:label"(1'r,2's)-9-(2-Hydroxy-3'-Keto-Cyclopenten-1-Yl)Adenine"
drug:(1'r,2's)-9-(2-Hydroxy-3'-Keto-Cyclopenten-1-Yl)Adenineowl:sameAsdrug:EXPT00427
drug:(1'r,2's)-9-(2-Hydroxy-3'-Keto-Cyclopenten-1-Yl)Adeninerdf:typedrugbank:drugs
drug:(1,10 Phenanthroline)-(Tri-Carbon Monoxide) Rhenium (I)drugbank:description" experimental This compound belongs to the phenanthrolines. These are aromatic polycyclic compounds containing the phenanthroline skeleton, which is a derivative of phenanthrene, and consists of two pyridine rings non-linearly joined by a benzene ring. Phenanthrolines Organic Compounds Heterocyclic Compounds Phenanthrolines Benzene and Substituted Derivatives Polyamines Metalloheterocyclic Compounds Organic Transition Metal Compounds benzene polyamine organonitrogen compound organometallic compound organic transition metal moeity logP 1.86 ALOGPS logS -2.5 ALOGPS Water Solubility 1.55e+00 g/l ALOGPS IUPAC Name 15,15,15-tris(hydroxymethyl)-1,12-diaza-15-rhenatetracyclo[10.2.1.0^{5,14}.0^{8,13}]pentadeca-2,4,6,8,10,13-hexaen-15-ylium ChemAxon Traditional IUPAC Name 15,15,15-tris(hydroxymethyl)-1,12-diaza-15-rhenatetracyclo[10.2.1.0^{5,14}.0^{8,13}]pentadeca-2,4,6,8,10,13-hexaen-15-ylium ChemAxon Molecular Weight 450.443 ChemAxon Monoisotopic Weight 451.009242919 ChemAxon SMILES [O]#C[Re+]1(C#[O])(C#[O])N2C=CC=C3C=CC4=CC=CN1C4=C23 ChemAxon Molecular Formula C15H8N2O3Re ChemAxon InChI InChI=1S/C12H8N2.3CO.Re/c1-3-9-5-6-10-4-2-8-14-12(10)11(9)13-7-1;3*1-2;/h1-8H;;;;/q-2;;;;+3 ChemAxon InChIKey InChIKey=MJGBWBLYZOUDIT-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 6.48 ChemAxon Refractivity 112.82 ChemAxon Polarizability 28.5 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 0 ChemAxon H Bond Donor Count 0 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon ChEBI 49851 PubChem Compound 17754141 PubChem Substance 46505489 PDB REP BE0001337 Azurin Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Azurin Energy production and conversion Transfers electrons from cytochrome c551 to cytochrome oxidase azu Periplasm None 6.93 16009.0 Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) GenBank Gene Database X07317 GenBank Protein Database 45292 UniProtKB P00282 UniProt Accession AZUR_PSEAE Azurin precursor >Azurin precursor MLRKLAAVSLLSLLSAPLLAAECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLP KNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVS KLKEGEQYMFFCTFPGHSALMKGTLTLK >447 bp ATGCTACGTAAACTCGCTGCGGTATCCCTGCTGTCCCTGCTCAGTGCGCCGCTGCTGGCT GCCGAGTGCTCGGTGGACATCCAGGGTAACGACCAGATGCAGTTCAACACCAATGCCATC ACCGTCGACAAGAGCTGCAAGCAGTTCACCGTCAACCTGTCCCACCCCGGCAACCTGCCG AAGAACGTCATGGGCCACAACTGGGTACTGAGCACCGCCGCCGACATGCAGGGCGTGGTC ACCGACGGCATGGCTTCCGGCCTGGACAAGGATTACCTGAAGCCCGACGACAGCCGCGTC ATCGCCCACACCAAGCTGATCGGCTCGGGCGAGAAGGACTCGGTGACCTTCGACGTCTCC AAGCTGAAGGAAGGCGAGCAGTACATGTTCTTCTGCACCTTCCCGGGCCACTCCGCGCTG ATGAAGGGCACCCTGACCCTGAAGTGA PF00127 Copper-bind function ion binding function cation binding function transition metal ion binding function transporter activity function electron transporter activity function binding function copper ion binding process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process BE0001069 Canalicular multispecific organic anion transporter 1 Human inhibitor # Akhteruzzaman S, Kato Y, Hisaka A, Sugiyama Y: Primary active transport of peptidic endothelin antagonists by rat hepatic canalicular membrane. J Pharmacol Exp Ther. 1999 Feb;288(2):575-81. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9918561 unknown Canalicular multispecific organic anion transporter 1 Defense mechanisms and drug export Mediates hepatobiliary excretion of numerous organic anions. May function as a cellular cisplatin transporter ABCC2 10q24 Membrane; multi-pass membrane protein 28-48 69-89 94-114 127-147 166-186 314-334 361-381 438-458 462-482 545-565 588-608 972-992 1034-1054 1098-1118 1120-1140 1212-1232 1235-1255 8.46 174194.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:53 GenAtlas ABCC2 GeneCards ABCC2 GenBank Gene Database U63970 GenBank Protein Database 1764162 UniProtKB Q92887 UniProt Accession MRP2_HUMAN ATP-binding cassette sub-family C member 2 Canalicular multidrug resistance protein Multidrug resistance-associated protein 2 >Canalicular multispecific organic anion transporter 1 MLEKFCNSTFWNSSFLDSPEADLPLCFEQTVLVWIPLGFLWLLAPWQLLHVYKSRTKRSS TTKLYLAKQVFVGFLLILAAIELALVLTEDSGQATVPAVRYTNPSLYLGTWLLVLLIQYS RQWCVQKNSWFLSLFWILSILCGTFQFQTLIRTLLQGDNSNLAYSCLFFISYGFQILILI FSAFSENNESSNNPSSIASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKTLVS KFETHMKRELQKARRALQRRQEKSSQQNSGARLPGLNKNQSQSQDALVLEDVEKKKKKSG TKKDVPKSWLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIG YLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKALTLSNLARKEYTVGET VNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAIL STKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFS QLQCVVIFVFQLTPVLVSVVTFSVYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMI SSMLQASVSTERLEKYLGGDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEATVRDVNLD IMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNIL FGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLD IYLLDDPLSAVDAHVGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIV EKGSYSALLAKKGEFAKNLKTFLRHTGPEEEATVHDGSEEEDDDYGLISSVEEIPEDAAS ITMRRENSFRRTLSRSSRSNGRHLKSLRNSLKTRNVNSLKEDEELVKGQKLIKKEFIETG KVKFSIYLEYLQAIGLFSIFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYPASQR DMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRI VNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMF YVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSW ITSNRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTS EIETNIVAVERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYRPELDLVLRGI TCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTII PQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIG QRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMD SDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKEAGIENVNSTKF >4638 bp ATGCTGGAGAAGTTCTGCAACTCTACTTTTTGGAATTCCTCATTCCTGGACAGTCCGGAG GCAGACCTGCCACTTTGTTTTGAGCAAACTGTTCTGGTGTGGATTCCCTTGGGCTTCCTA TGGCTCCTGGCCCCCTGGCAGCTTCTCCACGTGTATAAATCCAGGACCAAGAGATCCTCT ACCACCAAACTCTATCTTGCTAAGCAGGTATTCGTTGGTTTTCTTCTTATTCTAGCAGCC ATAGAGCTGGCCCTTGTACTCACAGAAGACTCTGGACAAGCCACAGTCCCTGCTGTTCGA TATACCAATCCAAGCCTCTACCTAGGCACATGGCTCCTGGTTTTGCTGATCCAATACAGC AGACAATGGTGTGTACAGAAAAACTCCTGGTTCCTGTCCCTATTCTGGATTCTCTCGATA CTCTGTGGCACTTTCCAATTTCAGACTCTGATCCGGACACTCTTACAGGGTGACAATTCT AATCTAGCCTACTCCTGCCTGTTCTTCATCTCCTACGGATTCCAGATCCTGATCCTGATC TTTTCAGCATTTTCAGAAAATAATGAGTCATCAAATAATCCATCATCCATAGCTTCATTC CTGAGTAGCATTACCTACAGCTGGTATGACAGCATCATTCTGAAAGGCTACAAGCGTCCT CTGACACTCGAGGATGTCTGGGAAGTTGATGAAGAGATGAAAACCAAGACATTAGTGAGC AAGTTTGAAACGCACATGAAGAGAGAGCTGCAGAAAGCCAGGCGGGCACTCCAGAGACGG CAGGAGAAGAGCTCCCAGCAGAACTCTGGAGCCAGGCTGCCTGGCTTGAACAAGAATCAG AGTCAAAGCCAAGATGCCCTTGTCCTGGAAGATGTTGAAAAGAAAAAAAAGAAGTCTGGG ACCAAAAAAGATGTTCCAAAATCCTGGTTGATGAAGGCTCTGTTCAAAACTTTCTACATG GTGCTCCTGAAATCATTCCTACTGAAGCTAGTGAATGACATCTTCACGTTTGTGAGTCCT CAGCTGCTGAAATTGCTGATCTCCTTTGCAAGTGACCGTGACACATATTTGTGGATTGGA TATCTCTGTGCAATCCTCTTATTCACTGCGGCTCTCATTCAGTCTTTCTGCCTTCAGTGT TATTTCCAACTGTGCTTCAAGCTGGGTGTAAAAGTACGGACAGCTATCATGGCTTCTGTA TATAAGAAGGCATTGACCCTATCCAACTTGGCCAGGAAGGAGTACACCGTTGGAGAAACA GTGAACCTGATGTCTGTGGATGCCCAGAAGCTCATGGATGTGACCAACTTCATGCACATG CTGTGGTCAAGTGTTCTACAGATTGTCTTATCTATCTTCTTCCTATGGAGAGAGTTGGGA CCCTCAGTCTTAGCAGGTGTTGGGGTGATGGTGCTTGTAATCCCAATTAATGCGATACTG TCCACCAAGAGTAAGACCATTCAGGTCAAAAATATGAAGAATAAAGACAAACGTTTAAAG ATCATGAATGAGATTCTTAGTGGAATCAAGATCCTGAAATATTTTGCCTGGGAACCTTCA TTCAGAGACCAAGTACAAAACCTCCGGAAGAAAGAGCTCAAGAACCTGCTGGCCTTTAGT CAACTACAGTGTGTAGTAATATTCGTCTTCCAGTTAACTCCAGTCCTGGTATCTGTGGTC ACATTTTCTGTTTATGTCCTGGTGGATAGCAACAATATTTTGGATGCACAAAAGGCCTTC ACCTCCATTACCCTCTTCAATATCCTGCGCTTTCCCCTGAGCATGCTTCCCATGATGATC TCCTCCATGCTCCAGGCCAGTGTTTCCACAGAGCGGCTAGAGAAGTACTTGGGAGGGGAT GACTTGGACACATCTGCCATTCGACATGACTGCAATTTTGACAAAGCCATGCAGTTTTCT GAGGCCTCCTTTACCTGGGAACATGATTCGGAAGCCACAGTCCGAGATGTGAACCTGGAC ATTATGGCAGGCCAACTTGTGGCTGTGATAGGCCCTGTCGGCTCTGGGAAATCCTCCTTG ATATCAGCCATGCTGGGAGAAATGGAAAATGTCCACGGGCACATCACCATCAAGGGCACC ACTGCCTATGTCCCACAGCAGTCCTGGATTCAGAATGGCACCATAAAGGACAACATCCTT TTTGGAACAGAGTTTAATGAAAAGAGGTACCAGCAAGTACTGGAGGCCTGTGCTCTCCTC CCAGACTTGGAAATGCTGCCTGGAGGAGATTTGGCTGAGATTGGAGAGAAGGGTATAAAT CTTAGTGGGGGTCAGAAGCAGCGGATCAGCCTGGCCAGAGCTACCTACCAAAATTTAGAC ATCTATCTTCTAGATGACCCCCTGTCTGCAGTGGATGCTCATGTAGGAAAACATATTTTT AATAAGGTCTTGGGCCCCAATGGCCTGTTGAAAGGCAAGACTCGACTCTTGGTTACACAT AGCATGCACTTTCTTCCTCAAGTGGATGAGATTGTAGTTCTGGGGAATGGAACAATTGTA GAGAAAGGATCCTACAGTGCTCTCCTGGCCAAAAAAGGAGAGTTTGCTAAGAATCTGAAG ACATTTCTAAGACATACAGGCCCTGAAGAGGAAGCCACAGTCCATGATGGCAGTGAAGAA GAAGACGATGACTATGGGCTGATATCCAGTGTGGAAGAGATCCCCGAAGATGCAGCCTCC ATAACCATGAGAAGAGAGAACAGCTTTCGTCGAACACTTAGCCGCAGTTCTAGGTCCAAT GGCAGGCATCTGAAGTCCCTGAGAAACTCCTTGAAAACTCGGAATGTGAATAGCCTGAAG GAAGACGAAGAACTAGTGAAAGGACAAAAACTAATTAAGAAGGAATTCATAGAAACTGGA AAGGTGAAGTTCTCCATCTACCTGGAGTACCTACAAGCAATAGGATTGTTTTCGATATTC TTCATCATCCTTGCGTTTGTGATGAATTCTGTGGCTTTTATTGGATCCAACCTCTGGCTC AGTGCTTGGACCAGTGACTCTAAAATCTTCAATAGCACCGACTATCCAGCATCTCAGAGG GACATGAGAGTTGGAGTCTACGGAGCTCTGGGATTAGCCCAAGGTATATTTGTGTTCATA GCACATTTCTGGAGTGCCTTTGGTTTCGTCCATGCATCAAATATCTTGCACAAGCAACTG CTGAACAATATCCTTCGAGCACCTATGAGATTTTTTGACACAACACCCACAGGCCGGATT GTGAACAGGTTTGCCGGCGATATTTCCACAGTGGATGACACCCTGCCTCAGTCCTTGCGC AGCTGGATTACATGCTTCCTGGGGATAATCAGCACCCTTGTCATGATCTGCATGGCCACT CCTGTCTTCACCATCATCGTCATTCCTCTTGGCATTATTTATGTATCTGTTCAGATGTTT TATGTGTCTACCTCCCGCCAGCTGAGGCGTCTGGACTCTGTCACCAGGTCCCCAATCTAC TCTCACTTCAGCGAGACCGTATCAGGTTTGCCAGTTATCCGTGCCTTTGAGCACCAGCAG CGATTTCTGAAACACAATGAGGTGAGGATTGACACCAACCAGAAATGTGTCTTTTCCTGG ATCACCTCCAACAGGTGGCTTGCAATTCGCCTGGAGCTGGTTGGGAACCTGACTGTCTTC TTTTCAGCCTTGATGATGGTTATTTATAGAGATACCCTAAGTGGGGACACTGTTGGCTTT GTTCTGTCCAATGCACTCAATATCACACAAACCCTGAACTGGCTGGTGAGGATGACATCA GAAATAGAGACCAACATTGTGGCTGTTGAGCGAATAACTGAGTACACAAAAGTGGAAAAT GAGGCACCCTGGGTGACTGATAAGAGGCCTCCGCCAGATTGGCCCAGCAAAGGCAAGATC CAGTTTAACAACTACCAAGTGCGGTACCGACCTGAGCTGGATCTGGTCCTCAGAGGGATC ACTTGTGACATCGGTAGCATGGAGAAGATTGGTGTGGTGGGCAGGACAGGAGCTGGAAAG TCATCCCTCACAAACTGCCTCTTCAGAATCTTAGAGGCTGCCGGTGGTCAGATTATCATT GATGGAGTAGATATTGCTTCCATTGGGCTCCACGACCTCCGAGAGAAGCTGACCATCATC CCCCAGGACCCCATCCTGTTCTCTGGAAGCCTGAGGATGAATCTCGACCCTTTCAACAAC TACTCAGATGAGGAGATTTGGAAGGCCTTGGAGCTGGCTCACCTCAAGTCTTTTGTGGCC AGCCTGCAACTTGGGTTATCCCACGAAGTGACAGAGGCTGGTGGCAACCTGAGCATAGGC CAGAGGCAGCTGCTGTGCCTGGGCAGGGCTCTGCTTCGGAAATCCAAGATCCTGGTCCTG GATGAGGCCACTGCTGCGGTGGATCTAGAGACAGACAACCTCATTCAGACGACCATCCAA AACGAGTTCGCCCACTGCACAGTGATCACCATCGCCCACAGGCTGCACACCATCATGGAC AGTGACAAGGTAATGGTCCTAGACAACGGGAAGATTATAGAGTGCGGCAGCCCTGAAGAA CTGCTACAAATCCCTGGACCCTTTTACTTTATGGCTAAGGAAGCTGGCATTGAGAATGTG AACAGCACAAAATTCTAG PF00005 ABC_tran PF00664 ABC_membrane component membrane component cell component intrinsic to membrane component integral to membrane function catalytic activity function ATP binding function hydrolase activity function hydrolase activity, acting on acid anhydrides function nucleotide binding function hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides function transporter activity function pyrophosphatase activity function purine nucleotide binding function nucleoside-triphosphatase activity function adenyl nucleotide binding function ATPase activity function hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances function ATPase activity, coupled to transmembrane movement of substances function binding process cellular physiological process process transport process physiological process "
drug:(1,10 Phenanthroline)-(Tri-Carbon Monoxide) Rhenium (I)rdfs:label"(1,10 Phenanthroline)-(Tri-Carbon Monoxide) Rhenium (I)"
drug:(1,10 Phenanthroline)-(Tri-Carbon Monoxide) Rhenium (I)owl:sameAsdrug:EXPT02771
drug:(1,10 Phenanthroline)-(Tri-Carbon Monoxide) Rhenium (I)rdf:typedrugbank:drugs
drug:(1-HYDROXY-1-PHOSPHONO-2-[1,1';3',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACIDdrugbank:description" experimental This compound belongs to the m-terphenyls. These are terphenyls whose structure contains the 1,3-diphenylbenzene skeleton. m-Terphenyls Organic Compounds Benzenoids Benzene and Substituted Derivatives Terphenyls Biphenyls and Derivatives Organic Phosphonic Acids Polyamines biphenyl phosphonic acid derivative phosphonic acid polyamine logP 1.82 ALOGPS logS -3.6 ALOGPS Water Solubility 1.17e-01 g/l ALOGPS logP 2.75 ChemAxon IUPAC Name {1-hydroxy-2-[3-(3-phenylphenyl)phenyl]-1-phosphonoethyl}phosphonic acid ChemAxon Traditional IUPAC Name 1-hydroxy-2-[3-(3-phenylphenyl)phenyl]-1-phosphonoethylphosphonic acid ChemAxon Molecular Weight 434.3161 ChemAxon Monoisotopic Weight 434.068426018 ChemAxon SMILES OC(CC1=CC=CC(=C1)C1=CC(=CC=C1)C1=CC=CC=C1)(P(O)(O)=O)P(O)(O)=O ChemAxon Molecular Formula C20H20O7P2 ChemAxon InChI InChI=1S/C20H20O7P2/c21-20(28(22,23)24,29(25,26)27)14-15-6-4-9-17(12-15)19-11-5-10-18(13-19)16-7-2-1-3-8-16/h1-13,21H,14H2,(H2,22,23,24)(H2,25,26,27) ChemAxon InChIKey InChIKey=YXQQNSYZOQHKHD-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 135.29 ChemAxon Refractivity 109.55 ChemAxon Polarizability 41.4 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 0.69 ChemAxon pKa (strongest basic) -5.2 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 16086422 PubChem Substance 99443875 ChemSpider 17245076 PDB B08 BE0003350 Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) Involved in transferase activity Generates undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide uppS None 6.96 28444.0 Escherichia coli (strain K12) GenBank Gene Database U00096 UniProtKB P60472 UniProt Accession UPPS_ECOLI Di-trans,poly-cis-decaprenylcistransferase EC 2.5.1.31 UDS Undecaprenyl diphosphate synthase UPP synthetase >Undecaprenyl pyrophosphate synthetase MMLSATQPLSEKLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANN GIEALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDTSRFNSRL QERIRKSEALTAGNTGLTLNIAANYGGRWDIVQGVRQLAEKVQQGNLQPDQIDEEMLNQH VCMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALNAFANRE RRFGGTEPGDETA >762 bp GTGATGTTGTCTGCTACTCAACCACTTAGCGAAAAATTGCCAGCGCATGGCTGCCGTCAT GTTGCGATCATTATGGACGGCAATGGCCGCTGGGCAAAAAAGCAAGGGAAGATTCGTGCC TTTGGGCATAAAGCCGGGGCAAAATCCGTCCGCCGGGCTGTCTCTTTTGCGGCCAACAAC GGTATTGAGGCGTTAACGCTGTATGCCTTTAGTAGTGAAAACTGGAACCGACCAGCGCAG GAAGTCAGTGCGTTAATGGAACTGTTTGTGTGGGCGCTCGATAGCGAAGTAAAAAGTCTG CACCGACATAACGTGCGTCTGCGTATTATTGGCGATACCAGTCGCTTTAACTCGCGTTTG CAAGAACGTATTCGTAAATCTGAAGCGCTAACAGCCGGGAATACCGGTCTGACGCTGAAT ATTGCGGCGAACTACGGTGGACGTTGGGATATAGTCCAGGGAGTCAGGCAACTGGCTGAA AAGGTGCAGCAAGGAAACCTGCAACCAGATCAGATAGATGAAGAGATGCTAAACCAGCAT GTCTGTATGCATGAACTGGCCCCTGTAGATTTAGTAATTAGGACTGGGGGGGAGCATCGC ATTAGTAACTTTTTGCTTTGGCAAATTGCCTATGCCGAACTTTACTTTACAGATGTTCTC TGGCCCGATTTCGATGAACAAGACTTTGAAGGGGCGTTAAATGCCTTTGCTAATCGAGAG CGTCGTTTCGGCGGCACCGAGCCCGGTGATGAAACAGCCTGA PF01255 Prenyltransf function transferase activity function catalytic activity process metabolism process physiological process "
drug:(1-HYDROXY-1-PHOSPHONO-2-[1,1';3',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACIDrdfs:label"(1-HYDROXY-1-PHOSPHONO-2-[1,1';3',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACID"
drug:(1-HYDROXY-1-PHOSPHONO-2-[1,1';3',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACIDrdf:typedrugbank:drugs
drug:(1-HYDROXY-1-PHOSPHONO-2-[1,1';4',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACIDdrugbank:description" experimental This compound belongs to the p-terphenyls. These are terphenyls whose structure contains the 1,4-diphenylbenzene skeleton. p-Terphenyls Organic Compounds Benzenoids Benzene and Substituted Derivatives Terphenyls Biphenyls and Derivatives Organic Phosphonic Acids Polyamines biphenyl phosphonic acid derivative phosphonic acid polyamine logP 1.84 ALOGPS logS -3.6 ALOGPS Water Solubility 1.04e-01 g/l ALOGPS logP 2.75 ChemAxon IUPAC Name {1-hydroxy-2-[3-(4-phenylphenyl)phenyl]-1-phosphonoethyl}phosphonic acid ChemAxon Traditional IUPAC Name 1-hydroxy-2-[3-(4-phenylphenyl)phenyl]-1-phosphonoethylphosphonic acid ChemAxon Molecular Weight 434.3161 ChemAxon Monoisotopic Weight 434.068426018 ChemAxon SMILES OC(CC1=CC=CC(=C1)C1=CC=C(C=C1)C1=CC=CC=C1)(P(O)(O)=O)P(O)(O)=O ChemAxon Molecular Formula C20H20O7P2 ChemAxon InChI InChI=1S/C20H20O7P2/c21-20(28(22,23)24,29(25,26)27)14-15-5-4-8-19(13-15)18-11-9-17(10-12-18)16-6-2-1-3-7-16/h1-13,21H,14H2,(H2,22,23,24)(H2,25,26,27) ChemAxon InChIKey InChIKey=MPBUFKZCEBTBSK-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 135.29 ChemAxon Refractivity 109.55 ChemAxon Polarizability 41.53 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 0.69 ChemAxon pKa (strongest basic) -5.2 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 16122554 PubChem Substance 99443880 ChemSpider 17279473 PDB B28 BE0003350 Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) Involved in transferase activity Generates undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide uppS None 6.96 28444.0 Escherichia coli (strain K12) GenBank Gene Database U00096 UniProtKB P60472 UniProt Accession UPPS_ECOLI Di-trans,poly-cis-decaprenylcistransferase EC 2.5.1.31 UDS Undecaprenyl diphosphate synthase UPP synthetase >Undecaprenyl pyrophosphate synthetase MMLSATQPLSEKLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANN GIEALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDTSRFNSRL QERIRKSEALTAGNTGLTLNIAANYGGRWDIVQGVRQLAEKVQQGNLQPDQIDEEMLNQH VCMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALNAFANRE RRFGGTEPGDETA >762 bp GTGATGTTGTCTGCTACTCAACCACTTAGCGAAAAATTGCCAGCGCATGGCTGCCGTCAT GTTGCGATCATTATGGACGGCAATGGCCGCTGGGCAAAAAAGCAAGGGAAGATTCGTGCC TTTGGGCATAAAGCCGGGGCAAAATCCGTCCGCCGGGCTGTCTCTTTTGCGGCCAACAAC GGTATTGAGGCGTTAACGCTGTATGCCTTTAGTAGTGAAAACTGGAACCGACCAGCGCAG GAAGTCAGTGCGTTAATGGAACTGTTTGTGTGGGCGCTCGATAGCGAAGTAAAAAGTCTG CACCGACATAACGTGCGTCTGCGTATTATTGGCGATACCAGTCGCTTTAACTCGCGTTTG CAAGAACGTATTCGTAAATCTGAAGCGCTAACAGCCGGGAATACCGGTCTGACGCTGAAT ATTGCGGCGAACTACGGTGGACGTTGGGATATAGTCCAGGGAGTCAGGCAACTGGCTGAA AAGGTGCAGCAAGGAAACCTGCAACCAGATCAGATAGATGAAGAGATGCTAAACCAGCAT GTCTGTATGCATGAACTGGCCCCTGTAGATTTAGTAATTAGGACTGGGGGGGAGCATCGC ATTAGTAACTTTTTGCTTTGGCAAATTGCCTATGCCGAACTTTACTTTACAGATGTTCTC TGGCCCGATTTCGATGAACAAGACTTTGAAGGGGCGTTAAATGCCTTTGCTAATCGAGAG CGTCGTTTCGGCGGCACCGAGCCCGGTGATGAAACAGCCTGA PF01255 Prenyltransf function transferase activity function catalytic activity process metabolism process physiological process "
drug:(1-HYDROXY-1-PHOSPHONO-2-[1,1';4',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACIDrdfs:label"(1-HYDROXY-1-PHOSPHONO-2-[1,1';4',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACID"
drug:(1-HYDROXY-1-PHOSPHONO-2-[1,1';4',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACIDrdf:typedrugbank:drugs
drug:(1-HYDROXYDODECANE-1,1-DIYL)BIS(PHOSPHONIC ACID)drugbank:description" experimental This compound belongs to the organic phosphonic acids. These are organic compounds containing phosphonic acid. Organic Phosphonic Acids Organic Compounds Organophosphorus Compounds Organic Phosphonic Acids and Derivatives Organic Phosphonic Acids Polyamines polyamine logP 1.57 ALOGPS logS -2 ALOGPS Water Solubility 3.11e+00 g/l ALOGPS logP 2.07 ChemAxon IUPAC Name (1-hydroxy-1-phosphonododecyl)phosphonic acid ChemAxon Traditional IUPAC Name 1-hydroxy-1-phosphonododecylphosphonic acid ChemAxon Molecular Weight 346.294 ChemAxon Monoisotopic Weight 346.131026274 ChemAxon SMILES CCCCCCCCCCCC(O)(P(O)(O)=O)P(O)(O)=O ChemAxon Molecular Formula C12H28O7P2 ChemAxon InChI InChI=1S/C12H28O7P2/c1-2-3-4-5-6-7-8-9-10-11-12(13,20(14,15)16)21(17,18)19/h13H,2-11H2,1H3,(H2,14,15,16)(H2,17,18,19) ChemAxon InChIKey InChIKey=KKVZONPEMODBBG-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 135.29 ChemAxon Refractivity 80.6 ChemAxon Polarizability 34.83 ChemAxon Rotatable Bond Count 12 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 0.69 ChemAxon pKa (strongest basic) -5.2 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 4395717 PubChem Substance 99444344 ChemSpider 3597115 PDB H23 BE0003570 Geranylgeranyl pyrophosphate synthase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Geranylgeranyl pyrophosphate synthase Coenzyme transport and metabolism Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins GGPS1 1q43 Cytoplasm None 6.06 34870.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:4249 GeneCards GGPS1 GenBank Gene Database AB017971 GenBank Protein Database 4520350 UniProtKB O95749 UniProt Accession GGPPS_HUMAN Dimethylallyltranstransferase Farnesyltranstransferase Geranylgeranyl diphosphate synthase Geranyltranstransferase GGPP synthetase GGPPSase >Geranylgeranyl pyrophosphate synthetase MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNAS LLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLL ELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTL GLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN IDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE PF00348 polyprenyl_synt process primary metabolism process lipid metabolism process cellular lipid metabolism process isoprenoid metabolism process isoprenoid biosynthesis process physiological process process metabolism "
drug:(1-HYDROXYDODECANE-1,1-DIYL)BIS(PHOSPHONIC ACID)rdfs:label"(1-HYDROXYDODECANE-1,1-DIYL)BIS(PHOSPHONIC ACID)"
drug:(1-HYDROXYDODECANE-1,1-DIYL)BIS(PHOSPHONIC ACID)rdf:typedrugbank:drugs
drug:(1-HYDROXYHEPTANE-1,1-DIYL)BIS(PHOSPHONIC ACID)drugbank:description" experimental This compound belongs to the organic phosphonic acids. These are organic compounds containing phosphonic acid. Organic Phosphonic Acids Organic Compounds Organophosphorus Compounds Organic Phosphonic Acids and Derivatives Organic Phosphonic Acids Polyamines polyamine logP 0.15 ALOGPS logS -1.4 ALOGPS Water Solubility 1.10e+01 g/l ALOGPS logP -0.035 ChemAxon IUPAC Name (1-hydroxy-1-phosphonoheptyl)phosphonic acid ChemAxon Traditional IUPAC Name 1-hydroxy-1-phosphonoheptylphosphonic acid ChemAxon Molecular Weight 276.1611 ChemAxon Monoisotopic Weight 276.052775954 ChemAxon SMILES CCCCCCC(O)(P(O)(O)=O)P(O)(O)=O ChemAxon Molecular Formula C7H18O7P2 ChemAxon InChI InChI=1S/C7H18O7P2/c1-2-3-4-5-6-7(8,15(9,10)11)16(12,13)14/h8H,2-6H2,1H3,(H2,9,10,11)(H2,12,13,14) ChemAxon InChIKey InChIKey=IJEGNOYPWRBKAE-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 135.29 ChemAxon Refractivity 57.59 ChemAxon Polarizability 23.73 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 0.69 ChemAxon pKa (strongest basic) -5.2 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5276520 PubChem Substance 99443301 ChemSpider 4440481 PDB 028 BE0003570 Geranylgeranyl pyrophosphate synthase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Geranylgeranyl pyrophosphate synthase Coenzyme transport and metabolism Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins GGPS1 1q43 Cytoplasm None 6.06 34870.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:4249 GeneCards GGPS1 GenBank Gene Database AB017971 GenBank Protein Database 4520350 UniProtKB O95749 UniProt Accession GGPPS_HUMAN Dimethylallyltranstransferase Farnesyltranstransferase Geranylgeranyl diphosphate synthase Geranyltranstransferase GGPP synthetase GGPPSase >Geranylgeranyl pyrophosphate synthetase MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNAS LLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLL ELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTL GLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN IDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE PF00348 polyprenyl_synt process primary metabolism process lipid metabolism process cellular lipid metabolism process isoprenoid metabolism process isoprenoid biosynthesis process physiological process process metabolism "
drug:(1-HYDROXYHEPTANE-1,1-DIYL)BIS(PHOSPHONIC ACID)rdfs:label"(1-HYDROXYHEPTANE-1,1-DIYL)BIS(PHOSPHONIC ACID)"
drug:(1-HYDROXYHEPTANE-1,1-DIYL)BIS(PHOSPHONIC ACID)rdf:typedrugbank:drugs
drug:(1-HYDROXYNONANE-1,1-DIYL)BIS(PHOSPHONIC ACID)drugbank:description" experimental This compound belongs to the organic phosphonic acids. These are organic compounds containing phosphonic acid. Organic Phosphonic Acids Organic Compounds Organophosphorus Compounds Organic Phosphonic Acids and Derivatives Organic Phosphonic Acids Polyamines polyamine logP 0.7 ALOGPS logS -1.6 ALOGPS Water Solubility 8.20e+00 g/l ALOGPS logP 0.81 ChemAxon IUPAC Name (1-hydroxy-1-phosphonononyl)phosphonic acid ChemAxon Traditional IUPAC Name 1-hydroxy-1-phosphonononylphosphonic acid ChemAxon Molecular Weight 304.2143 ChemAxon Monoisotopic Weight 304.084076082 ChemAxon SMILES CCCCCCCCC(O)(P(O)(O)=O)P(O)(O)=O ChemAxon Molecular Formula C9H22O7P2 ChemAxon InChI InChI=1S/C9H22O7P2/c1-2-3-4-5-6-7-8-9(10,17(11,12)13)18(14,15)16/h10H,2-8H2,1H3,(H2,11,12,13)(H2,14,15,16) ChemAxon InChIKey InChIKey=COHUUYPEYRMWTH-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 135.29 ChemAxon Refractivity 66.79 ChemAxon Polarizability 27.94 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 0.69 ChemAxon pKa (strongest basic) -5.2 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5276507 PubChem Substance 99443402 ChemSpider 4440469 PDB 252 BE0003570 Geranylgeranyl pyrophosphate synthase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Geranylgeranyl pyrophosphate synthase Coenzyme transport and metabolism Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins GGPS1 1q43 Cytoplasm None 6.06 34870.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:4249 GeneCards GGPS1 GenBank Gene Database AB017971 GenBank Protein Database 4520350 UniProtKB O95749 UniProt Accession GGPPS_HUMAN Dimethylallyltranstransferase Farnesyltranstransferase Geranylgeranyl diphosphate synthase Geranyltranstransferase GGPP synthetase GGPPSase >Geranylgeranyl pyrophosphate synthetase MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNAS LLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLL ELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTL GLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN IDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE PF00348 polyprenyl_synt process primary metabolism process lipid metabolism process cellular lipid metabolism process isoprenoid metabolism process isoprenoid biosynthesis process physiological process process metabolism "
drug:(1-HYDROXYNONANE-1,1-DIYL)BIS(PHOSPHONIC ACID)rdfs:label"(1-HYDROXYNONANE-1,1-DIYL)BIS(PHOSPHONIC ACID)"
drug:(1-HYDROXYNONANE-1,1-DIYL)BIS(PHOSPHONIC ACID)rdf:typedrugbank:drugs
drug:(1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanonedrugbank:description" experimental This compound belongs to the benzofurans. These are organic compounds containing a benzene ring fused to a furan. Benzofurans Organic Compounds Heterocyclic Compounds Benzofurans Phenol Ethers Alkyl Aryl Ethers Pyridines and Derivatives N-substituted Imidazoles Furans Ketones Enolates Dialkylamines Polyamines phenol ether alkyl aryl ether benzene pyridine n-substituted imidazole azole imidazole furan ketone secondary amine polyamine secondary aliphatic amine enolate ether amine carbonyl group organonitrogen compound Dietary Supplements Micronutrients Supplements logP 2.83 ALOGPS logS -4 ALOGPS Water Solubility 4.25e-02 g/l ALOGPS logP 2.55 ChemAxon IUPAC Name [3-({3-methyl-2-[(1-methyl-1H-imidazol-2-yl)carbonyl]-1-benzofuran-4-yl}oxy)propyl](pyridin-3-ylmethyl)amine ChemAxon Traditional IUPAC Name [3-({3-methyl-2-[(1-methylimidazol-2-yl)carbonyl]-1-benzofuran-4-yl}oxy)propyl](pyridin-3-ylmethyl)amine ChemAxon Molecular Weight 404.4617 ChemAxon Monoisotopic Weight 404.184840654 ChemAxon SMILES CN1C=CN=C1C(=O)C1=C(C)C2=C(O1)C=CC=C2OCCCNCC1=CN=CC=C1 ChemAxon Molecular Formula C23H24N4O3 ChemAxon InChI InChI=1S/C23H24N4O3/c1-16-20-18(29-13-5-10-25-15-17-6-4-9-24-14-17)7-3-8-19(20)30-22(16)21(28)23-26-11-12-27(23)2/h3-4,6-9,11-12,14,25H,5,10,13,15H2,1-2H3 ChemAxon InChIKey InChIKey=VZBQJKIOAOUYJL-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 82.18 ChemAxon Refractivity 114.23 ChemAxon Polarizability 44.88 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 8.99 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 446386 PubChem Substance 46505140 ChemSpider 393760 PDB R64 BE0001502 Glycylpeptide N-tetradecanoyltransferase Yeast # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Glycylpeptide N-tetradecanoyltransferase Involved in glycylpeptide N-tetradecanoyltransferase activity Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N- terminal glycine in the nascent polypeptide substrates. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6. Basic residues are preferred at positions 7 and 8 NMT1 Cytoplasm None 6.44 51878.0 Yeast GenBank Gene Database M80544 GenBank Protein Database 170884 UniProtKB P30418 UniProt Accession NMT_CANAL EC 2.3.1.97 Myristoyl-CoA:protein N-myristoyltransferase NMT Peptide N- myristoyltransferase >Glycylpeptide N-tetradecanoyltransferase MSGDNTGNKSNSAPSKSIEELLKLLAMGQELSPAQQKEMKDYKFWKTQPVPSLSETVTEE GPIDKLKTPEDVPNDPLPLISDFEWSTLDIDDNLQLDELYKLLYDNYVEDIDATFRFKYS HEFFQWALKPPGWRKDWHVGVRVKSTGKLVAFIAATPVTFKLNKSNKVIDSVEINFLCIH KKLRNKRLAPVLIKEITRRVNKQNIWQALYTGGSILPTPLTTCRYQHRPINWSKLHDVGF SHLPPNQTKSSMVASYTLPNNPKLKGLRPMTGKDVSTVLSLLYKYQERFDIVQLFTEEEF KHWMLGHDENSDSNVVKSYVVEDENGIITDYFSYYLLPFTVLDNAQHDELGIAYLFYYAS DSFEKPNYKKRLNELITDALITSKKFGVDVFNCLTCQDNTYFLKDCKFGSGDGFLNYYLF NYRTFPMDGGIDKKTKEVVEDQTSGIGVVLL >1356 bp ATGTCGGGAGATAACACAGGGAATAAATCCAATTCAGCACCTTCAAAATCAATTGAAGAA TTGTTGAAATTATTGGCTATGGGACAAGAATTATCCCCGGCTCAACAAAAGGAAATGAAA GATTATAAATTTTGGAAGACTCAACCTGTACCATCATTAAGTGAAACCGTCACTGAAGAA GGTCCTATTGATAAATTGAAAACTCCAGAAGATGTTCCTAATGATCCATTACCATTGATC AGTGATTTTGAATGGAGTACTTTAGATATTGACGATAATTTACAATTGGATGAATTATAT AAATTATTATATGATAATTATGTTGAAGATATTGATGCCACATTTAGATTCAAATATAGT CATGAATTTTTCCAATGGGCTTTGAAACCACCGGGATGGAGAAAAGATTGGCATGTTGGG GTTAGAGTGAAATCAACTGGGAAATTAGTAGCTTTTATAGCTGCTACTCCGGTCACTTTT AAATTAAATAAATCAAATAAAGTGATTGATTCAGTGGAAATCAACTTTTTATGTATTCAT AAAAAATTAAGAAATAAGAGATTAGCCCCTGTATTAATCAAAGAAATCACTCGTAGGGTT AATAAACAAAACATTTGGCAAGCATTATATACTGGTGGATCGATTTTACCTACACCATTG ACAACTTGTCGTTATCAACATCGCCCAATCAATTGGTCGAAATTGCATGATGTGGGGTTC AGTCATTTACCTCCAAATCAAACGAAAAGCAGCATGGTGGCAAGTTATACATTACCTAAT AATCCTAAATTGAAAGGTTTACGTCCAATGACTGGGAAAGATGTTTCCACCGTATTATCT TTATTGTATAAATATCAAGAACGATTTGATATTGTACAACTTTTCACCGAAGAAGAATTT AAACATTGGATGTTGGGTCATGATGAAAATTCAGATTCTAATGTGGTTAAAAGTTATGTA GTTGAAGATGAAAATGGGATTATTACCGATTATTTTTCATATTATTTGTTACCATTCACA GTATTAGACAATGCTCAACATGATGAATTAGGAATTGCTTATTTGTTTTATTATGCCAGT GATTCCTTTGAAAAACCAAATTATAAAAAGAGATTAAATGAATTAATCACTGATGCATTA ATTACCAGTAAAAAATTTGGAGTTGATGTTTTCAATTGTTTAACTTGTCAAGATAATACT TATTTCTTAAAAGATTGTAAATTTGGTAGTGGTGATGGTTTTTTAAATTATTATCTTTTT AATTATAGAACATTCCCTATGGATGGAGGAATTGATAAAAAGACAAAAGAAGTTGTCGAA GATCAAACAAGTGGTATAGGTGTAGTTTTATTATAA PF01233 NMT PF02799 NMT_C function transferase activity function transferase activity, transferring acyl groups function transferase activity, transferring groups other than amino-acyl groups function acyltransferase activity function N-acyltransferase activity function catalytic activity function glycylpeptide N-tetradecanoyltransferase activity process biopolymer modification process N-terminal protein myristoylation process protein modification process physiological process process metabolism process protein amino acid lipidation process macromolecule metabolism process protein myristoylation process biopolymer metabolism process protein amino acid myristoylation BE0004329 Glycylpeptide N-tetradecanoyltransferase 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Glycylpeptide N-tetradecanoyltransferase 1 Involved in glycylpeptide N-tetradecanoyltransferase ac Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins NMT1 17q21.31 Cytoplasm None 7.91 56805.9 Human HUGO Gene Nomenclature Committee (HGNC) GNC:7857 GeneCards NMT1 GenBank Gene Database AF043324 GenBank Protein Database 3005063 UniProtKB P30419 UniProt Accession NMT1_HUMAN Myristoyl-CoA:protein N-myristoyltransferase 1 NMT 1 Peptide N-myristoyltransferase 1 Type I N-myristoyltransferase >Glycylpeptide N-tetradecanoyltransferase 1 MADESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKK QKKKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFW DTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENY VEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEK KMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRS LNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQF HLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAY SFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYN WKCPSMGAEKVGLVLQ >1491 bp ATGGCGGACGAGAGTGAGACAGCAGTGAAGCCGCCGGCACCTCCGCTGCCGCAGATGATG GAAGGGAACGGGAACGGCCATGAGCACTGCAGCGATTGCGAGAATGAGGAGGACAACAGC TACAACCGGGGTGGTTTGAGTCCAGCCAATGACACTGGAGCCAAAAAGAAGAAAAAGAAA CAAAAAAAGAAGAAAGAAAAAGGCAGTGAGACAGATTCAGCCCAGGATCAGCCTGTGAAG ATGAACTCTTTGCCAGCAGAGAGGATCCAGGAAATACAGAAGGCCATTGAGCTGTTCTCA GTGGGTCAGGGACCTGCCAAAACCATGGAGGAGGCTAGCAAGCGAAGCTACCAGTTCTGG GATACGCAGCCCGTCCCCAAGCTGGGCGAAGTGGTGAACACCCATGGCCCCGTGGAGCCT GACAAGGACAATATCCGCCAGGAGCCCTACACCCTGCCCCAGGGCTTCACCTGGGATGCT TTGGACTTGGGCGATCGTGGTGTGCTAAAAGAACTGTACACCCTCCTGAATGAGAACTAT GTGGAAGATGATGACAACATGTTCCGATTTGATTATTCCCCGGAGTTTCTTTTGTGGGCT CTCCGGCCACCCGGCTGGCTCCCCCAGTGGCACTGTGGGGTTCGAGTGGTCTCAAGTCGG AAATTGGTTGGGTTCATTAGCGCCATCCCAGCAAACATCCATATCTATGACACAGAGAAG AAGATGGTAGAGATCAACTTCCTGTGTGTCCACAAGAAGCTGCGTTCCAAGAGGGTTGCT CCAGTTCTGATCCGAGAGATCACCAGGCGGGTTCACCTGGAGGGCATCTTCCAAGCAGTT TACACTGCCGGGGTGGTACTACCAAAGCCCGTTGGCACCTGCAGGTATTGGCATCGGTCC CTAAACCCACGGAAGCTGATTGAAGTGAAGTTCTCCCACCTGAGCAGAAATATGACCATG CAGCGCACCATGAAGCTCTACCGACTGCCAGAGACTCCCAAGACAGCTGGGCTGCGACCA ATGGAAACAAAGGACATTCCAGTAGTGCACCAGCTCCTCACCAGGTACTTGAAGCAATTT CACCTTACGCCCGTCATGAGCCAGGAGGAGGTGGAGCACTGGTTCTACCCCCAGGAGAAT ATCATCGACACTTTCGTGGTGGAGAACGCAAACGGAGAGGTGACAGATTTCCTGAGCTTT TATACGCTGCCCTCCACCATCATGAACCATCCAACCCACAAGAGTCTCAAAGCTGCTTAT TCTTTCTACAACGTTCACACCCAGACCCCTCTTCTAGACCTCATGAGCGACGCCCTTGTC CTCGCCAAAATGAAAGGGTTTGATGTGTTCAATGCACTGGATCTCATGGAGAACAAAACC TTCCTGGAGAAGCTCAAGTTTGGCATAGGGGACGGCAACCTGCAGTATTACCTTTACAAT TGGAAATGCCCCAGCATGGGGGCAGAGAAGGTTGGACTGGTGCTACAATAA PF01233 NMT PF02799 NMT_C function transferase activity function transferase activity, transferring acyl groups function transferase activity, transferring groups other than amino-acyl groups function acyltransferase activity function N-acyltransferase activity function catalytic activity function glycylpeptide N-tetradecanoyltransferase activity process protein modification process physiological process process metabolism process protein amino acid lipidation process macromolecule metabolism process protein myristoylation process biopolymer metabolism process protein amino acid myristoylation process biopolymer modification process N-terminal protein myristoylation "
drug:(1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanonedrugbank:drugCategorydrugcategory:Dietary Supplements
drug:(1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanonedrugbank:drugCategorydrugcategory:Micronutrients
drug:(1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanonedrugbank:drugCategorydrugcategory:Supplements
drug:(1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanonerdfs:label"(1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanone"
drug:(1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanoneowl:sameAsdrug:EXPT02748
drug:(1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanonerdf:typedrugbank:drugs
drug:(1-Tert-Butyl-5-Hydroxy-1h-Pyrazol-4-Yl)-(6-Methanesulfonyl-4'-Methoxy-2-Methyl-Biphenyl-3-Yl)-Methanonedrugbank:description" experimental This compound belongs to the biphenyls and derivatives. These are organic compounds containing to benzene rings linked together by a C-C bond. Biphenyls and Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Biphenyls and Derivatives Acetophenones Anisoles Benzoyl Derivatives Toluenes Alkyl Aryl Ethers Pyrazoles Ketones Polyamines Enolates acetophenone phenol ether anisole benzoyl toluene alkyl aryl ether pyrazole azole ketone polyamine enolate ether amine carbonyl group organonitrogen compound logP 4.06 ALOGPS logS -5 ALOGPS Water Solubility 4.36e-03 g/l ALOGPS logP 4.21 ChemAxon IUPAC Name {4-[(1-tert-butyl-5-hydroxy-1H-pyrazol-4-yl)carbonyl]-2-(4-methoxyphenyl)-3-methylphenyl}(methyl)-$l^{4}-sulfanediol ChemAxon Traditional IUPAC Name {4-[(1-tert-butyl-5-hydroxypyrazol-4-yl)carbonyl]-2-(4-methoxyphenyl)-3-methylphenyl}(methyl)-$l^{4}-sulfanediol ChemAxon Molecular Weight 444.544 ChemAxon Monoisotopic Weight 444.171892706 ChemAxon SMILES COC1=CC=C(C=C1)C1=C(C)C(=CC=C1S(C)(O)O)C(=O)C1=C(O)N(N=C1)C(C)(C)C ChemAxon Molecular Formula C23H28N2O5S ChemAxon InChI InChI=1S/C23H28N2O5S/c1-14-17(21(26)18-13-24-25(22(18)27)23(2,3)4)11-12-19(31(6,28)29)20(14)15-7-9-16(30-5)10-8-15/h7-13,27-29H,1-6H3 ChemAxon InChIKey InChIKey=GXVKJVRSQXCDKX-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 104.81 ChemAxon Refractivity 133.46 ChemAxon Polarizability 48.38 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 5.9 ChemAxon pKa (strongest basic) 1.24 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 5287556 PubChem Substance 46508138 PDB 869 BE0000455 4-hydroxyphenylpyruvate dioxygenase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown 4-hydroxyphenylpyruvate dioxygenase Amino acid transport and metabolism HPD 12q24-qter None 7.01 44804.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:5147 GenAtlas HPD GeneCards HPD GenBank Gene Database U29895 GenBank Protein Database 3860238 UniProtKB P32754 UniProt Accession HPPD_HUMAN 4-hydroxyphenylpyruvic acid oxidase 4HPPD EC 1.13.11.27 HPD HPPDase >4-hydroxyphenylpyruvate dioxygenase TTYSDKGAKPERGRFLHFHSVTFWVGNAKQAASFYCSKMGFEPLAYRGLETGSREVVSHV IKQGKIVFVLSSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCDYIVQKARERGAKIMREP WVEQDKFGKVKFAVLQTYGDTTHTLVEKMNYIGQFLPGYEAPAFMDPLLPKLPKCSLEMI DHIVGNQPDQEMVSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPIN EPAPGKKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRHLRERGLEFLSVPSTYYKQLRE KLKTAKIKVKENIDALEELKILVDYDEKGYLLQIFTKPVQDRPTLFLEVIQRHNHQGFGA GNFNSLFKAFEEEQNLRGNLTNMETNGVVPGM >1182 bp ATGACGACTTACAGTGACAAAGGGGCAAAGCCTGAGAGAGGCCGATTCCTCCACTTCCAC TCTGTGACCTTCTGGGTTGGCAACGCCAAGCAGGCCGCGTCATTCTACTGCAGCAAGATG GGCTTTGAACCTCTAGCCTACAGGGGCCTGGAGACCGGTTCCCGGGAGGTGGTCAGCCAT GTAATCAAACAAGGGAAGATTGTGTTTGTCCTCTCCTCAGCGCTCAACCCCTGGAACAAA GAGATGGGCGATCACCTGGTGAAACACGGTGACGGAGTGAAGGACATTGCGTTCGAGGTG GAAGATTGTGACTACATCGTGCAGAAAGCACGGGAACGGGGCGCCAAAATCATGCGGGAG CCCTGGGTAGAGCAAGACAAGTTTGGGAAGGTGAAGTTTGCTGTGCTGCAGACGTATGGG GACACCACACACACCCTGGTGGAGAAGATGAACTACATCGGCCAATTCTTGCCTGGATAT GAGCCCCCAGCGTTCATGGACCCCCTACTTCCTAAACTGCCCAAATGCAGTCTGGAGATG ATCGACCACATTGTGGGAAACCAGCCTGATCAGGAGATGGTGTCCGCCTCCGAATGGTAC CTGAAAAACCTGCAGTTCCACCGCTTCTGGTCCGTGGATGACACGCAGGTGCACACGGAA TATAGCTCTCTGCGATCCATTGTGGTGGCCAACTATGAAGAGTCCATCAAGATGCCCATC AATGAGCCAGCGCCTGGCAAGAAGAAGTCCCAGATCCAGGAATATGTGGACTATAACGGG GGCGCTGGGGTCCAGCACATCGCTCTCAAGACCGAAGACATCATCACAGCGATTCGCCAC TTGAGAGAGAGAGGCCTGGAGTTCTTATCTGTTCCCTCCACGTACTACAAACAACTGCGG GAGAAGCTGAAGACGGCCAAGATCAAGGTGAAGGAGAACATTGATGCCCTGGAGGAGCTG AAAATCCTGGTGGACTACGACGAGAAAGGCTACCTCCTGCAGATCTTCACCAAACCGGTG CAGGACCGGCCCACGCTCTTCCTGGAAGTCATCCAGCGCCACAACCACCAGGGTTTTGGA GCCGGCAACTTCAACTCACTGTTCAAGGCTTTCGAGGAGGAGCAGAACCTGCGGGGTAAC CTCACCAACATGGAGACCAATGGGGTGGTGCCCGGCATGTAA PF00903 Glyoxalase function oxidoreductase activity function oxidoreductase activity, acting on single donors with incorporation of molecular oxygen function oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen function 4-hydroxyphenylpyruvate dioxygenase activity function catalytic activity process amino acid and derivative metabolism process aromatic amino acid family metabolism process physiological process process metabolism process cellular metabolism process amino acid metabolism "
drug:(1-Tert-Butyl-5-Hydroxy-1h-Pyrazol-4-Yl)-(6-Methanesulfonyl-4'-Methoxy-2-Methyl-Biphenyl-3-Yl)-Methanonerdfs:label"(1-Tert-Butyl-5-Hydroxy-1h-Pyrazol-4-Yl)-(6-Methanesulfonyl-4'-Methoxy-2-Methyl-Biphenyl-3-Yl)-Methanone"
drug:(1-Tert-Butyl-5-Hydroxy-1h-Pyrazol-4-Yl)-(6-Methanesulfonyl-4'-Methoxy-2-Methyl-Biphenyl-3-Yl)-Methanoneowl:sameAsdrug:EXPT00327
drug:(1-Tert-Butyl-5-Hydroxy-1h-Pyrazol-4-Yl)-(6-Methanesulfonyl-4'-Methoxy-2-Methyl-Biphenyl-3-Yl)-Methanonerdf:typedrugbank:drugs
drug:(10ALPHA,13ALPHA,14BETA,17ALPHA)-17-HYDROXYANDROST-4-EN-3-ONEdrugbank:description" experimental This compound belongs to the androgens and derivatives. These are hydroxylated C19 steroid hormones. They are known to favour the development of masculine characteristics. They also show profound effects on scalp and body hair in humans. Androgens and Derivatives Organic Compounds Lipids Steroids and Steroid Derivatives Androgens and Derivatives Ketosteroids Hydroxysteroids Secondary Alcohols Ketones Cyclic Alcohols and Derivatives Polyamines cyclic alcohol ketone secondary alcohol polyamine alcohol carbonyl group logP 2.99 ALOGPS logS -3.9 ALOGPS Water Solubility 3.33e-02 g/l ALOGPS logP 3.37 ChemAxon IUPAC Name (1S,2R,10R,11S,14R,15S)-14-hydroxy-2,15-dimethyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadec-6-en-5-one ChemAxon Traditional IUPAC Name epitestosterone ChemAxon Molecular Weight 288.4244 ChemAxon Monoisotopic Weight 288.20893014 ChemAxon SMILES [H][C@@]1(O)CC[C@@]2([H])[C@]3([H])CCC4=CC(=O)CC[C@]4(C)[C@@]3([H])CC[C@]12C ChemAxon Molecular Formula C19H28O2 ChemAxon InChI InChI=1S/C19H28O2/c1-18-9-7-13(20)11-12(18)3-4-14-15-5-6-17(21)19(15,2)10-8-16(14)18/h11,14-17,21H,3-10H2,1-2H3/t14-,15-,16-,17+,18-,19-/m0/s1 ChemAxon InChIKey InChIKey=MUMGGOZAMZWBJJ-KZYORJDKSA-N ChemAxon Polar Surface Area (PSA) 37.3 ChemAxon Refractivity 84.43 ChemAxon Polarizability 33.8 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 19.09 ChemAxon pKa (strongest basic) -0.88 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 10204 PubChem Substance 99444239 ChemSpider 9789 PDB FFA BE0000126 Aldo-keto reductase family 1 member C1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aldo-keto reductase family 1 member C1 Involved in oxidoreductase activity Converts progesterone to its inactive form, 20alpha- dihydroxyprogesterone (20alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. May play a role in myelin formation AKR1C1 10p15-p14 Cytoplasm None 7.99 36789.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:384 GenAtlas AKR1C1 GeneCards AKR1C1 GenBank Gene Database M86609 GenBank Protein Database 181549 UniProtKB Q04828 UniProt Accession AK1C1_HUMAN 20-alpha- hydroxysteroid dehydrogenase 20-alpha-HSD Chlordecone reductase homolog HAKRC DD1/DD2 Dihydrodiol dehydrogenase 1/2 EC 1.1.1.- EC 1.1.1.149 EC 1.3.1.20 HBAB High- affinity hepatic bile acid-binding protein Trans- 1,2-dihydrobenzene-1,2-diol dehydrogenase >Aldo-keto reductase family 1 member C1 MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQ VGLAIRSKIADGSVKREDIFYTSKLWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV SVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKP GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN RNVRYLTLDIFAGPPNYPFSDEY >972 bp ATGGATTCGAAATATCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTTTAGAGGCCACCAAATTG GCAATTGAAGCTGGCTTCCGCCATATTGATTCTGCTCATTTATACAATAATGAGGAGCAG GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC TACACTTCAAAGCTTTGGTGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA AGGTCACTGAAAAATCTTCAATTGGATTATGTTGACCTCTACCTTATTCATTTTCCAGTG TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC ACAGTGGATCTCTGTGCCACGTGGGAGGCCGTGGAGAAGTGTAAAGATGCAGGATTGGCC AAGTCCATCGGGGTGTCCAACTTCAACCGCAGGCAGCTGGAGATGATCCTCAACAAGCCA GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA TCCCACCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG CTACAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT GATGAATATTAA PF00248 Aldo_ket_red function catalytic activity function oxidoreductase activity BE0000622 Aldo-keto reductase family 1 member C2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aldo-keto reductase family 1 member C2 Involved in oxidoreductase activity Works in concert with the 5alpha/5beta-steroid reductases to convert steroid hormones into the 3alpha/5alpha and 3alpha/5beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5alpha-DHT) to 5-alpha-androstane-3alpha,17beta-diol (3-alpha-diol) AKR1C2 10p15-p14 Cytoplasm (Potential) None 7.55 36736.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:385 GenAtlas AKR1C2 GeneCards AKR1C2 GenBank Gene Database U05598 GenBank Protein Database 531160 UniProtKB P52895 UniProt Accession AK1C2_HUMAN 3-alpha-HSD3 Chlordecone reductase homolog HAKRD DD/BABP DD2 Dihydrodiol dehydrogenase 2 Dihydrodiol dehydrogenase/bile acid-binding protein EC 1.-.-.- EC 1.1.1.213 EC 1.3.1.20 Trans-1,2- dihydrobenzene-1,2-diol dehydrogenase Type III 3- alpha-hydroxysteroid dehydrogenase >Aldo-keto reductase family 1 member C2 MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQ VGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV SVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKP GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN RNVRYLTLDIFAGPPNYPFSDEY >972 bp ATGGATTCGAAATACCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTCTAGAGGCCGTCAAATTG GCAATAGAAGCCGGGTTCCACCATATTGATTCTGCACATGTTTACAATAATGAGGAGCAG GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC TACACTTCAAAGCTTTGGAGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA AGGTCACTGAAAAATCTTCAATTGGACTATGTTGACCTCTATCTTATTCATTTTCCAGTG TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC ACAGTGGATCTCTGTGCCACGTGGGAGGCCATGGAGAAGTGTAAAGATGCAGGATTGGCC AAGTCCATCGGGGTGTCCAACTTCAACCACAGGCTGCTGGAGATGATCCTCAACAAGCCA GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA TCCCATCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT GATGAATATTAA PF00248 Aldo_ket_red function catalytic activity function oxidoreductase activity "
drug:(10ALPHA,13ALPHA,14BETA,17ALPHA)-17-HYDROXYANDROST-4-EN-3-ONErdfs:label"(10ALPHA,13ALPHA,14BETA,17ALPHA)-17-HYDROXYANDROST-4-EN-3-ONE"
drug:(10ALPHA,13ALPHA,14BETA,17ALPHA)-17-HYDROXYANDROST-4-EN-3-ONErdf:typedrugbank:drugs
drug:(10E,12Z)-octadeca-10,12-dienoic aciddrugbank:description" experimental This compound belongs to the lineolic acids and derivatives. These are derivatives of lineolic acid. Lineolic Acids and Derivatives Organic Compounds Lipids Lineolic Acids and Derivatives Unsaturated Fatty Acids Straight Chain Fatty Acids Polyamines Enolates Carboxylic Acids enolate polyamine carboxylic acid carboxylic acid derivative 10-TRANS-12-CIS-OCTADECADIENOIC ACID 10E,12Z-octadecadienoic acid 10E,Z12-CLA logP 7.1 ALOGPS logS -6.3 ALOGPS Water Solubility 1.49e-04 g/l ALOGPS logP 6.42 ChemAxon IUPAC Name (10E,12Z)-octadeca-10,12-dienoic acid ChemAxon Traditional IUPAC Name (10E,12Z)-octadeca-10,12-dienoic acid ChemAxon Molecular Weight 280.4455 ChemAxon Monoisotopic Weight 280.240230268 ChemAxon SMILES CCCCC\C=C/C=C/CCCCCCCCC(O)=O ChemAxon Molecular Formula C18H32O2 ChemAxon InChI InChI=1S/C18H32O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18(19)20/h6-9H,2-5,10-17H2,1H3,(H,19,20)/b7-6-,9-8+ ChemAxon InChIKey InChIKey=GKJZMAHZJGSBKD-NMMTYZSQSA-N ChemAxon Polar Surface Area (PSA) 37.3 ChemAxon Refractivity 88.52 ChemAxon Polarizability 36.57 ChemAxon Rotatable Bond Count 14 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 5.02 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 0 ChemAxon Bioavailability 0 ChemAxon ChEBI 44526 PubChem Compound 5282800 PubChem Substance 46507143 PDB ODD BE0003358 Putative aminooxidase Propionibacterium acnes (strain KPA171202 / DSM 16379) unknown Putative aminooxidase Involved in oxidoreductase activity PPA1039 None 4.81 49022.0 Propionibacterium acnes (strain KPA171202 / DSM 16379) GenBank Gene Database AE017283 UniProtKB Q6A8X5 UniProt Accession Q6A8X5_PROAC >Putative aminooxidase MSISKDSRIAIIGAGPAGLAAGMYLEQAGFHDYTILERTDHVGGKCHSPNYHGRRYEMGA IMGVPSYDTIQEIMDRTGDKVDGPKLRREFLHEDGEIYVPEKDPVRGPQVMAAVQKLGQL LATKYQGYDANGHYNKVHEDLMLPFDEFLALNGCEAARDLWINPFTAFGYGHFDNVPAAY VLKYLDFVTMMSFAKGDLWTWADGTQAMFEHLNATLEHPAERNVDITRITREDGKVHIHT TDWDRESDVLVLTVPLEKFLDYSDADDDEREYFSKIIHQQYMVDACLVKEYPTISGYVPD NMRPERLGHVMVYYHRWADDPHQIITTYLLRNHPDYADKTQEECRQMVLDDMETFGHPVE KIIEEQTWYYFPHVSSEDYKAGWYEKVEGMQGRRNTFYAGEIMSFGNFDEVCHYSKDLVT RFFV >1275 bp ATGTCCATCTCGAAGGATTCACGTATCGCCATCATCGGCGCTGGCCCGGCCGGGCTGGCT GCCGGAATGTACCTCGAACAGGCCGGATTTCACGACTACACGATCCTGGAACGCACCGAC CACGTCGGAGGCAAGTGCCACTCACCGAACTACCACGGCCGTCGTTATGAGATGGGGGCC ATCATGGGCGTCCCCAGTTACGACACCATCCAGGAGATCATGGATCGCACTGGCGACAAG GTCGACGGGCCGAAACTGCGTCGCGAGTTCCTGCACGAGGACGGCGAGATCTACGTCCCG GAAAAGGATCCAGTGCGTGGTCCGCAGGTCATGGCAGCAGTGCAGAAGCTGGGCCAGTTG CTCGCGACGAAGTACCAGGGATATGACGCCAACGGCCACTACAACAAGGTTCACGAGGAC CTCATGCTGCCCTTCGACGAGTTCCTCGCCCTCAACGGGTGCGAGGCCGCCCGAGACCTG TGGATCAACCCCTTCACGGCCTTCGGCTACGGGCACTTCGACAACGTCCCGGCCGCCTAC GTGCTGAAGTACCTCGACTTCGTCACCATGATGTCCTTTGCCAAGGGAGATCTGTGGACG TGGGCCGACGGCACCCAGGCGATGTTCGAGCACCTCAACGCCACCCTGGAGCACCCGGCC GAACGCAACGTTGACATCACTCGCATCACCCGCGAGGACGGCAAGGTCCACATCCACACC ACGGACTGGGATCGCGAGTCCGACGTCCTCGTCCTCACCGTCCCGCTGGAAAAGTTCCTC GACTACTCCGACGCGGACGATGACGAGCGGGAGTACTTCTCGAAGATCATCCACCAGCAG TACATGGTGGATGCCTGCCTGGTGAAGGAGTACCCGACCATCTCCGGGTACGTCCCCGAC AACATGAGGCCCGAACGTCTCGGGCACGTCATGGTTTACTACCACCGCTGGGCTGATGAT CCGCACCAGATCATCACGACCTACCTGCTACGTAACCATCCGGACTACGCGGACAAGACT CAGGAGGAGTGCCGCCAGATGGTCCTCGACGACATGGAGACCTTCGGTCATCCGGTCGAG AAGATCATCGAGGAGCAGACCTGGTACTACTTCCCGCACGTTAGCTCGGAGGACTACAAG GCCGGGTGGTACGAGAAGGTCGAGGGAATGCAGGGTCGTCGCAACACCTTCTACGCCGGA GAAATTATGAGTTTCGGTAATTTCGACGAGGTGTGCCACTACTCGAAGGACCTGGTGACG CGGTTCTTCGTGTGA PF01593 Amino_oxidase function oxidoreductase activity function catalytic activity process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process "
drug:(10E,12Z)-octadeca-10,12-dienoic acidrdfs:label"(10E,12Z)-octadeca-10,12-dienoic acid"
drug:(10E,12Z)-octadeca-10,12-dienoic acidrdf:typedrugbank:drugs
drug:(10R)-10-Formyl-5,8,10-Trideazafolic Aciddrugbank:description" experimental This compound belongs to the stilbenes. These are organic compounds containing a 1,2-diphenylethylene moiety. Stilbenes (C6-C2-C6 ) are derived from the common phenylpropene (C6-C3) skeleton building block. The introduction of one or more hydroxyl groups to a phenyl ring lead to stilbenoids. Stilbenes Organic Compounds Phenylpropanoids and Polyketides Stilbenes Hippuric Acid Derivatives N-acyl-alpha Amino Acids Quinazolinamines Phenylpropanoic Acids Bicyclic Monoterpenes Aromatic Monoterpenes Phenylacetic Acid Derivatives Tricarboxylic Acids and Derivatives Benzoyl Derivatives Amino Fatty Acids Primary Aromatic Amines Pyrimidines and Pyrimidine Derivatives Polyols Secondary Carboxylic Acid Amides Carboxylic Acids Enolates Polyamines 3-phenylpropanoic-acid quinazolinamine aromatic monoterpene quinazoline phenylacetate monoterpene bicyclic monoterpene p-cymene alpha-amino acid or derivative tricarboxylic acid derivative benzamide benzoyl primary aromatic amine benzene pyrimidine secondary carboxylic acid amide polyol carboxamide group enolate carboxylic acid derivative carboxylic acid polyamine organonitrogen compound primary amine amine logP 1.08 ALOGPS logS -3.8 ALOGPS Water Solubility 7.16e-02 g/l ALOGPS logP 1.72 ChemAxon IUPAC Name (2S)-2-({4-[(1R)-2-(2-amino-4-hydroxyquinazolin-6-yl)-1-carboxyethyl]phenyl}formamido)pentanedioic acid ChemAxon Traditional IUPAC Name (2S)-2-({4-[(1R)-2-(2-amino-4-hydroxyquinazolin-6-yl)-1-carboxyethyl]phenyl}formamido)pentanedioic acid ChemAxon Molecular Weight 482.4428 ChemAxon Monoisotopic Weight 482.1437637 ChemAxon SMILES NC1=NC(O)=C2C=C(C[C@@H](C(O)=O)C3=CC=C(C=C3)C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=CC2=N1 ChemAxon Molecular Formula C23H22N4O8 ChemAxon InChI InChI=1S/C23H22N4O8/c24-23-26-16-6-1-11(10-15(16)20(31)27-23)9-14(21(32)33)12-2-4-13(5-3-12)19(30)25-17(22(34)35)7-8-18(28)29/h1-6,10,14,17H,7-9H2,(H,25,30)(H,28,29)(H,32,33)(H,34,35)(H3,24,26,27,31)/t14-,17+/m1/s1 ChemAxon InChIKey InChIKey=DAOQLLQRJAXMGY-PBHICJAKSA-N ChemAxon Polar Surface Area (PSA) 213.03 ChemAxon Refractivity 121.66 ChemAxon Polarizability 47 ChemAxon Rotatable Bond Count 10 ChemAxon H Bond Acceptor Count 11 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) 3.11 ChemAxon pKa (strongest basic) 2.03 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 3 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PDB NHR BE0001476 Phosphoribosylglycinamide formyltransferase Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Phosphoribosylglycinamide formyltransferase Nucleotide transport and metabolism 10-formyltetrahydrofolate + 1-N-(5-phospho-D- ribosyl)glycinamide = tetrahydrofolate + 2-N-formyl-1-N-(5- phospho-D-ribosyl)glycinamide purN None 5.74 23239.0 Escherichia coli (strain K12) GenBank Gene Database M13747 GenBank Protein Database 147425 UniProtKB P08179 UniProt Accession PUR3_ECOLI 5'-phosphoribosylglycinamide transformylase EC 2.1.2.2 GAR transformylase GART >Phosphoribosylglycinamide formyltransferase MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAGIATHTLIASA FDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEDDITARVQTQEHAIYPLV ISWFADGRLKMHENAAWLDGQRLPPQGYAADE >639 bp ATGAATATTGTGGTGCTTATTTCCGGCAACGGAAGTAATTTACAGGCAATTATTGACGCC TGTAAAACCAACAAAATTAAAGGCACCGTACGGGCAGTTTTCAGCAATAAGGCCGACGCG TTCGGCCTTGAACGCGCCCGCCAGGCGGGTATTGCAACGCATACGCTCATCGCCAGCGCG TTTGACAGTCGTGAAGCCTATGACCGGGAGTTGATTCATGAAATCGACATGTACGCACCC GATGTGGTCGTGCTGGCTGGTTTTATGCGCATTCTCAGCCCGGCGTTTGTCTCCCACTAT GCCGGGCGTTTGCTGAACATTCACCCTTCTCTGCTGCCGAAATATCCCGGATTACACACC CATCGTCAGGCGCTGGAAAATGGCGATGAAGAGCACGGTACATCGGTGCATTTCGTCACC GATGAACTGGACGGTGGCCCGGTTATTTTACAGGCGAAAGTCCCGGTATTTGCTGGTGAT TCGGAAGATGACATCACCGCCCGCGTGCAAACCCAGGAACACGCCATTTATCCACTGGTG ATTAGCTGGTTTGCCGATGGTCGTCTGAAAATGCACGAAAACGCCGCGTGGCTGGATGGT CAACGTCTGCCGCCGCAGGGCTACGCTGCCGACGAGTAA PF00551 Formyl_trans_N function phosphoribosylglycinamide formyltransferase activity function transferase activity function hydroxymethyl-, formyl- and related transferase activity function transferase activity, transferring one-carbon groups function methyltransferase activity function glycine hydroxymethyltransferase activity function catalytic activity process metabolism process purine nucleotide metabolism process cellular metabolism process purine nucleotide biosynthesis process biosynthesis process IMP biosynthesis process 'de novo' IMP biosynthesis process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process nucleotide metabolism process physiological process process purine nucleoside monophosphate biosynthesis process purine ribonucleoside monophosphate biosynthesis "
drug:(10R)-10-Formyl-5,8,10-Trideazafolic Acidrdfs:label"(10R)-10-Formyl-5,8,10-Trideazafolic Acid"
drug:(10R)-10-Formyl-5,8,10-Trideazafolic Acidowl:sameAsdrug:EXPT02347
drug:(10R)-10-Formyl-5,8,10-Trideazafolic Acidrdf:typedrugbank:drugs
drug:(10R)-10-methyl-3-(6-methylpyridin-3-yl)-9,10,11,12-tetrahydro-8H-[1,4]diazepino[5',6':4,5]thieno[3,2-f]quinolin-8-onedrugbank:description" experimental This compound belongs to the bipyridines and oligopyridines. These are organic compounds containing two pyridine rings linked to each other. Bipyridines and Oligopyridines Organic Compounds Heterocyclic Compounds Pyridines and Derivatives Bipyridines and Oligopyridines Quinolines and Derivatives Thienodiazepines Benzothiophenes 1,4-Diazepines Benzene and Substituted Derivatives Thiophenes Secondary Carboxylic Acid Amides Carboxylic Acids Polyamines Secondary Amines quinoline thieno-para-diazepine benzothiophene para-diazepine benzene thiophene carboxamide group secondary carboxylic acid amide polyamine carboxylic acid derivative carboxylic acid secondary amine amine organonitrogen compound logP 3.86 ALOGPS logS -5.4 ALOGPS Water Solubility 1.53e-03 g/l ALOGPS logP 3.53 ChemAxon IUPAC Name (15R)-15-methyl-5-(6-methylpyridin-3-yl)-11-thia-6,14,17-triazatetracyclo[8.8.0.0^{2,7}.0^{12,18}]octadeca-1(10),2,4,6,8,12(18)-hexaen-13-one ChemAxon Traditional IUPAC Name (15R)-15-methyl-5-(6-methylpyridin-3-yl)-11-thia-6,14,17-triazatetracyclo[8.8.0.0^{2,7}.0^{12,18}]octadeca-1(10),2,4,6,8,12(18)-hexaen-13-one ChemAxon Molecular Weight 374.459 ChemAxon Monoisotopic Weight 374.120131908 ChemAxon SMILES [H][C@@]1(C)CNC2=C(SC3=C2C2=C(C=C3)N=C(C=C2)C2=CN=C(C)C=C2)C(=O)N1 ChemAxon Molecular Formula C21H18N4OS ChemAxon InChI InChI=1S/C21H18N4OS/c1-11-3-4-13(10-22-11)15-6-5-14-16(25-15)7-8-17-18(14)19-20(27-17)21(26)24-12(2)9-23-19/h3-8,10,12,23H,9H2,1-2H3,(H,24,26)/t12-/m1/s1 ChemAxon InChIKey InChIKey=CMWRPDHVGMHLSZ-GFCCVEGCSA-N ChemAxon Polar Surface Area (PSA) 66.91 ChemAxon Refractivity 106.92 ChemAxon Polarizability 41.3 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 15.79 ChemAxon pKa (strongest basic) 5 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 5 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 44631903 PubChem Substance 99443901 PDB B97 BE0001373 MAP kinase-activated protein kinase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown MAP kinase-activated protein kinase 2 Involved in protein kinase activity Its physiological substrate seems to be the small heat shock protein (HSP27/HSP25). In vitro can phosphorylate glycogen synthase at 'Ser-7' and tyrosine hydroxylase (on 'Ser-19' and 'Ser-40'). This kinase phosphorylates Ser in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Mediates both ERK and p38 MAPK/MAPK14 dependent neutrophil responses. Participates in TNF alpha-stimulated exocytosis of secretory vesicles in neutrophils. Plays a role in phagocytosis-induced respiratory burst activity MAPKAPK2 1q32 None 8.92 45568.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6887 GenAtlas MAPKAPK2 GeneCards MAPKAPK2 GenBank Gene Database U12779 GenBank Protein Database 530090 UniProtKB P49137 UniProt Accession MAPK2_HUMAN EC 2.7.11.1 MAPK-activated protein kinase 2 MAPKAP kinase 2 MAPKAPK-2 MK2 >MAP kinase-activated protein kinase 2 MLSNSQGQSPPVPFPAPAPPPQPPTPALPHPPAQPPPPPPQQFPQFHVKSGLQIKKNAII DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRI VDVYENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSI NIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKY DKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKM LIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSAL ATMRVDYEQIKIKKIEDASNPLLLKRRKKARALEAAALAH >1113 bp ATGCTGTCCAACTCCCAGGGCCAGAGCCCGCCGGTGCCGTTCCCCGCCCCGGCCCCGCCG CCGCAGCCCCCCACCCCTGCCCTGCCGCACCCCCCGGCGCAGCCGCCGCCGCCGCCCCCG CAGCAGTTCCCGCAGTTCCACGTCAAGTCCGGCCTGCAGATCAAGAAGAACGCCATCATC GATGACTACAAGGTCACCAGCCAGGTCCTGGGGCTGGGCATCAACGGCAAAGTTTTGCAG ATCTTCAACAAGAGGACCCAGGAGAAATTCGCCCTCAAAATGCTTCAGGACTGCCCCAAG GCCCGCAGGGAGGTGGAGCTGCACTGGCGGGCCTCCCAGTGCCCGCACATCGTACGGATC GTGGATGTGTACGAGAATCTGTACGCAGGGAGGAAGTGCCTGCTGATTGTCATGGAATGT TTGGACGGTGGAGAACTCTTTAGCCGAATCCAGGATCGAGGAGACCAGGCATTCACAGAA AGAGAAGCATCCGAAATCATGAAGAGCATCGGTGAGGCCATCCAGTATCTGCATTCAATC AACATTGCCCATCGGGATGTCAAGCCTGAGAATCTCTTATACACCTCCAAAAGGCCCAAC GCCATCCTGAAACTCACTGACTTTGGCTTTGCCAAGGAAACCACCAGCCACAACTCTTTG ACCACTCCTTGTTATACACCGTACTATGTGGCTCCAGAAGTGCTGGGTCCAGAGAAGTAT GACAAGTCCTGTGACATGTGGTCCCTGGGTGTCATCATGTACATCCTGCTGTGTGGGTAT CCCCCCTTCTACTCCAACCACGGCCTTGCCATCTCTCCGGGCATGAAGACTCGCATCCGA ATGGGCCAGTATGAATTTCCCAACCCAGAATGGTCAGAAGTATCAGAGGAAGTGAAGATG CTCATTCGGAATCTGCTGAAAACAGAGCCCACCCAGAGAATGACCATCACCGAGTTTATG AACCACCCTTGGATCATGCAATCAACAAAGGTCCCTCAAACCCCACTGCACACCAGCCGG GTCCTGAAGGAGGACAAGGAGCGGTGGGAGGATGTCAAGGGGTGTCTTCATGACAAGAAC AGCGACCAGGCCACTTGGCTGACCAGGTTGTGA PF00069 Pkinase function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process "
drug:(10R)-10-methyl-3-(6-methylpyridin-3-yl)-9,10,11,12-tetrahydro-8H-[1,4]diazepino[5',6':4,5]thieno[3,2-f]quinolin-8-onerdfs:label"(10R)-10-methyl-3-(6-methylpyridin-3-yl)-9,10,11,12-tetrahydro-8H-[1,4]diazepino[5',6':4,5]thieno[3,2-f]quinolin-8-one"
drug:(10R)-10-methyl-3-(6-methylpyridin-3-yl)-9,10,11,12-tetrahydro-8H-[1,4]diazepino[5',6':4,5]thieno[3,2-f]quinolin-8-onerdf:typedrugbank:drugs
drug:(10S)-10-Formyl-5,8,10-Trideazafolic Aciddrugbank:description" experimental This compound belongs to the stilbenes. These are organic compounds containing a 1,2-diphenylethylene moiety. Stilbenes (C6-C2-C6 ) are derived from the common phenylpropene (C6-C3) skeleton building block. The introduction of one or more hydroxyl groups to a phenyl ring lead to stilbenoids. Stilbenes Organic Compounds Phenylpropanoids and Polyketides Stilbenes Hippuric Acid Derivatives N-acyl-alpha Amino Acids Quinazolinamines Phenylpropanoic Acids Bicyclic Monoterpenes Aromatic Monoterpenes Phenylacetic Acid Derivatives Tricarboxylic Acids and Derivatives Benzoyl Derivatives Amino Fatty Acids Primary Aromatic Amines Pyrimidines and Pyrimidine Derivatives Polyols Secondary Carboxylic Acid Amides Carboxylic Acids Enolates Polyamines 3-phenylpropanoic-acid quinazolinamine aromatic monoterpene quinazoline phenylacetate monoterpene bicyclic monoterpene p-cymene alpha-amino acid or derivative tricarboxylic acid derivative benzamide benzoyl primary aromatic amine benzene pyrimidine secondary carboxylic acid amide polyol carboxamide group enolate carboxylic acid derivative carboxylic acid polyamine organonitrogen compound primary amine amine logP 0.73 ALOGPS logS -4.1 ALOGPS Water Solubility 3.92e-02 g/l ALOGPS logP -0.14 ChemAxon IUPAC Name (2R)-2-({4-[(1R)-2-(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)-1-carboxyethyl]phenyl}formamido)pentanedioic acid ChemAxon Traditional IUPAC Name (2R)-2-({4-[(1R)-2-(2-amino-4-oxo-3H-quinazolin-6-yl)-1-carboxyethyl]phenyl}formamido)pentanedioic acid ChemAxon Molecular Weight 482.4428 ChemAxon Monoisotopic Weight 482.1437637 ChemAxon SMILES NC1=NC2=CC=C(C[C@@H](C(O)=O)C3=CC=C(C=C3)C(=O)N[C@H](CCC(O)=O)C(O)=O)C=C2C(=O)N1 ChemAxon Molecular Formula C23H22N4O8 ChemAxon InChI InChI=1S/C23H22N4O8/c24-23-26-16-6-1-11(10-15(16)20(31)27-23)9-14(21(32)33)12-2-4-13(5-3-12)19(30)25-17(22(34)35)7-8-18(28)29/h1-6,10,14,17H,7-9H2,(H,25,30)(H,28,29)(H,32,33)(H,34,35)(H3,24,26,27,31)/t14-,17-/m1/s1 ChemAxon InChIKey InChIKey=DAOQLLQRJAXMGY-RHSMWYFYSA-N ChemAxon Polar Surface Area (PSA) 208.48 ChemAxon Refractivity 122.11 ChemAxon Polarizability 46.33 ChemAxon Rotatable Bond Count 10 ChemAxon H Bond Acceptor Count 10 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) 2.75 ChemAxon pKa (strongest basic) 5.23 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 3 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 46936419 PubChem Substance 46507892 PDB NHS BE0001476 Phosphoribosylglycinamide formyltransferase Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Phosphoribosylglycinamide formyltransferase Nucleotide transport and metabolism 10-formyltetrahydrofolate + 1-N-(5-phospho-D- ribosyl)glycinamide = tetrahydrofolate + 2-N-formyl-1-N-(5- phospho-D-ribosyl)glycinamide purN None 5.74 23239.0 Escherichia coli (strain K12) GenBank Gene Database M13747 GenBank Protein Database 147425 UniProtKB P08179 UniProt Accession PUR3_ECOLI 5'-phosphoribosylglycinamide transformylase EC 2.1.2.2 GAR transformylase GART >Phosphoribosylglycinamide formyltransferase MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAGIATHTLIASA FDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHT HRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEDDITARVQTQEHAIYPLV ISWFADGRLKMHENAAWLDGQRLPPQGYAADE >639 bp ATGAATATTGTGGTGCTTATTTCCGGCAACGGAAGTAATTTACAGGCAATTATTGACGCC TGTAAAACCAACAAAATTAAAGGCACCGTACGGGCAGTTTTCAGCAATAAGGCCGACGCG TTCGGCCTTGAACGCGCCCGCCAGGCGGGTATTGCAACGCATACGCTCATCGCCAGCGCG TTTGACAGTCGTGAAGCCTATGACCGGGAGTTGATTCATGAAATCGACATGTACGCACCC GATGTGGTCGTGCTGGCTGGTTTTATGCGCATTCTCAGCCCGGCGTTTGTCTCCCACTAT GCCGGGCGTTTGCTGAACATTCACCCTTCTCTGCTGCCGAAATATCCCGGATTACACACC CATCGTCAGGCGCTGGAAAATGGCGATGAAGAGCACGGTACATCGGTGCATTTCGTCACC GATGAACTGGACGGTGGCCCGGTTATTTTACAGGCGAAAGTCCCGGTATTTGCTGGTGAT TCGGAAGATGACATCACCGCCCGCGTGCAAACCCAGGAACACGCCATTTATCCACTGGTG ATTAGCTGGTTTGCCGATGGTCGTCTGAAAATGCACGAAAACGCCGCGTGGCTGGATGGT CAACGTCTGCCGCCGCAGGGCTACGCTGCCGACGAGTAA PF00551 Formyl_trans_N function transferase activity function hydroxymethyl-, formyl- and related transferase activity function transferase activity, transferring one-carbon groups function methyltransferase activity function glycine hydroxymethyltransferase activity function catalytic activity function phosphoribosylglycinamide formyltransferase activity process IMP biosynthesis process 'de novo' IMP biosynthesis process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process nucleotide metabolism process physiological process process purine nucleoside monophosphate biosynthesis process purine ribonucleoside monophosphate biosynthesis process metabolism process purine nucleotide metabolism process cellular metabolism process purine nucleotide biosynthesis process biosynthesis "
drug:(10S)-10-Formyl-5,8,10-Trideazafolic Acidrdfs:label"(10S)-10-Formyl-5,8,10-Trideazafolic Acid"
drug:(10S)-10-Formyl-5,8,10-Trideazafolic Acidowl:sameAsdrug:EXPT02348
drug:(10S)-10-Formyl-5,8,10-Trideazafolic Acidrdf:typedrugbank:drugs
drug:(11-BETA)-11,21-DIHYDROXY-PREGN-4-ENE-3,20-DIONEdrugbank:description"An adrenocortical steroid that has modest but significant activities as a mineralocorticoid and a glucocorticoid. (From Goodman and Gilman's The Pharmacological Basis of Therapeutics, 8th ed, p1437)"
drug:(11-BETA)-11,21-DIHYDROXY-PREGN-4-ENE-3,20-DIONErdfs:label"(11-BETA)-11,21-DIHYDROXY-PREGN-4-ENE-3,20-DIONE"
drug:(11-BETA)-11,21-DIHYDROXY-PREGN-4-ENE-3,20-DIONErdf:typedrugbank:drugs
drug:(11E)-OCTADEC-11-ENOIC ACIDdrugbank:description" experimental This compound belongs to the straight chain fatty acids. These are fatty acids with a straight aliphatic chain. Straight Chain Fatty Acids Organic Compounds Lipids Fatty Acids and Conjugates Straight Chain Fatty Acids Unsaturated Fatty Acids Polyamines Enolates Carboxylic Acids enolate polyamine carboxylic acid carboxylic acid derivative logP 7.67 ALOGPS logS -6.4 ALOGPS Water Solubility 1.23e-04 g/l ALOGPS logP 6.78 ChemAxon IUPAC Name (11Z)-octadec-11-enoic acid ChemAxon Traditional IUPAC Name cis-vaccenic acid ChemAxon Molecular Weight 282.4614 ChemAxon Monoisotopic Weight 282.255880332 ChemAxon SMILES CCCCCC\C=C/CCCCCCCCCC(O)=O ChemAxon Molecular Formula C18H34O2 ChemAxon InChI InChI=1S/C18H34O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18(19)20/h7-8H,2-6,9-17H2,1H3,(H,19,20)/b8-7- ChemAxon InChIKey InChIKey=UWHZIFQPPBDJPM-FPLPWBNLSA-N ChemAxon Polar Surface Area (PSA) 37.3 ChemAxon Refractivity 87.4 ChemAxon Polarizability 37.1 ChemAxon Rotatable Bond Count 15 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 4.95 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 0 ChemAxon Bioavailability 0 ChemAxon PubChem Compound 5282761 PubChem Substance 46507844 PDB VCA BE0001007 Peroxisome proliferator-activated receptor delta Human unknown Peroxisome proliferator-activated receptor delta Involved in DNA binding Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Decreases expression of NPC1L1 once activated by a ligand PPARD 6p21.2-p21.1 Nucleus None 7.65 49904.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9235 GenAtlas PPARD GeneCards PPARD GenBank Gene Database L07592 GenBank Protein Database 190230 IUPHAR 594 Guide to Pharmacology 86 UniProtKB Q03181 UniProt Accession PPARD_HUMAN NUC1 NUCI Nuclear hormone receptor 1 PPAR- beta PPAR-delta >Peroxisome proliferator-activated receptor delta MEQPQEEAPEVREEEEKEEVAEAEGAPELNGGPQHALPSSSYTDLSRSSSPPSLLDQLQM GCDGASCGSLNMECRVCGDKASGFHYGVHACEGCKGFFRRTIRMKLEYEKCERSCKIQKK NRNKCQYCRFQKCLALGMSHNAIRFGRMPEAEKRKLVAGLTANEGSQYNPQVADLKAFSK HIYNAYLKNFNMTKKKARSILTGKASHTAPFVIHDIETLWQAEKGLVWKQLVNGLPPYKE ISVHVFYRCQCTTVETVRELTEFAKSIPSFSSLFLNDQVTLLKYGVHEAIFAMLASIVNK DGLLVANGSGFVTREFLRSLRKPFSDIIEPKFEFAVKFNALELDDSDLALFIAAIILCGD RPGLMNVPRVEAIQDTILRALEFHLQANHPDAQYLFPKLLQKMADLRQLVTEHAQMMQRI KKTETETSLHPLLQEIYKDMY >1326 bp ATGGAGCAGCCACAGGAGGAAGCCCCTGAGGTCCGGGAAGAGGAGGAGAAAGAGGAAGTG GCAGAGGCAGAAGGAGCCCCAGAGCTCAATGGGGGACCACAGCATGCACTTCCTTCCAGC AGCTACACAGACCTCTCCCGGAGCTCCTCGCCACCCTCACTGCTGGACCAACTGCAGATG GGCTGTGACGGGGCCTCATGCGGCAGCCTCAACATGGAGTGCCGGGTGTGCGGGGACAAG GCATCGGGCTTCCACTACGGTGTTCATGCATGTGAGGGGTGCAAGGGCTTCTTCCGTCGT ACGATCCGCATGAAGCTGGAGTACGAGAAGTGTGAGCGCAGCTGCAAGATTCAGAAGAAG AACCGCAACAAGTGCCAGTACTGCCGCTTCCAGAAGTGCCTGGCACTGGGCATGTCACAC AACGCTATCCGTTTTGGTCGGATGCCGGAGGCTGAGAAGAGGAAGCTGGTGGCAGGGCTG ACTGCAAACGAGGGGAGCCAGTACAACCCACAGGTGGCCGACCTGAAGGCCTTCTCCAAG CACATCTACAATGCCTACCTGAAAAACTTCAACATGACCAAAAAGAAGGCCCGCAGCATC CTCACCGGCAAAGCCAGCCACACGGCGCCCTTTGTGATCCACGACATCGAGACATTGTGG CAGGCAGAGAAGGGGCTGGTGTGGAAGCAGTTGGTGAATGGCCTGCCTCCCTACAAGGAG ATCAGCGTGCACGTCTTCTACCGCTGCCAGTGCACCACAGTGGAGACCGTGCGGGAGCTC ACTGAGTTCGCCAAGAGCATCCCCAGCTTCAGCAGCCTCTTCCTCAACGACCAGGTTACC CTTCTCAAGTATGGCGTGCACGAGGCCATCTTCGCCATGCTGGCCTCTATCGTCAACAAG GACGGGCTGCTGGTAGCCAACGGCAGTGGCTTTGTCACCCGTGAGTTCCTGCGCAGCCTC CGCAAACCCTTCAGTGATATCATTGAGCCTAAGTTTGAATTTGCTGTCAAGTTCAACGCC CTGGAACTTGATGACAGTGACCTGGCCCTATTCATTGCGGCCATCATTCTGTGTGGAGAC CGGCCAGGCCTCATGAACGTTCCACGGGTGGAGGCTATCCAGGACACCATCCTGCGTGCC CTCGAATTCCACCTGCAGGCCAACCACCCTGATGCCCAGTACCTCTTCCCCAAGCTGCTG CAGAAGATGGCTGACCTGCGGCAACTGGTCACCGAGCACGCCCAGATGATGCAGCGGATC AAGAAGACCGAAACCGAGACCTCGCTGCACCCTCTGCTCCAGGAGATCTACAAGGACATG TACTAA PF00104 Hormone_recep PF00105 zf-C4 component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function transcription factor activity function ligand-dependent nuclear receptor activity function DNA binding function binding function signal transducer activity function receptor activity function nucleic acid binding function steroid hormone receptor activity process regulation of biological process process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent "
drug:(11E)-OCTADEC-11-ENOIC ACIDrdfs:label"(11E)-OCTADEC-11-ENOIC ACID"
drug:(11E)-OCTADEC-11-ENOIC ACIDrdf:typedrugbank:drugs
drug:(11R)-10-acetyl-11-(2,4-dichlorophenyl)-6-hydroxy-3,3-dimethyl-2,3,4,5,10,11-hexahydro-1H-dibenzo[b,e][1,4]diazepin-1-onedrugbank:description" experimental This compound belongs to the benzodiazepines. These are organic compounds containing a benzene ring fused to either isomers of diazepine(unsaturated seven-member heterocycle with two nitrogen atoms replacing two carbon atoms). Benzodiazepines Organic Compounds Heterocyclic Compounds Benzodiazepines Dichlorobenzenes Phenols and Derivatives Aryl Chlorides Tertiary Carboxylic Acid Amides Ketones Tertiary Amines Enolates Enols Enamines Polyamines Carboxylic Acids Organochlorides 1,3-dichlorobenzene chlorobenzene phenol derivative benzene aryl halide aryl chloride tertiary carboxylic acid amide carboxamide group ketone tertiary amine enol enolate polyamine carboxylic acid derivative enamine carboxylic acid organohalogen amine carbonyl group organonitrogen compound organochloride logP 5.12 ALOGPS logS -5.1 ALOGPS Water Solubility 3.33e-03 g/l ALOGPS logP 4.1 ChemAxon IUPAC Name (10R)-9-acetyl-10-(2,4-dichlorophenyl)-4-hydroxy-14,14-dimethyl-2,9-diazatricyclo[9.4.0.0^{3,8}]pentadeca-1(11),3,5,7-tetraen-12-one ChemAxon Traditional IUPAC Name (10R)-9-acetyl-10-(2,4-dichlorophenyl)-4-hydroxy-14,14-dimethyl-2,9-diazatricyclo[9.4.0.0^{3,8}]pentadeca-1(11),3,5,7-tetraen-12-one ChemAxon Molecular Weight 445.338 ChemAxon Monoisotopic Weight 444.100747994 ChemAxon SMILES [H][C@]1(N(C(C)=O)C2=CC=CC(O)=C2NC2=C1C(=O)CC(C)(C)C2)C1=C(Cl)C=C(Cl)C=C1 ChemAxon Molecular Formula C23H22Cl2N2O3 ChemAxon InChI InChI=1S/C23H22Cl2N2O3/c1-12(28)27-17-5-4-6-18(29)21(17)26-16-10-23(2,3)11-19(30)20(16)22(27)14-8-7-13(24)9-15(14)25/h4-9,22,26,29H,10-11H2,1-3H3/t22-/m0/s1 ChemAxon InChIKey InChIKey=JJTPPGUNMJMPLY-QFIPXVFZSA-N ChemAxon Polar Surface Area (PSA) 69.64 ChemAxon Refractivity 120.12 ChemAxon Polarizability 44.94 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 9.58 ChemAxon pKa (strongest basic) -2 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon ChemSpider 24692535 PDB XND BE0004389 Genome polyprotein HCV # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Genome polyprotein Involved in ATP binding NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication (By similarity) RNA-directed RNA polymerase:Host endoplasmic reticulum membrane 169-189 359-379 726-746 758-778 783-803 814-834 882-902 929-949 1658-1678 1806-1826 1829-1849 1851-1871 1882-1902 2990-3010 8.17 326763.6 HCV GenBank Gene Database D10750 GenBank Protein Database 221607 UniProtKB O92972 UniProt Accession POLG_HCVJ4 Capsid protein C Core protein p19 Core protein p21 Envelope glycoprotein E1 Envelope glycoprotein E2 gp32 gp35 gp68 gp70 Hepacivirin Non-structural protein 4A Non-structural protein 4B Non-structural protein 5A NS1 NS3P NS4A NS4B NS5A NS5B p21 p23 p27 p56 p68 p7 p70 p8 Protease NS2-3 RNA-directed RNA polymerase Serine protease/NTPase/helicase NS3 >Genome polyprotein MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKASERSQPRG RRQPIPKARRPEGRAWAQPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLG KVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLA LLSCLTIPASAYEVRNVSGIYHVTNDCSNSSIVYEAADVIMHTPGCVPCVREGNSSRCWV ALTPTLAARNASVPTTTIRRHVDLLVGTAAFCSAMYVGDLCGSIFLVSQLFTFSPRRHET VQDCNCSIYPGHVSGHRMAWDMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLA YYSMVGNWAKVLIVALLFAGVDGETHTTGRVAGHTTSGFTSLFSSGASQKIQLVNTNGSW HINRTALNCNDSLQTGFFAALFYAHKFNSSGCPERMASCRPIDWFAQGWGPITYTKPNSS DQRPYCWHYAPRPCGVVPASQVCGPVYCFTPSPVVVGTTDRSGVPTYSWGENETDVMLLN NTRPPQGNWFGCTWMNSTGFTKTCGGPPCNIGGVGNRTLICPTDCFRKHPEATYTKCGSG PWLTPRCLVDYPYRLWHYPCTLNFSIFKVRMYVGGVEHRLNAACNWTRGERCNLEDRDRS ELSPLLLSTTEWQILPCAFTTLPALSTGLIHLHQNIVDVQYLYGVGSAFVSFAIKWEYIL LLFLLLADARVCACLWMMLLIAQAEAALENLVVLNAASVAGAHGILSFLVFFCAAWYIKG RLAPGAAYAFYGVWPLLLLLLALPPRAYALDREMAASCGGAVLVGLVFLTLSPYYKVFLT RLIWWLQYFITRAEAHMQVWVPPLNVRGGRDAIILLTCAVHPELIFDITKLLLAILGPLM VLQAGITRVPYFVRAQGLIRACMLVRKVAGGHYVQMAFMKLGALTGTYVYNHLTPLRDWA HAGLRDLAVAVEPVVFSAMETKVITWGADTAACGDIILGLPVSARRGKEIFLGPADSLEG QGWRLLAPITAYSQQTRGVLGCIITSLTGRDKNQVEGEVQVVSTATQSFLATCINGVCWT VYHGAGSKTLAGPKGPITQMYTNVDLDLVGWQAPPGARSMTPCSCGSSDLYLVTRHADVI PVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHVVGVFRAAVCTRGVAKAVDFIPVES METTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAA TLGFGAYMSKAHGIDPNIRTGVRTITTGGSITYSTYGKFLADGGCSGGAYDIIICDECHS TDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEIGLSNNGEIPFYGKAI PIEAIKGGRHLIFCHSKKKCDELAAKLTGLGLNAVAYYRGLDVSVIPPIGDVVVVATDAL MTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRSGIYR FVTPGERPSGMFDSSVLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWES VFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHG PTPLLYRLGAVQNEVILTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSV VIVGRIILSGKPAVVPDREVLYQEFDEMEECASQLPYIEQGMQLAEQFKQKALGLLQTAT KQAEAAAPVVESKWRALETFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSP LTTQNTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVGSIGLGKVLVDILAGYGAGVA GALVAFKVMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI AFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLRDV WDWICTVLTDFKTWLQSKLLPRLPGVPFLSCQRGYKGVWRGDGIMQTTCPCGAQIAGHVK NGSMRIVGPRTCSNTWHGTFPINAYTTGPCTPSPAPNYSRALWRVAAEEYVEVTRVGDFH YVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPACKPLLREDVTFQVGLNQYLVGSQL PCEPEPDVTVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHD SPDADLIEANLLWRQEMGGNITRVESENKVVILDSFEPLHAEGDEREISVAAEILRKSRK FPSALPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPPTKAPPIPPPRRKRTVVLTESNV SSALAELATKTFGSSGSSAVDSGTATALPDLASDDGDKGSDVESYSSMPPLEGEPGDPDL SDGSWSTVSEEASEDVVCCSMSYTWTGALITPCAAEESKLPINPLSNSLLRHHNMVYATT SRSASLRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKAKLLSIEEACKLTPPHSAKSKF GYGAKDVRNLSSRAVNHIRSVWEDLLEDTETPIDTTIMAKSEVFCVQPEKGGRKPARLIV FPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPKQRVEFLVNTWKSKKCPMGFSYDT RCFDSTVTESDIRVEESIYQCCDLAPEARQAIRSLTERLYIGGPLTNSKGQNCGYRRCRA SGVLTTSCGNTLTCYLKATAACRAAKLQDCTMLVNGDDLVVICESAGTQEDAAALRAFTE AMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETAR HTPINSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQ IIERLHGLSAFTLHSYSPGEINRVASCLRKLGVPPLRTWRHRARSVRAKLLSQGGRAATC GRYLFNWAVRTKLKLTPIPAASQLDLSGWFVAGYSGGDIYHSLSRARPRWFPLCLLLLSV GVGIYLLPNR >9033 bp ATGAGCACGAATCCTAAACCTCAAAGAAAAACCAAACGTAACACCAACCGCCGCCCACAG GACGTCAAGTTCCCGGGCGGTGGTCAGATCGTTGGTGGAGTTTACCTGTTGCCGCGCAGG GGCCCCAGGTTGGGTGTGCGCGCGACTAGGAAGACTTCCGAGCGGTCGCAACCTCGTGGA AGGCGACAACCTATCCCAAAGGCTCGCCAACCCGAGGGCAGGGCCTGGGCTCAGCCCGGG TACCCTTGGCCCCTCTATGGCAATGAGGGCTTGGGGTGGGCAGGATGGCTCCTGTCACCC CGCGGCTCCCGGCCTAGTTGGGGCCCCACGGACCCCCGGCGTAGGTCGCGTAACTTGGGT AAGGTCATCGATACCCTTACATGCGGCTTCGCCGATCTCATGGGGTACATTCCGCTCGTC GGCGCCCCCCTAGGGGGCGCTGCCAGGGCCTTGGCACACGGTGTCCGGGTTCTGGAGGAC GGCGTGAACTATGCAACAGGGAACTTGCCCGGTTGCTCTTTCTCTATCTTCCTCTTGGCT CTGCTGTCCTGTTTGACCATCCCAGCTTCCGCTTATGAAGTGCGCAACGTGTCCGGGATA TACCATGTCACGAACGACTGCTCCAACTCAAGCATTGTGTATGAGGCAGCGGACGTGATC ATGCATACTCCCGGGTGCGTGCCCTGTGTTCGGGAGGGCAACAGCTCCCGTTGCTGGGTA GCGCTCACTCCCACGCTCGCGGCCAGAGATGCCAGCGTCCCCACTACGACAATACGACGC CACGTCGACTTGCTCGTTGGGACGGCTGCTTTCTGCTCCGCTATGTACGTGGGGGATCTC TGCGGATCTATTTTCCTCGTCTCCCAGCTGTTCACCTTCTCGCCTCGCCGGCATGAGACA GTGCAGGACTGCAACTGCTCAATCTATCCCGGCCATGTATCAGGTCACCGCATGGCTTGG GATATGATGATGAACTGGTCACCTACAACAGCCCTAGTGGTGTCGCAGTTGCTCCGGATC CCACAAGCTGTCGTGGACATGGTGGCGGGGGCCCACTGGGGAGTCCTGGCGGGCCTTGCC TACTATTCCATGGTAGGGAACTGGGCTAAGGTTCTGATTGTGGCGCTACTCTTTGCCGGC GTTGACGGGGCGACCTACACGTCGGGGGGGGTGGCCGGCCGCACCACCTCCGGGTTCACG TCCCTCTTCTCATCTGGGGCGTCTCAGAAAATCCAGCTTGTGAATACCAACGGCAGCTGG CACATCAACAGGACTGCCCTAAATTGCAATGACTCCCTCCACACTGGGTTCCTTGCCGCG CTGTTCTACACACACAAGTTCAACTCGTCCGGGTGCCCGGAGCGCATGGCCAGCTGCCGC CCCATTGACGGGTTCGCCCAGGGATGGGGCCCCATCACCTATACTGAGCCTAACAGCCCG GATCAGAGGCCTTATTGCTGGCATTACGCGCCTCGACCGTGTGGTATCGTACCCGCGTCG CAGGTGTGTGGTCCAGTGTATTGTTTCACCCCAAGCCCTGTTGTGGTGGGGACCACCGAT CGTTCCGGTGTCCCTACGTATAGCTGGGGGGAGAATGAGACAGACGTGATGCTCCTCAAC AACACGCGTCCGCCACAAGGCAACTGGTTCGGCTGTACATGGATGAATAGTACTGGGTTC ACTAAGACGTGCGGAGGCCCCCCGTGTAACATCGGGGGGGTCGGTAACCGCACCTTGATC TGCCCCACGGACTGCTTCCGGAAGCACCCCGAGGCTACTTACACAAAATGTGGCTCGGGG CCCTGGTTGACACCTAGGTGCCTAGTAGACTACCCATACAGGCTCTGGCACTACCCCTGC ACTCTCAATTTTTCCATCTTTAAGGTTAGGATGTATGTGGGGGGCGTGGAGCACAGGCTC AATGCCGCATGCAATTGGACTCGAGGAGAGCGCTGTAACTTGGAGGACAGGGATAGGTCA GAACTCAGCCCGCTGCTGCTGTCTACAACAGAGTGGCAGATACTGCCCTGTGCCTTCACC ACCCTACCGGCTTTATCCACTGGTTTGATCCATCTCCATCAGAACATCGTGGACGTGCAA TACCTGTACGGTGTAGGGTCAGCGTTTGTCTCCTTTGCAATCAAATGGGAGTACATCCTG TTGCTTTTCCTTCTCCTGGCAGACGCGCGCGTGTGTGCCTGCTTGTGGATGATGCTGCTG ATAGCCCAGGCTGAGGCCGCCTTAGAGAACTTGGTGGTCCTCAATGCGGCGTCCGTGGCC GGAGCGCATGGTATTCTCTCCTTTCTTGTGTTCTTCTGCGCCGCCTGGTACATTAAGGGC AGGCTGGCTCCTGGGGCGGCGTATGCTTTTTATGGCGTATGGCCGCTGCTCCTGCTCCTA CTGGCGTTACCACCACGAGCTTACGCCTTGGACCGGGAGATGGCTGCATCGTGCGGGGGT GCGGTTCTTGTAGGTCTGGTATTCTTGACCTTGTCACCATACTACAAAGTGTTTCTCACT AGGCTCATATGGTGGTTACAATACTTTATCACCAGAGCCGAGGCGCACATGCAAGTGTGG GTCCCCCCCCTCAACGTTCGGGGAGGCCGCGATGCCATCATCCTCCTCACGTGTGCGGTT CATCCAGAGTTAATTTTTGACATCACCAAACTCCTGCTCGCCATACTCGGCCCGCTCATG GTGCTCCAGGCTGGCATAACGAGAGTGCCGTACTTCGTGCGCGCTCAAGGGCTCATTCGT GCATGCATGTTAGTGCGGAAAGTCGCCGGGGGTCATTATGTCCAAATGGCCTTCATGAAG CTGGGCGCGCTGACAGGTACGTACGTTTATAACCATCTTACCCCACTGCGGGACTGGGCC CACGCGGGCCTACGAGACCTTGCGGTGGCGGTAGAGCCCGTCGTCTTCTCCGCCATGGAG ACCAAGGTCATCACCTGGGGAGCAGACACCGCAGCATGTGGAGACATCATCTTGGGCCTA CCCGTCTCCGCCCGAAGGGGGAAGGAGATATTTTTGGGACCGGCTGATAGTCTCGAAGGG CAAGGGTGGCGACTCCTTGCGCCCATCACGGCCTACTCCCAACAAACGCGGGGCGTACTT GGTTGCATCATCACTAGCCTCACAGGCCGGGACAAGAACCAGGTCGAGGGGGAGGTTCAA GTGGTTTCTACCGCAACACAATCTTTCCTGGCGACCTGCATCAACGGCGTGTGCTGGACT GTCTACCATGGCGCTGGCTCGAAGACCCTAGCCGGTCCAAAAGGTCCAATCACCCAAATG TACACCAATGTAGACCTGGACCTCGTCGGCTGGCAGGCGCCCCCCGGGGCGCGCTCCATG ACACCATGCAGCTGTGGCAGCTCGGACCTTTACTTGGTCACGAGACATGCTGATGTCATT CCGGTGCGCCGGCGAGGCGACAGCAGGGGAAGTCTACTCTCCCCCAGGCCCGTCTCCTAC CTGAAGGGCTCCTCGGGTGGTCCATTGCTTTGCCCTTCGGGGCACGTCGTGGGCGTCTTC CGGGCTGCTGTGTGCACCCGGGGGGTCGCGAAGGCGGTGGACTTCATACCCGTTGAGTCT ATGGAAACTACCATGCGGTCTCCGGTCTTCACAGACAACTCATCCCCCCCGGCTGTACCG CAGACATTCCAAGTGGCACATCTGCACGCTCCTACTGGCAGCGGCAAGAGCACTAAAGTG CCGGCTGCGTATGCAGCCCAAGGGTACAAGGTGCTCGTCCTGAACCCGTCCGTTGCCGCC ACCTTAGGGTTTGGGGCGTATATGTCCAAGGCACACGGTATCGACCCTAACATCAGAACT GGGGTAAGGACCATTACCACGGGCGGCTCCATTACGTACTCCACCTATGGCAAGTTCCTT GCCGACGGTGGCTGCTCCGGGGGCGCCTATGACATCATAATATGTGATGAGTGCCACTCA ACTGACTCGACTACCATCTTGGGCATCGGCACAGTCCTGGACCAAGCGGAGACGGCTGGA GCGCGGCTTGTCGTGCTCGCCACCGCTACACCTCCGGGATCGGTTACCGTGCCACACCCC AATATCGAGGAAATAGGCCTGTCCAACAATGGAGAGATCCCCTTCTATGGCAAAGCCATC CCCATTGAGGCCATCAAGGGGGGGAGGCATCTCATTTTCTGCCATTCCAAGAAGAAATGT GACGAGCTCGCCGCAAAGCTGACAGGCCTCGGACTGAATGCTGTAGCATATTACCGGGGC CTTGATGTGTCCGTCATACCGCCTATCGGAGACGTCGTTGTCGTGGCAACAGACGCTCTA ATGACGGGTTTCACCGGCGATTTTGACTCAGTGATCGACTGCAACACATGTGTCACCCAG ACAGTCGACTTCAGCTTGGATCCCACCTTCACCATTGAGACGACGACCGTGCCCCAAGAC GCGGTGTCGCGCTCGCAACGGCGAGGTAGAACTGGCAGGGGTAGGAGTGGCATCTACAGG TTTGTGACTCCAGGAGAACGGCCCTCGGGCATGTTCGATTCTTCGGTCCTGTGTGAGTGC TATGACGCGGGCTGTGCTTGGTATGAGCTCACGCCCGCTGAGACCTCGGTTAGGTTGCGG GCTTACCTAAATACACCAGGGTTGCCCGTCTGCCAGGACCATCTGGAGTTCTGGGAGAGC GTCTTCACAGGCCTCACCCACATAGATGCCCACTTCCTGTCCCAGACTAAACAGGCAGGA GACAACTTTCCTTACCTGGTGGCATATCAAGCTACAGTATGCGCCAGGGCTCAAGCTCCA CCTCCATCGTGGGACCAAATGTGGAAGTGTCTCATACGGCTGAAACCTACACTGCACGGG CCAACACCCCTGCTGTATAGGCTAGGAGCCGTCCAAAATGAGGTCATCCTCACACACCCC ATAACTAAATACATCATGGCATGCATGTCGGCTGACCTGGAGGTCGTCACTAGCACCTGG GTGCTGGTAGGCGGAGTCCTTGCAGCTTTGGCCGCATATTGCCTGACGACAGGCAGTGTG GTCATTGTGGGCAGGATCATCTTGTCCGGGAAGCCAGCTGTCGTTCCCGACAGGGAAGTC CTCTACCAGGAGTTCGATGAGATGGAAGAGTGTGCCTCACAACTTCCTTACATCGAGCAG GGAATGCAGCTCGCCGAGCAATTTAAGCAAAAGGCGCTCGGGTTGTTGCAAACGGCCACC AAGCAAGCGGAGGCTGCTGCTCCCGTGGTGGAGTCCAAGTGGCGAGCCCTTGAGACCTTC TGGGCGAAGCACATGTGGAATTTCATCAGCGGGATACAGTACCTAGCAGGCTTATCCACT CTGCCTGGGAACCCCGCGATAGCATCATTGATGGCATTTACAGCTTCTATCACTAGCCCG CTCACCACCCAAAACACCCTCCTGTTTAACATCTTGGGGGGATGGGTGGCTGCCCAACTC GCTCCTCCCAGCGCTGCGTCAGCTTTCGTGGGCGCCGGCATCGCCGGAGCGGCTGTTGGC AGCATAGGCCTTGGGAAGGTGCTCGTGGACATCTTGGCGGGCTATGGGGCAGGGGTAGCC GGCGCACTCGTGGCCTTTAAGGTCATGAGCGGCGAGGTGCCCTCCACCGAGGACCTGGTC AACTTACTCCCTGCCATCCTCTCTCCTGGTGCCCTGGTCGTCGGGGTCGTGTGCGCAGCA ATACTGCGTCGGCACGTGGGCCCGGGAGAGGGGGCTGTGCAGTGGATGAACCGGCTGATA GCGTTCGCTTCGCGGGGTAACCACGTCTCCCCCACGCACTATGTGCCTGAGAGCGACGCT GCAGCACGTGTCACTCAGATCCTCTCTAGCCTTACCATCACTCAACTGCTGAAGCGGCTT CACCAGTGGATTAATGAGGACTGCTCTACGCCATGCTCCGGCTCGTGGCTAAGGGATGTT TGGGATTGGATATGCACGGTGTTGACTGACTTCAAGACCTGGCTCCAGTCCAAGCTCCTG CCGCGGTTACCGGGAGTCCCTTTCCTGTCATGCCAACGCGGGTACAAGGGAGTCTGGCGG GGGGACGGCATCATGCAAACCACCTGCCCATGTGGAGCACAGATCGCCGGACATGTCAAA AACGGTTCCATGAGGATCGTAGGGCCTAGAACCTGCAGCAACACGTGGCACGGAACGTTC CCCATCAACGCATACACCACGGGACCCTGCACACCCTCCCCGGCGCCCAACTATTCCAGG GCGCTATGGCGGGTGGCTGCTGAGGAGTACGTGGAGGTTACGCGTGTGGGAGATTTCCAC TACGTGACGGGCATGACCACTGACAACGTAAAGTGCCCATGCCAGGTTCCGGCCCCCGAA TTCTTCACGGAGGTGGATGGAGTGCGGTTGCACAGGTACGCTCCGGCGTGCAAACCTCTC CTACGGGAGGACGTCACGTTCCAGGTCGGGCTCAACCAATACTTGGTCGGGTCGCAGCTC CCATGCGAGCCCGAACCGGACGTAACAGTGCTTACTTCCATGCTCACCGATCCCTCCCAC ATTACAGCAGAGACGGCTAAGCGTAGGCTGGCTAGAGGGTCCCCCCCCTCTTTAGCCAGC TCATCAGCTAGCCAGTTGTCTGCGCCTTCTTTGAAGGCGACATGCACTACCCACCATGAC TCCCCGGACGCTGACCTCATCGAGGCCAACCTCTTGTGGCGGCAGGAGATGGGCGGAAAC ATCACTCGCGTGGAGTCAGAGAATAAGGTAGTAATTCTGGACTCTTTCGAACCGCTTCAC GCGGAGGGGGATGAGAGGGAGATATCCGTCGCGGCGGAGATCCTGCGAAAATCCAGGAAG TTCCCCTCAGCGTTGCCCATATGGGCACGCCCGGACTACAATCCTCCACTGCTAGAGTCC TGGAAGGACCCGGACTACGTCCCTCCGGTGGTACACGGATGCCCATTGCCACCTACCAAG GCTCCTCCAATACCACCTCCACGGAGAAAGAGGACGGTTGTCCTGACAGAATCCAATGTG TCTTCTGCCTTGGCGGAGCTCGCCACTAAGACCTTCGGTAGCTCCGGATCGTCGGCCGTT GATAGCGGCACGGCGACCGCCCTTCCTGACCTGGCCTCCGACGACGGTGACAAAGGGTCC GACGTTGAGTCGTACTCCTCCATGCCCCCCCTTGAAGGGGAGCCGGGGGACCCCGATCTC AGCGACGGGTCTTGGTCTACCGTGAGTGAGGAGGCTAGTGAGGACGTCGTCTGCTGCTCA ATGTCCTATACGTGGACAGGCGCCCTGATCACGCCATGCGCTGCGGAGGAAAGTAAGCTG CCCATCAACCCGTTGAGCAACTCTTTGCTGCGTCACCACAACATGGTCTACGCCACAACA TCCCGCAGCGCAAGCCTCCGGCAGAAGAAGGTCACCTTTGACAGATTGCAAGTCCTGGAT GACCATTACCGGGACGTGCTCAAGGAGATGAAGGCGAAGGCGTCCACAGTTAAGGCTAAG CTTCTATCTATAGAGGAGGCCTGCAAGCTGACGCCCCCACATTCGGCCAAATCCAAATTT GGCTATGGGGCAAAGGACGTCCGGAACCTATCCAGCAGGGCCGTTAACCACATCCGCTCC GTGTGGGAGGACTTGCTGGAAGACACTGAAACACCAATTGACACCACCATCATGGCAAAA AGTGAGGTTTTCTGCGTCCAACCAGAGAAGGGAGGCCGCAAGCCAGCTCGCCTTATCGTA TTCCCAGACCTGGGAGTTCGTGTATGCGAGAAGATGGCCCTTTACGACGTGGTCTCCACC CTTCCTCAGGCCGTGATGGGCTCCTCATACGGATTTCAATACTCCCCCAAGCAGCGGGTC GAGTTCCTGGTGAATACCTGGAAATCAAAGAAATGCCCTATGGGCTTCTCATATGACACC CGCTGTTTTGACTCAACGGTCACTGAGAGTGACATTCGTGTTGAGGAGTCAATTTACCAA TGTTGTGACTTGGCCCCCGAGGCCAGACAGGCCATAAGGTCGCTCACGGAGCGGCTTTAC ATCGGGGGTCCCCTGACTAACTCAAAAGGGCAGAACTGCGGTTATCGCCGGTGCCGCGCA AGTGGCGTGCTGACGACTAGCTGCGGTAATACCCTCACATGTTACTTGAAGGCCACTGCG GCCTGTCGAGCTGCAAAGCTCCAGGACTGCACGATGCTCGTGAACGGAGACGACCTTGTC GTTATCTGTGAAAGCGCGGGAACCCAGGAGGATGCGGCGGCCCTACGAGCCTTCACGGAG GCTATGACTAGGTACTCCGCCCCCCCCGGGGATCCGCCCCAACCAGAATACGACCTGGAG CTGATAACATCATGTTCCTCCAATGTGTCAGTCGCGCACGATGCATCTGGCAAAAGGGTA TACTACCTCACCCGTGACCCCACCACCCCCCTTGCACGGGCTGCGTGGGAGACAGCTAGA CACACTCCAATCAACTCTTGGCTAGGCAATATCATCATGTATGCGCCCACCCTATGGGCA AGGATGATTCTGATGACTCACTTTTTCTCCATCCTTCTAGCTCAAGAGCAACTTGAAAAA GCCCTGGATTGTCAGATCTACGGGGCCTGCTACTCCATTGAGCCACTTGACCTACCTCAG ATCATTGAACGACTCCATGGTCTTAGCGCATTTACACTCCACAGTTACTCTCCAGGTGAG ATCAATAGGGTGGCTTCATGCCTCAGGAAACTTGGGGTACCACCCTTGCGAACCTGGAGA CATCGGGCCAGAAGTGTCCGCGCTAAGCTACTGTCCCAGGGGGGGAGGGCCGCCACTTGT GGCAGATACCTCTTTAACTGGGCAGTAAGGACCAAGCTTAAACTCACTCCAATCCCGGCT GCGTCCCAGCTGGACTTGTCCGGCTGGTTCGTCGCTGGTTACAGCGGGGGAGACATATAT CACAGCCTGTCTCGTGCCCGACCCCGCTGGTTTCCGTTGTGCCTACTCCTACTTTTTGTA GGGGTAGGCATTTACCTGCTCCCCAACCGATGA PF01543 HCV_capsid PF01542 HCV_core PF01539 HCV_env PF01560 HCV_NS1 PF01538 HCV_NS2 PF01006 HCV_NS4a PF01001 HCV_NS4b PF01506 HCV_NS5a PF08300 HCV_NS5a_1a PF08301 HCV_NS5a_1b PF02907 Peptidase_S29 PF00998 RdRP_3 component viral capsid component virion component viral envelope function hydrolase activity function nucleotide binding function purine nucleotide binding function peptidase activity function helicase activity function adenyl nucleotide binding function transferase activity function nucleotidyltransferase activity function binding function ATP binding function transferase activity, transferring phosphorus-containing groups function serine-type peptidase activity function catalytic activity function nucleic acid binding function RNA-directed RNA polymerase activity function RNA binding function structural molecule activity process viral infectious cycle process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process viral genome replication process macromolecule metabolism process protein metabolism process cellular protein metabolism process proteolysis process interaction between organisms process interspecies interaction between organisms process transcription process physiological process process symbiosis, encompassing mutualism through parasitism process interaction with host process metabolism process virus-host interaction process viral life cycle process cellular metabolism process transformation of host cell by virus "
drug:(11R)-10-acetyl-11-(2,4-dichlorophenyl)-6-hydroxy-3,3-dimethyl-2,3,4,5,10,11-hexahydro-1H-dibenzo[b,e][1,4]diazepin-1-onerdfs:label"(11R)-10-acetyl-11-(2,4-dichlorophenyl)-6-hydroxy-3,3-dimethyl-2,3,4,5,10,11-hexahydro-1H-dibenzo[b,e][1,4]diazepin-1-one"
drug:(11R)-10-acetyl-11-(2,4-dichlorophenyl)-6-hydroxy-3,3-dimethyl-2,3,4,5,10,11-hexahydro-1H-dibenzo[b,e][1,4]diazepin-1-onerdf:typedrugbank:drugs
drug:(11S)-8-CHLORO-11-[1-(METHYLSULFONYL)PIPERIDIN-4-YL]-6-PIPERAZIN-1-YL-11H-BENZO[5,6]CYCLOHEPTA[1,2-B]PYRIDINEdrugbank:description" experimental This compound belongs to the benzocycloheptapyridines. These are aromatic compounds containing a benzene ring and a pyridine ring fused to a seven membered carbocycle. Benzocycloheptapyridines Organic Compounds Heterocyclic Compounds Benzocycloheptapyridines Chlorobenzenes Diazinanes Aryl Chlorides Pyridines and Derivatives Piperidines Piperazines Sulfonamides Sulfonyls Tertiary Amines Enamines Polyamines Dialkylamines Organochlorides chlorobenzene piperazine 1,4-diazinane aryl halide piperidine pyridine benzene aryl chloride sulfonic acid derivative sulfonyl sulfonamide tertiary amine polyamine enamine secondary aliphatic amine secondary amine amine organochloride organonitrogen compound organohalogen logP 2.62 ALOGPS logS -4 ALOGPS Water Solubility 4.72e-02 g/l ALOGPS logP 1.82 ChemAxon IUPAC Name (2S)-13-chloro-2-(1-methanesulfonylpiperidin-4-yl)-10-(piperazin-1-yl)-4-azatricyclo[9.4.0.0^{3,8}]pentadeca-1(11),3(8),4,6,9,12,14-heptaene ChemAxon Traditional IUPAC Name (2S)-13-chloro-2-(1-methanesulfonylpiperidin-4-yl)-10-(piperazin-1-yl)-4-azatricyclo[9.4.0.0^{3,8}]pentadeca-1(11),3(8),4,6,9,12,14-heptaene ChemAxon Molecular Weight 473.031 ChemAxon Monoisotopic Weight 472.169974589 ChemAxon SMILES [H][C@]1(C2CCN(CC2)S(C)(=O)=O)C2=C(C=C(Cl)C=C2)C(=CC2=C1N=CC=C2)N1CCNCC1 ChemAxon Molecular Formula C24H29ClN4O2S ChemAxon InChI InChI=1S/C24H29ClN4O2S/c1-32(30,31)29-11-6-17(7-12-29)23-20-5-4-19(25)16-21(20)22(28-13-9-26-10-14-28)15-18-3-2-8-27-24(18)23/h2-5,8,15-17,23,26H,6-7,9-14H2,1H3/t23-/m0/s1 ChemAxon InChIKey InChIKey=ZMGCFGGMTCMSDP-QHCPKHFHSA-N ChemAxon Polar Surface Area (PSA) 65.54 ChemAxon Refractivity 129.91 ChemAxon Polarizability 50.16 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 9.23 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 5 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 9547909 PubChem Substance 99443687 ChemSpider 7826847 PDB 736 BE0002373 Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Involved in protein prenyltransferase activity Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate FNTA 8p11 None 4.72 44409.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3782 GenAtlas FNTA GeneCards FNTA GenBank Gene Database L10413 UniProtKB P49354 UniProt Accession FNTA_HUMAN CAAX farnesyltransferase alpha subunit EC 2.5.1.58 EC 2.5.1.59 FTase-alpha GGTase-I-alpha Ras proteins prenyltransferase alpha Type I protein geranyl-geranyltransferase alpha subunit >Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDS PSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLT RDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLR DPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQR YFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLL DLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIG RSLQSKHSTENDSPTNVQQ >1140 bp ATGGCGGCCACCGAGGGGGTCGGGGAGGCTGCGCAAGGGGGCGAGCCCGGGCAGCCGGCG CAACCCCCGCCCCAGCCGCACCCACCGCCGCCCCAGCAGCAGCACAAGGAAGAGATGGCG GCCGAGGCTGGGGAAGCCGTGGCGTCCCCCATGGACGACGGGTTTGTGAGCCTGGACTCG CCCTCCTATGTCCTGTACAGGGACAGAGCAGAATGGGCTGATATAGATCCGGTGCCGCAG AATGATGGCCCCAATCCCGTGGTCCAGATCATTTATAGTGACAAATTTAGAGATGTTTAT GATTACTTCCGAGCTGTCCTGCAGCGTGATGAAAGAAGTGAACGAGCTTTTAAGCTAACC CGGGATGCTATTGAGTTAAATGCAGCCAATTATACAGTGTGGCATTTCCGGAGAGTTCTT TTGAAGTCACTTCAGAAGGATCTACATGAGGAAATGAACTACATCACTGCAATAATTGAG GAGCAGCCCAAAAACTATCAAGTTTGGCATCATAGGCGAGTATTAGTGGAATGGCTAAGA GATCCATCTCAGGAGCTTGAATTTATTGCTGATATTCTTAATCAGGATGCAAAGAATTAT CATGCCTGGCAGCATCGACAATGGGTTATTCAGGAATTTAAACTTTGGGATAATGAGCTG CAGTATGTGGACCAACTTCTGAAAGAGGATGTGAGAAATAACTCTGTCTGGAACCAAAGA TACTTCGTTATTTCTAACACCACTGGCTACAATGATCGTGCTGTATTGGAGAGAGAAGTC CAATACACTCTGGAAATGATTAAACTAGTACCACATAATGAAAGTGCATGGAACTATTTG AAAGGGATTTTGCAGGATCGTGGTCTTTCCAAATATCCTAATCTGTTAAATCAATTACTT GATTTACAACCAAGTCATAGTTCCCCCTACCTAATTGCCTTTCTTGTGGATATCTATGAA GACATGCTAGAAAATCAGTGTGACAATAAGGAAGACATTCTTAATAAAGCATTAGAGTTA TGTGAAATCCTAGCTAAAGAAAAGGACACTATAAGAAAGGAATATTGGAGATACATTGGA AGATCCCTTCAAAGCAAACACAGCACAGAAAATGACTCACCAACAAATGTACAGCAATAA PF01239 PPTA function transferase activity function transferase activity, transferring alkyl or aryl (other than methyl) groups function prenyltransferase activity function protein prenyltransferase activity function catalytic activity process biopolymer modification process protein modification process protein amino acid lipidation process physiological process process protein prenylation process metabolism process protein amino acid prenylation process macromolecule metabolism process biopolymer metabolism BE0002372 Protein farnesyltransferase subunit beta Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Protein farnesyltransferase subunit beta Involved in catalytic activity Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding FNTB 14q23-q24 None 5.67 48774.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3785 GenAtlas FNTB GeneCards FNTB GenBank Gene Database L00635 UniProtKB P49356 UniProt Accession FNTB_HUMAN CAAX farnesyltransferase subunit beta EC 2.5.1.58 FTase-beta RAS proteins prenyltransferase beta >Protein farnesyltransferase subunit beta MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFS SYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ IVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQY LYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIG GVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCY SFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDF YHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPV PGFEELKDETSAEPATD >1314 bp ATGGCTTCTCCGAGTTCTTTCACCTACTATTGCCCTCCATCTTCCTCCCCCGTCTGGTCA GAGCCGCTGTACAGTCTGAGGCCCGAGCACGCGCGAGAGCGGTTGCAGGACGACTCGGTG GAAACAGTCACGTCCATAGAACAGGCAAAAGTAGAAGAAAAGATCCAAGAGGTCTTCAGT TCTTACAAGTTCAACCACCTTGTACCAAGGCTTGTTTTGCAGAGGGAGAAGCACTTCCAT TATCTGAAAAGAGGCCTTCGACAACTGACAGATGCCTATGAGTGTCTGGATGCCAGCCGC CCATGGCTCTGCTATTGGATCCTGCACAGCTTGGAACTGCTAGATGAACCCATCCCCCAG ATAGTGGCTACAGATGTGTGTCAGTTCCTGGAGCTGTGTCAGAGCCCAGAAGGTGGCTTT GGAGGAGGACCCGGTCAGTATCCACACCTTGCACCCACATATGCAGCAGTCAATGCATTG TGCATCATTGGCACCGAGGAGGCCTATGACATCATTAACAGAGAGAAGCTTCTTCAGTAT TTGTACTCCCTGAAGCAACCTGACGGCTCCTTTCTCATGCATGTCGGAGGTGAGGTGGAT GTGAGAAGCGCATACTGTGCTGCCTCCGTAGCCTCGCTGACCAACATCATCACTCCAGAC CTCTTTGAGGGCACTGCTGAATGGATAGCAAGGTGTCAGAACTGGGAAGGTGGCATTGGC GGGGTACCAGGGATGGAAGCCCATGGTGGCTATACCTTCTGTGGCCTGGCCGCGCTGGTA ATCCTCAAGAGGGAACGTTCCTTGAACTTGAAGAGCTTATTACAATGGGTGACAAGCCGG CAGATGCGATTTGAAGGAGGATTTCAGGGCCGCTGCAACAAGCTGGTGGATGGCTGCTAC TCCTTCTGGCAGGCGGGGCTCCTGCCCCTGCTCCACCGCGCACTGCACGCCCAAGGTGAC CCTGCCCTTAGCATGAGCCACTGGATGTTCCATCAGCAGGCCCTGCAGGAGTACATCCTG ATGTGCTGCCAGTGCCCTGCGGGGGGGCTTCTGGATAAACCTGGCAAGTCGCGTGATTTC TACCACACCTGCTACTGCCTGAGCGGCCTGTCCATAGCCCAGCACTTCGGCAGCGGAGCC ATGTTGCATGATGTGGTCCTGGGTGTGCCCGAAAACGCTCTGCAGCCCACTCACCCAGTG TACAACATTGGACCAGACAAGGTGATCCAGGCCACTACATACTTTCTACAGAAGCCAGTC CCAGGTTTTGAGGAGCTTAAGGATGAGACATCGGCAGAGCCTGCAACCGACTAG PF00432 Prenyltrans function catalytic activity "
drug:(11S)-8-CHLORO-11-[1-(METHYLSULFONYL)PIPERIDIN-4-YL]-6-PIPERAZIN-1-YL-11H-BENZO[5,6]CYCLOHEPTA[1,2-B]PYRIDINErdfs:label"(11S)-8-CHLORO-11-[1-(METHYLSULFONYL)PIPERIDIN-4-YL]-6-PIPERAZIN-1-YL-11H-BENZO[5,6]CYCLOHEPTA[1,2-B]PYRIDINE"
drug:(11S)-8-CHLORO-11-[1-(METHYLSULFONYL)PIPERIDIN-4-YL]-6-PIPERAZIN-1-YL-11H-BENZO[5,6]CYCLOHEPTA[1,2-B]PYRIDINErdf:typedrugbank:drugs
drug:(11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dionedrugbank:description" experimental This compound belongs to the gluco/mineralocorticoids, progestogins and derivatives. These are steroids whose structure is based on an hydroxylated prostane moiety. Gluco/mineralocorticoids, Progestogins and Derivatives Organic Compounds Lipids Steroids and Steroid Derivatives Gluco/mineralocorticoids, Progestogins and Derivatives Ketosteroids Hydroxysteroids Cyclohexanols Tertiary Alcohols Ketones Cyclic Alcohols and Derivatives Enolates Polyamines Primary Alcohols Aldehydes 3-keto-steroid 11-hydroxy-steroid 17-hydroxy-steroid 20-keto-steroid cyclohexanol tertiary alcohol cyclic alcohol secondary alcohol ketone primary alcohol enolate polyamine alcohol carbonyl group aldehyde logP 1.79 ALOGPS logS -3.3 ALOGPS Water Solubility 1.99e-01 g/l ALOGPS logP 1.28 ChemAxon IUPAC Name (1S,2R,10S,11S,14R,15S,17S)-14,17-dihydroxy-14-(2-hydroxyacetyl)-2,15-dimethyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadec-6-en-5-one ChemAxon Traditional IUPAC Name hydrocortisone ChemAxon Molecular Weight 362.4599 ChemAxon Monoisotopic Weight 362.20932407 ChemAxon SMILES [H][C@@]12CC[C@](O)(C(=O)CO)[C@@]1(C)C[C@]([H])(O)[C@@]1([H])[C@@]2([H])CCC2=CC(=O)CC[C@]12C ChemAxon Molecular Formula C21H30O5 ChemAxon InChI InChI=1S/C21H30O5/c1-19-7-5-13(23)9-12(19)3-4-14-15-6-8-21(26,17(25)11-22)20(15,2)10-16(24)18(14)19/h9,14-16,18,22,24,26H,3-8,10-11H2,1-2H3/t14-,15-,16-,18+,19-,20-,21-/m0/s1 ChemAxon InChIKey InChIKey=JYGXADMDTFJGBT-VWUMJDOOSA-N ChemAxon Polar Surface Area (PSA) 94.83 ChemAxon Refractivity 97.4 ChemAxon Polarizability 39.55 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 12.58 ChemAxon pKa (strongest basic) -2.8 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5754 PubChem Substance 99444357 ChemSpider 5551 PDB HCY BE0000209 Corticosteroid-binding globulin Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Corticosteroid-binding globulin Involved in serine-type endopeptidase inhibitor activity Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species SERPINA6 14q32.1 Secreted protein None 5.94 45141.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1540 GenAtlas SERPINA6 GeneCards SERPINA6 GenBank Gene Database J02943 GenBank Protein Database 179971 UniProtKB P08185 UniProt Accession CBG_HUMAN CBG Corticosteroid-binding globulin precursor Serpin A6 Transcortin >Corticosteroid-binding globulin precursor MPLLLYTCLLWLPTSGLWTVQAMDPNAAYVNMSNHHRGLASANVDFAFSLYKHLVALSPK KNIFISPVSISMALAMLSLGTCGHTRAQLLQGLGFNLTERSETEIHQGFQHLHQLFAKSD TSLEMTMGNALFLDGSLELLESFSADIKHYYESEVLAMNFQDWATASRQINSYVKNKTQG KIVDLFSGLDSPAILVLVNYIFFKGTWTQPFDLASTREENFYVDETTVVKVPMMLQSSTI SYLHDSELPCQLVQMNYVGNGTVFFILPDKGKMNTVIAALSRDTINRWSAGLTSSQVDLY IPKVTISGVYDLGDVLEEMGIADLFTNQANFSRITQDAQLKSSKVVHKAVLQLNEEGVDT AGSTGVTLNLTSKPIILRFNQPFIIMIFDHFTWSSLFLARVMNPV >1218 bp ATGCCACTCCTCCTGTACACCTGTCTTCTCTGGCTGCCCACCAGCGGCCTCTGGACCGTC CAGGCCATGGATCCTAACGCTGCTTATGTGAACATGAGTAACCATCACCGGGGCCTGGCT TCAGCCAACGTTGACTTTGCCTTCAGCCTGTATAAGCACCTAGTGGCCTTGAGTCCCAAA AAGAACATTTTCATCTCCCCTGTGAGCATCTCCATGGCCTTAGCTATGCTGTCCCTGGGC ACCTGTGGCCACACACGGGCCCAGCTTCTCCAGGGCCTGGGTTTCAACCTCACTGAGAGG TCTGAGACTGAGATCCACCAGGGTTTCCAGCACCTGCACCAACTCTTTGCAAAGTCAGAC ACCAGCTTAGAAATGACTATGGGCAATGCCTTGTTTCTTGATGGCAGCCTGGAGTTGCTG GAGTCATTCTCAGCAGACATCAAGCACTACTATGAGTCAGAGGTCTTGGCTATGAATTTC CAGGACTGGGCAACAGCCAGCAGACAGATCAACAGCTATGTCAAGAATAAGACACAGGGG AAAATTGTCGACTTGTTTTCAGGGCTGGATAGCCCAGCCATCCTCGTCCTGGTCAACTAT ATCTTCTTCAAAGGCACATGGACACAGCCCTTTGACCTGGCAAGCACCAGGGAGGAGAAC TTCTATGTGGACGAGACAACTGTGGTGAAGGTGCCCATGATGTTGCAGTCGAGCACCATC AGTTACCTTCATGACTCAGAGCTCCCCTGCCAGCTGGTGCAGATGAACTACGTGGGCAAT GGGACTGTCTTCTTCATCCTTCCGGACAAGGGGAAGATGAACACAGTCATCGCTGCACTG AGCCGGGACACGATTAACAGGTGGTCCGCAGGCCTGACCAGCAGCCAGGTGGACCTGTAC ATTCCAAAGGTCACCATCTCTGGAGTCTATGACCTTGGAGATGTGCTGGAGGAAATGGGC ATTGCAGACTTGTTCACCAACCAGGCAAATTTCTCACGCATCACCCAGGACGCCCAGCTG AAGTCATCAAAGGTGGTCCATAAAGCTGTGCTGCAACTCAATGAGGAGGGTGTGGACACA GCTGGCTCCACTGGGGTCACCCTAAACCTGACGTCCAAGCCTATCATCTTGCGTTTCAAC CAGCCCTTCATCATCATGATCTTCGACCACTTCACCTGGAGCAGCCTTTTCCTGGCGAGG GTTATGAACCCAGTGTAA PF00079 Serpin function enzyme inhibitor activity function protease inhibitor activity function endopeptidase inhibitor activity function serine-type endopeptidase inhibitor activity function enzyme regulator activity "
drug:(11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dionerdfs:label"(11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione"
drug:(11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dionerdf:typedrugbank:drugs
drug:(13R,15S)-13-METHYL-16-OXA-8,9,12,22,24-PENTAAZAHEXACYCLO[15.6.2.16,9.1,12,15.0,2,7.0,21,25]HEPTACOSA-1(24),2,4,6,17(25),18,20-HEPTAENE-23,26-DIONEdrugbank:description" experimental This compound belongs to the quinoxalines. These are compounds containing a quinoxaline moiety, a bicyclic heterocycle made up of a benzene ring fused to a pyrazine ring. Quinoxalines Organic Compounds Heterocyclic Compounds Naphthyridines Quinoxalines Indazoles Alkyl Aryl Ethers Pyrazines Pyrazolones Benzene and Substituted Derivatives Pyrazoles Pyrrolidines Tertiary Amines Polyamines alkyl aryl ether benzene pyrazolinone pyrazine pyrrolidine pyrazole azole tertiary amine ether polyamine amine organonitrogen compound logP 1.86 ALOGPS logS -3.1 ALOGPS Water Solubility 3.35e-01 g/l ALOGPS logP 2.14 ChemAxon IUPAC Name (13R,15S)-13-methyl-16-oxa-8,9,12,22,24-pentaazahexacyclo[15.6.2.1^{6,9}.1^{12,15}.0^{2,7}.0^{21,25}]heptacosa-1(24),2(7),3,5,17(25),18,20-heptaene-23,27-dione ChemAxon Traditional IUPAC Name (13R,15S)-13-methyl-16-oxa-8,9,12,22,24-pentaazahexacyclo[15.6.2.1^{6,9}.1^{12,15}.0^{2,7}.0^{21,25}]heptacosa-1(24),2(7),3,5,17(25),18,20-heptaene-23,27-dione ChemAxon Molecular Weight 403.4338 ChemAxon Monoisotopic Weight 403.164439563 ChemAxon SMILES [H][C@]12CN(CCN3NC4=C(C=CC=C4C3=O)C3=NC4=C(NC3=O)C=CC=C4O1)[C@]([H])(C)C2 ChemAxon Molecular Formula C22H21N5O3 ChemAxon InChI InChI=1S/C22H21N5O3/c1-12-10-13-11-26(12)8-9-27-22(29)15-5-2-4-14(18(15)25-27)19-21(28)23-16-6-3-7-17(30-13)20(16)24-19/h2-7,12-13,25H,8-11H2,1H3,(H,23,28)/t12-,13+/m1/s1 ChemAxon InChIKey InChIKey=KBLPHMRCKHFBJB-OLZOCXBDSA-N ChemAxon Polar Surface Area (PSA) 86.27 ChemAxon Refractivity 116.32 ChemAxon Polarizability 42.01 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 8.26 ChemAxon pKa (strongest basic) 7.01 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 6 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 16046126 PubChem Substance 99443359 ChemSpider 13174538 PDB 1CD BE0001072 Cyclin-dependent kinase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cyclin-dependent kinase 2 Involved in protein kinase activity ATP + a protein = ADP + a phosphoprotein CDK2deltaT None 9.76 30061.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1771 GenAtlas CDK2deltaT GeneCards CDK2deltaT GenBank Gene Database AB012305 GenBank Protein Database 3551191 UniProtKB P24941 UniProt Accession CDK2_HUMAN EC 2.7.11.22 p33 protein kinase >Cell division protein kinase 2 MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL >897 bp ATGGAGAACTTCCAAAAGGTGGAAAAGATCGGAGAGGGCACGTACGGAGTTGTGTACAAA GCCAGAAACAAGTTGACGGGAGAGGTGGTGGCGCTTAAGAAAATCCGCCTGGACACTGAG ACTGAGGGTGTGCCCAGTACTGCCATCCGAGAGATCTCTCTGCTTAAGGAGCTTAACCAT CCTAATATTGTCAAGCTGCTGGATGTCATTCACACAGAAAATAAACTCTACCTGGTTTTT GAATTTCTGCACCAAGATCTCAAGAAATTCATGGATGCCTCTGCTCTCACTGGCATTCCT CTTCCCCTCATCAAGAGCTATCTGTTCCAGCTGCTCCAGGGCCTAGCTTTCTGCCATTCT CATCGGGTCCTCCACCGAGACCTTAAACCTCAGAATCTGCTTATTAACACAGAGGGGGCC ATCAAGCTAGCAGACTTTGGACTAGCCAGAGCTTTTGGAGTCCCTGTTCGTACTTACACC CATGAGGTGGTGACCCTGTGGTACCGAGCTCCTGAAATCCTCCTGGGCTCGAAATATTAT TCCACAGCTGTGGACATCTGGAGCCTGGGCTGCATCTTTGCTGAGATGGTGACTCGCCGG GCCCTGTTCCCTGGAGATTCTGAGATTGACCAGCTCTTCCGGATCTTTCGGACTCTGGGG ACCCCAGATGAGGTGGTGTGGCCAGGAGTTACTTCTATGCCTGATTACAAGCCAAGTTTC CCCAAGTGGGCCCGGCAAGATTTTAGTAAAGTTGTACCTCCCCTGGATGAAGATGGACGG AGCTTGTTATCGCAAATGCTGCACTACGACCCTAACAAGCGGATTTCGGCCAAGGCAGCC CTGGCTCACCCTTTCTTCCAGGATGTGACCAAGCCAGTACCCCATCTTCGACTCTGA PF00069 Pkinase function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism "
drug:(13R,15S)-13-METHYL-16-OXA-8,9,12,22,24-PENTAAZAHEXACYCLO[15.6.2.16,9.1,12,15.0,2,7.0,21,25]HEPTACOSA-1(24),2,4,6,17(25),18,20-HEPTAENE-23,26-DIONErdfs:label"(13R,15S)-13-METHYL-16-OXA-8,9,12,22,24-PENTAAZAHEXACYCLO[15.6.2.16,9.1,12,15.0,2,7.0,21,25]HEPTACOSA-1(24),2,4,6,17(25),18,20-HEPTAENE-23,26-DIONE"
drug:(13R,15S)-13-METHYL-16-OXA-8,9,12,22,24-PENTAAZAHEXACYCLO[15.6.2.16,9.1,12,15.0,2,7.0,21,25]HEPTACOSA-1(24),2,4,6,17(25),18,20-HEPTAENE-23,26-DIONErdf:typedrugbank:drugs
drug:(13S)-13-METHYLDODECAHYDRO-1H-CYCLOPENTA[A]PHENANTHRENE-3,17(2H,4H)-DIONEdrugbank:description" experimental This compound belongs to the ketosteroids. These are steroid derivatives comprising a ketone group attached to steroid skeleton. Ketosteroids Organic Compounds Lipids Steroids and Steroid Derivatives Ketosteroids Estrogens and Derivatives Cyclohexanones Polyamines cyclohexanone ketone polyamine carbonyl group logP 3.2 ALOGPS logS -4.5 ALOGPS Water Solubility 8.79e-03 g/l ALOGPS logP 3.67 ChemAxon IUPAC Name (1R,2S,7S,10R,11S,15S)-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadecane-5,14-dione ChemAxon Traditional IUPAC Name (1R,2S,7S,10R,11S,15S)-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadecane-5,14-dione ChemAxon Molecular Weight 274.3978 ChemAxon Monoisotopic Weight 274.193280076 ChemAxon SMILES C[C@]12CC[C@H]3[C@@H](CC[C@H]4CC(=O)CC[C@H]34)[C@@H]1CCC2=O ChemAxon Molecular Formula C18H26O2 ChemAxon InChI InChI=1S/C18H26O2/c1-18-9-8-14-13-5-3-12(19)10-11(13)2-4-15(14)16(18)6-7-17(18)20/h11,13-16H,2-10H2,1H3/t11-,13-,14+,15+,16-,18-/m0/s1 ChemAxon InChIKey InChIKey=CRDKSBHJIGNEOH-IMRIKWHGSA-N ChemAxon Polar Surface Area (PSA) 34.14 ChemAxon Refractivity 78.31 ChemAxon Polarizability 32.21 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest acidic) 19.96 ChemAxon pKa (strongest basic) -7.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5288172 PubChem Substance 46506451 PDB ESR BE0001607 Steroid Delta-isomerase Comamonas testosteroni unknown Steroid Delta-isomerase Involved in steroid delta-isomerase activity A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)- steroid ksi None 5.13 13398.0 Comamonas testosteroni GenBank Gene Database M22749 GenBank Protein Database 151322 UniProtKB P00947 UniProt Accession SDIS_COMTE Delta(5)-3-ketosteroid isomerase EC 5.3.3.1 >Steroid Delta-isomerase MNTPEHMTAVVQRYVAALNAGDLDGIVALFADDATVEDPVGSEPRSGTAAIREFYANSLK LPLAVELTQEVRAVANEAAFAFTVSFEYQGRKTVVAPIDHFRFNGAGKVVSMRALFGEKN IHAGA >378 bp ATGAATACCCCAGAACATATGACCGCCGTGGTACAGCGCTATGTGGCTGCGCTCAATGCC GGCGATCTGGACGGCATCGTCGCGCTGTTTGCCGATGACGCCACGGTGGAAGACCCCGTG GGTTCCGAGCCCAGGTCCGGTACGGCTGCGATTCGTGAGTTTTACGCCAACTCGCTCAAA CTGCCTTTGGCGGTGGAGCTGACGCAGGAGGTACGCGCGGTCGCCAACGAAGCGGCCTTC GCTTTCACCGTCAGCTTCGAGTATCAGGGCCGCAAGACCGTGGTTGCGCCCATCGATCAC TTTCGCTTCAATGGCGCCGGCAAGGTGGTGAGCATGCGCGCCTTGTTTGGCGAGAAGAAT ATTCACGCTGGCGCCTGA PF02136 NTF2 component cell component intracellular function catalytic activity function transporter activity function isomerase activity function intramolecular oxidoreductase activity function intramolecular oxidoreductase activity, transposing C=C bonds function steroid delta-isomerase activity process transport process physiological process process cellular physiological process "
drug:(13S)-13-METHYLDODECAHYDRO-1H-CYCLOPENTA[A]PHENANTHRENE-3,17(2H,4H)-DIONErdfs:label"(13S)-13-METHYLDODECAHYDRO-1H-CYCLOPENTA[A]PHENANTHRENE-3,17(2H,4H)-DIONE"
drug:(13S)-13-METHYLDODECAHYDRO-1H-CYCLOPENTA[A]PHENANTHRENE-3,17(2H,4H)-DIONErdf:typedrugbank:drugs
drug:(16ALPHA,17ALPHA)-ESTRA-1,3,5(10)-TRIENE-3,16,17-TRIOLdrugbank:description" experimental This compound belongs to the hydroxysteroids. These are compounds containing an steroid backbone, with at least one hydrogen substituted by an hydroxyl group. Hydroxysteroids Organic Compounds Lipids Steroids and Steroid Derivatives Hydroxysteroids Phenanthrenes and Derivatives Tetralins Phenols and Derivatives 1,2-Diols Secondary Alcohols Cyclic Alcohols and Derivatives Enols Polyamines phenanthrene tetralin phenol derivative benzene cyclic alcohol secondary alcohol 1,2-diol polyol polyamine enol alcohol logP 2.54 ALOGPS logS -3.4 ALOGPS Water Solubility 1.19e-01 g/l ALOGPS logP 2.67 ChemAxon IUPAC Name (1S,10R,11S,13R,14S,15S)-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadeca-2,4,6-triene-5,13,14-triol ChemAxon Traditional IUPAC Name 17-epiestriol ChemAxon Molecular Weight 288.3814 ChemAxon Monoisotopic Weight 288.172544634 ChemAxon SMILES [H][C@@]1(O)C[C@@]2([H])[C@]3([H])CCC4=CC(O)=CC=C4[C@@]3([H])CC[C@]2(C)[C@]1([H])O ChemAxon Molecular Formula C18H24O3 ChemAxon InChI InChI=1S/C18H24O3/c1-18-7-6-13-12-5-3-11(19)8-10(12)2-4-14(13)15(18)9-16(20)17(18)21/h3,5,8,13-17,19-21H,2,4,6-7,9H2,1H3/t13-,14-,15+,16-,17-,18+/m1/s1 ChemAxon InChIKey InChIKey=PROQIPRRNZUXQM-PNVOZDDCSA-N ChemAxon Polar Surface Area (PSA) 60.69 ChemAxon Refractivity 81.27 ChemAxon Polarizability 32.97 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 10.33 ChemAxon pKa (strongest basic) -3.2 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 256737 PubChem Substance 99444173 ChemSpider 225189 PDB E3O BE0004057 Nuclear receptor coactivator 5 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Nuclear receptor coactivator 5 Translation, ribosomal structure and biogenesis Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC/c-myc in response to 17-beta-estradiol (E2) NCOA5 20q12-q13.12 Nucleus None 9.93 65535.8 Human HUGO Gene Nomenclature Committee (HGNC) GNC:15909 GeneCards NCOA5 GenBank Gene Database AF230533 GenBank Protein Database 11526821 UniProtKB Q9HCD5 UniProt Accession NCOA5_HUMAN CIA Coactivator independent of AF-2 NCoA-5 >Nuclear receptor coactivator 5 MNTAPSRPSPTRRDPYGFGDSRDSRRDRSPIRGSPRREPRDGRNGRDARDSRDIRDPRDL RDHRHSRDLRDHRDSRSVRDVRDVRDLRDFRDLRDSRDFRDQRDPMYDRYRDMRDSRDPM YRREGSYDRYLRMDDYCRRKDDSYFDRYRDSFDGRGPPGPESQSRAKERLKREERRREEL YRQYFEEIQRRFDAERPVDCSVIVVNKQTKDYAESVGRKVRDLGMVVDLIFLNTEVSLSQ ALEDVSRGGSPFAIVITQQHQIHRSCTVNIMFGTPQEHRNMPQADAMVLVARNYERYKNE CREKEREEIARQAAKMADEAILQERERGGPEEGVRGGHPPAIQSLINLLADNRYLTAEET DKIINYLRERKERLMRSSTDSLPGPISRQPLGATSGASLKTQPSSQPLQSGQVLPSATPT PSAPPTSQQELQAKILSLFNSGTVTANSSSASPSVAAGNTPNQNFSTAANSQPQQRSQAS GNQPPSILGQGGSAQNMGPRPGAPSQGLFGQPSSRLAPASNMTSQRPVSSTGINFDNPSV QKALDTLIQSGPALSHLVSQTTAQMGQPQAPMGSYQRHY BE0000792 Estrogen receptor beta Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Estrogen receptor beta Involved in transcription factor activity Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA- binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual ESR2 14q23.2 Nucleus None 8.55 59217.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3468 GenAtlas ESR2 GeneCards ESR2 GenBank Gene Database AB006590 GenBank Protein Database 2911152 IUPHAR 621 Guide to Pharmacology 107 UniProtKB Q92731 UniProt Accession ESR2_HUMAN ER-beta >Estrogen receptor beta MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPS NVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVN RETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGH NDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLH CAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTK LADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDL VLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDA DSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMK CKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ >1593 bp ATGGATATAAAAAACTCACCATCTAGCCTTAATTCTCCTTCCTCCTACAACTGCAGTCAA TCCATCTTACCCCTGGAGCACGGCTCCATATACATACCTTCCTCCTATGTAGACAGCCAC CATGAATATCCAGCCATGACATTCTATAGCCCTGCTGTGATGAATTACAGCATTCCCAGC AATGTCACTAACTTGGAAGGTGGGCCTGGTCGGCAGACCACAAGCCCAAATGTGTTGTGG CCAACACCTGGGCACCTTTCTCCTTTAGTGGTCCATCGCCAGTTATCACATCTGTATGCG GAACCTCAAAAGAGTCCCTGGTGTGAAGCAAGATCGCTAGAACACACCTTACCTGTAAAC AGAGAGACACTGAAAAGGAAGGTTAGTGGGAACCGTTGCGCCAGCCCTGTTACTGGTCCA GGTTCAAAGAGGGATGCTCACTTCTGCGCTGTCTGCAGCGATTACGCATCGGGATATCAC TATGGAGTCTGGTCGTGTGAAGGATGTAAGGCCTTTTTTAAAAGAAGCATTCAAGGACAT AATGATTATATTTGTCCAGCTACAAATCAGTGTACAATCGATAAAAACCGGCGCAAGAGC TGCCAGGCCTGCCGACTTCGGAAGTGTTACGAAGTGGGAATGGTGAAGTGTGGCTCCCGG AGAGAGAGATGTGGGTACCGCCTTGTGCGGAGACAGAGAAGTGCCGACGAGCAGCTGCAC TGTGCCGGCAAGGCCAAGAGAAGTGGCGGCCACGCGCCCCGAGTGCGGGAGCTGCTGCTG GACGCCCTGAGCCCCGAGCAGCTAGTGCTCACCCTCCTGGAGGCTGAGCCGCCCCATGTG CTGATCAGCCGCCCCAGTGCGCCCTTCACCGAGGCCTCCATGATGATGTCCCTGACCAAG TTGGCCGACAAGGAGTTGGTACACATGATCAGCTGGGCCAAGAAGATTCCCGGCTTTGTG GAGCTCAGCCTGTTCGACCAAGTGCGGCTCTTGGAGAGCTGTTGGATGGAGGTGTTAATG ATGGGGCTGATGTGGCGCTCAATTGACCACCCCGGCAAGCTCATCTTTGCTCCAGATCTT GTTCTGGACAGGGATGAGGGGAAATGCGTAGAAGGAATTCTGGAAATCTTTGACATGCTC CTGGCAACTACTTCAAGGTTTCGAGAGTTAAAACTCCAACACAAAGAATATCTCTGTGTC AAGGCCATGATCCTGCTCAATTCCAGTATGTACCCTCTGGTCACAGCGACCCAGGATGCT GACAGCAGCCGGAAGCTGGCTCACTTGCTGAACGCCGTGACCGATGCTTTGGTTTGGGTG ATTGCCAAGAGCGGCATCTCCTCCCAGCAGCAATCCATGCGCCTGGCTAACCTCCTGATG CTCCTGTCCCACGTCAGGCATGCGAGTAACAAGGGCATGGAACATCTGCTCAACATGAAG TGCAAAAATGTGGTCCCAGTGTATGACCTGCTGCTGGAGATGCTGAATGCCCACGTGCTT CGCGGGTGCAAGTCCTCCATCACGGGGTCCGAGTGCAGCCCGGCAGAGGACAGTAAAAGC AAAGAGGGCTCCCAGAACCCACAGTCTCAGTGA PF00104 Hormone_recep PF00105 zf-C4 component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function ion binding function transcription factor activity function steroid binding function cation binding function ligand-dependent nuclear receptor activity function transition metal ion binding function DNA binding function zinc ion binding function signal transducer activity function receptor activity function nucleic acid binding function binding function steroid hormone receptor activity process regulation of biological process process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent "
drug:(16ALPHA,17ALPHA)-ESTRA-1,3,5(10)-TRIENE-3,16,17-TRIOLrdfs:label"(16ALPHA,17ALPHA)-ESTRA-1,3,5(10)-TRIENE-3,16,17-TRIOL"
drug:(16ALPHA,17ALPHA)-ESTRA-1,3,5(10)-TRIENE-3,16,17-TRIOLrdf:typedrugbank:drugs
drug:(17beta)-17-(cyanomethyl)-2-methoxyestra-1(10),2,4-trien-3-yl sulfamatedrugbank:description" experimental This compound belongs to the steroids and steroid derivatives. These are compounds based on the cyclopenta[a]phenanthrene carbon skeleton, partially or completely hydrogenated; there are usually methyl groups at C-10 and C-13, and often an alkyl group at C-17. By extension, one or more bond scissions, ring expansions and/or ring contractions of the skeleton may have occurred. Steroids and Steroid Derivatives Organic Compounds Lipids Steroids and Steroid Derivatives Phenanthrenes and Derivatives Tetralins Anisoles Alkyl Aryl Ethers Organic Sulfites Sulfuric Acid Amide Esters Nitriles Polyamines phenanthrene tetralin anisole phenol ether alkyl aryl ether benzene sulfuric acid amide ester sulfuric acid derivative organic sulfite polyamine nitrile ether carbonitrile organonitrogen compound logP 3.9 ALOGPS logS -4.8 ALOGPS Water Solubility 6.59e-03 g/l ALOGPS logP 3.24 ChemAxon IUPAC Name (1S,10S,11S,14R,15R)-14-(cyanomethyl)-4-methoxy-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadeca-2,4,6-trien-5-yl sulfamate ChemAxon Traditional IUPAC Name (1S,10S,11S,14R,15R)-14-(cyanomethyl)-4-methoxy-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadeca-2,4,6-trien-5-yl sulfamate ChemAxon Molecular Weight 404.523 ChemAxon Monoisotopic Weight 404.176978084 ChemAxon SMILES [H][C@]1(CC#N)CC[C@@]2([H])[C@]3([H])CCC4=CC(OS(N)(=O)=O)=C(OC)C=C4[C@@]3([H])CC[C@]12C ChemAxon Molecular Formula C21H28N2O4S ChemAxon InChI InChI=1S/C21H28N2O4S/c1-21-9-7-15-16(18(21)6-4-14(21)8-10-22)5-3-13-11-20(27-28(23,24)25)19(26-2)12-17(13)15/h11-12,14-16,18H,3-9H2,1-2H3,(H2,23,24,25)/t14-,15+,16-,18+,21-/m1/s1 ChemAxon InChIKey InChIKey=NTSPHKOMJMBWOU-NNKXXINSSA-N ChemAxon Polar Surface Area (PSA) 102.41 ChemAxon Refractivity 106.17 ChemAxon Polarizability 44.39 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 10.5 ChemAxon pKa (strongest basic) -4.9 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11188898 PubChem Substance 99444067 ChemSpider 9363982 PDB CTF BE0000322 Carbonic anhydrase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Carbonic anhydrase 2 Inorganic ion transport and metabolism Reversible hydration of carbon dioxide CA2 8q22 Cytoplasm None 7.47 29115.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1373 GenAtlas CA2 GeneCards CA2 GenBank Gene Database M77181 GenBank Protein Database 179780 UniProtKB P00918 UniProt Accession CAH2_HUMAN CA-II Carbonate dehydratase II Carbonic anhydrase C Carbonic anhydrase II EC 4.2.1.1 >Carbonic anhydrase 2 SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILN NGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLV HWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPR GLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV DNWRPAQPLKNRQIKASFK >783 bp ATGTCCCATCACTGGGGGTACGGCAAACACAACGGACCTGAGCACTGGCATAAGGACTTC CCCATTGCCAAGGGAGAGCGCCAGTCCCCTGTTGACATCGACACTCATACAGCCAAGTAT GACCCTTCCCTGAAGCCCCTGTCTGTTTCCTATGATCAAGCAACTTCCCTGAGGATCCTC AACAATGGTCATGCTTTCAACGTGGAGTTTGATGACTCTCAGGACAAAGCAGTGCTCAAG GGAGGACCCCTGGATGGCACTTACAGATTGATTCAGTTTCACTTTCACTGGGGTTCACTT GATGGACAAGGTTCAGAGCATACTGTGGATAAAAAGAAATATGCTGCAGAACTTCACTTG GTTCACTGGAACACCAAATATGGGGATTTTGGGAAAGCTGTGCAGCAACCTGATGGACTG GCCGTTCTAGGTATTTTTTTGAAGGTTGGCAGCGCTAAACCGGGCCTTCAGAAAGTTGTT GATGTGCTGGATTCCATTAAAACAAAGGGCAAGAGTGCTGACTTCACTAACTTCGATCCT CGTGGCCTCCTTCCTGAATCCTTGGATTACTGGACCTACCCAGGCTCACTGACCACCCCT CCTCTTCTGGAATGTGTGACCTGGATTGTGCTCAAGGAACCCATCAGCGTCAGCAGCGAG CAGGTGTTGAAATTCCGTAAACTTAACTTCAATGGGGAGGGTGAACCCGAAGAACTGATG GTGGACAACTGGCGCCCAGCTCAGCCACTGAAGAACAGGCAAATCAAAGCTTCCTTCAAA TAA PF00194 Carb_anhydrase function lyase activity function ion binding function cation binding function transition metal ion binding function zinc ion binding function carbon-oxygen lyase activity function binding function hydro-lyase activity function carbonate dehydratase activity function catalytic activity process physiological process process one-carbon compound metabolism process metabolism process cellular metabolism "
drug:(17beta)-17-(cyanomethyl)-2-methoxyestra-1(10),2,4-trien-3-yl sulfamaterdfs:label"(17beta)-17-(cyanomethyl)-2-methoxyestra-1(10),2,4-trien-3-yl sulfamate"
drug:(17beta)-17-(cyanomethyl)-2-methoxyestra-1(10),2,4-trien-3-yl sulfamaterdf:typedrugbank:drugs
drug:(1E)-5-(1-piperidin-4-yl-3-pyridin-4-yl-1H-pyrazol-4-yl)-2,3-dihydro-1H-inden-1-one oximedrugbank:description" experimental This compound belongs to the phenylpyrazoles. These are compounds containing a phenylpyrazole skeleton, which consists of a pyrazole bound to a phenyl group. Phenylpyrazoles Organic Compounds Heterocyclic Compounds Azoles Pyrazoles Indanes Aminopiperidines Pyridines and Derivatives Benzene and Substituted Derivatives Oximes Polyamines Dialkylamines indane 4-aminopiperidine benzene pyridine piperidine oxime secondary aliphatic amine polyamine secondary amine amine organonitrogen compound logP 2.39 ALOGPS logS -4 ALOGPS Water Solubility 3.87e-02 g/l ALOGPS logP 1.15 ChemAxon IUPAC Name N-[(1E)-5-[1-(piperidin-4-yl)-3-(pyridin-4-yl)-1H-pyrazol-4-yl]-2,3-dihydro-1H-inden-1-ylidene]hydroxylamine ChemAxon Traditional IUPAC Name N-[(1E)-5-[1-(piperidin-4-yl)-3-(pyridin-4-yl)pyrazol-4-yl]-2,3-dihydroinden-1-ylidene]hydroxylamine ChemAxon Molecular Weight 373.4509 ChemAxon Monoisotopic Weight 373.190260383 ChemAxon SMILES O\N=C1/CCC2=CC(=CC=C12)C1=CN(N=C1C1=CC=NC=C1)C1CCNCC1 ChemAxon Molecular Formula C22H23N5O ChemAxon InChI InChI=1S/C22H23N5O/c28-26-21-4-2-16-13-17(1-3-19(16)21)20-14-27(18-7-11-24-12-8-18)25-22(20)15-5-9-23-10-6-15/h1,3,5-6,9-10,13-14,18,24,28H,2,4,7-8,11-12H2/b26-21+ ChemAxon InChIKey InChIKey=KWEFZSZCLBHIEQ-YYADALCUSA-N ChemAxon Polar Surface Area (PSA) 75.33 ChemAxon Refractivity 120.35 ChemAxon Polarizability 41.93 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 8.37 ChemAxon pKa (strongest basic) 10.13 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 5 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11653652 PubChem Substance 99445024 ChemSpider 9828390 PDB SM5 BE0000634 Serine/threonine-protein kinase B-raf Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Serine/threonine-protein kinase B-raf Involved in protein kinase activity Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May play a role in the postsynaptic responses of hippocampal neuron BRAF 7q34 Cytoplasm None 7.58 84438.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1097 GenAtlas BRAF GeneCards BRAF GenBank Gene Database M95712 GenBank Protein Database 41387220 UniProtKB P15056 UniProt Accession BRAF_HUMAN EC 2.7.11.1 p94 v-Raf murine sarcoma viral oncogene homolog B1 >B-Raf proto-oncogene serine/threonine-protein kinase MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEH IEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTV TSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDS LKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRK TFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPI PQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQR DRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSP GPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDV AVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHH LHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATV KSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNIN NRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARS LPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH >2301 bp ATGGCGGCGCTGAGCGGTGGCGGTGGTGGCGGCGCGGAGCCGGGCCAGGCTCTGTTCAAC GGGGACATGGAGCCCGAGGCCGGCGCCGGCGCCGGCGCCGCGGCCTCTTCGGCTGCGGAC CCTGCCATTCCGGAGGAGGTGTGGAATATCAAACAAATGATTAAGTTGACACAGGAACAT ATAGAGGCCCTATTGGACAAATTTGGTGGGGAGCATAATCCACCATCAATATATCTGGAG GCCTATGAAGAATACACCAGCAAGCTAGATGCACTCCAACAAAGAGAACAACAGTTATTG GAATCTCTGGGGAACGGAACTGATTTTTCTGTTTCTAGCTCTGCATCAATGGATACCGTT ACATCTTCTTCCTCTTCTAGCCTTTCAGTGCTACCTTCATCTCTTTCAGTTTTTCAAAAT CCCACAGATGTGGCACGGAGCAACCCCAAGTCACCACAAAAACCTATCGTTAGAGTCTTC CTGCCCAACAAACAGAGGACAGTGGTACCTGCAAGGTGTGGAGTTACAGTCCGAGACAGT CTAAAGAAAGCACTGATGATGAGAGGTCTAATCCCAGAGTGCTGTGCTGTTTACAGAATT CAGGATGGAGAGAAGAAACCAATTGGTTGGGACACTGATATTTCCTGGCTTACTGGAGAA GAATTGCATGTGGAAGTGTTGGAGAATGTTCCACTTACAACACACAACTTTGTACGAAAA ACGTTTTTCACCTTAGCATTTTGTGACTTTTGTCGAAAGCTGCTTTTCCAGGGTTTCCGC TGTCAAACATGTGGTTATAAATTTCACCAGCGTTGTAGTACAGAAGTTCCACTGATGTGT GTTAATTATGACCAACTTGATTTGCTGTTTGTCTCCAAGTTCTTTGAACACCACCCAATA CCACAGGAAGAGGCGTCCTTAGCAGAGACTGCCCTAACATCTGGATCATCCCCTTCCGCA CCCGCCTCGGACTCTATTGGGCCCCAAATTCTCACCAGTCCGTCTCCTTCAAAATCCATT CCAATTCCACAGCCCTTCCGACCAGCAGATGAAGATCATCGAAATCAATTTGGGCAACGA GACCGATCCTCATCAGCTCCCAATGTGCATATAAACACAATAGAACCTGTCAATATTGAT GACTTGATTAGAGACCAAGGATTTCGTGGTGATGGAGGATCAACCACAGGTTTGTCTGCT ACCCCCCCTGCCTCATTACCTGGCTCACTAACTAACGTGAAAGCCTTACAGAAATCTCCA GGACCTCAGCGAGAAAGGAAGTCATCTTCATCCTCAGAAGACAGGAATCGAATGAAAACA CTTGGTAGACGGGACTCGAGTGATGATTGGGAGATTCCTGATGGGCAGATTACAGTGGGA CAAAGAATTGGATCTGGATCATTTGGAACAGTCTACAAGGGAAAGTGGCATGGTGATGTG GCAGTGAAAATGTTGAATGTGACAGCACCTACACCTCAGCAGTTACAAGCCTTCAAAAAT GAAGTAGGAGTACTCAGGAAAACACGACATGTGAATATCCTACTCTTCATGGGCTATTCC ACAAAGCCACAACTGGCTATTGTTACCCAGTGGTGTGAGGGCTCCAGCTTGTATCACCAT CTCCATATCATTGAGACCAAATTTGAGATGATCAAACTTATAGATATTGCACGACAGACT GCACAGGGCATGGATTACTTACACGCCAAGTCAATCATCCACAGAGACCTCAAGAGTAAT AATATATTTCTTCATGAAGACCTCACAGTAAAAATAGGTGATTTTGGTCTAGCTACAGTG AAATCTCGATGGAGTGGGTCCCATCAGTTTGAACAGTTGTCTGGATCCATTTTGTGGATG GCACCAGAAGTCATCAGAATGCAAGATAAAAATCCATACAGCTTTCAGTCAGATGTATAT GCATTTGGGATTGTTCTGTATGAATTGATGACTGGACAGTTACCTTATTCAAACATCAAC AACAGGGACCAGATAATTTTTATGGTGGGACGAGGATACCTGTCTCCAGATCTCAGTAAG GTACGGAGTAACTGTCCAAAAGCCATGAAGAGATTAATGGCAGAGTGCCTCAAAAAGAAA AGAGATGAGAGACCACTCTTTCCCCAAATTCTCGCCTCTATTGAGCTGCTGGCCCGCTCA TTGCCAAAAATTCACCGCAGTGCATCAGAACCCTCCTTGAATCGGGCTGGTTTCCAAACA GAGGATTTTAGTCTATATGCTTGTGCTTCTCCAAAAACACCCATCCAGGCAGGGGGATAT GGTGCGTTTCCTGTCCACTGA PF00069 Pkinase PF00130 C1_1 PF02196 RBD function kinase activity function nucleotide binding function protein kinase activity function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function protein serine/threonine kinase activity function signal transducer activity function receptor signaling protein activity function catalytic activity function ATP binding function transferase activity, transferring phosphorus-containing groups process intracellular signaling cascade process protein amino acid phosphorylation process physiological process process cellular process process metabolism process cell communication process macromolecule metabolism process signal transduction process biopolymer metabolism process biopolymer modification process protein modification "
drug:(1E)-5-(1-piperidin-4-yl-3-pyridin-4-yl-1H-pyrazol-4-yl)-2,3-dihydro-1H-inden-1-one oximerdfs:label"(1E)-5-(1-piperidin-4-yl-3-pyridin-4-yl-1H-pyrazol-4-yl)-2,3-dihydro-1H-inden-1-one oxime"
drug:(1E)-5-(1-piperidin-4-yl-3-pyridin-4-yl-1H-pyrazol-4-yl)-2,3-dihydro-1H-inden-1-one oximerdf:typedrugbank:drugs
drug:(1R)-1,2,2-TRIMETHYLPROPYL (R)-METHYLPHOSPHINATEdrugbank:description" experimental This compound belongs to the polyamines. These are compounds containing more than one amine group. Polyamines Organic Compounds Organonitrogen Compounds Amines Polyamines logP 1.42 ALOGPS logS -1.9 ALOGPS Water Solubility 1.87e+00 g/l ALOGPS logP 1.67 ChemAxon IUPAC Name (2R)-3,3-dimethylbutan-2-yl methylphosphinate ChemAxon Traditional IUPAC Name (2R)-3,3-dimethylbutan-2-yl methylphosphinate ChemAxon Molecular Weight 164.1824 ChemAxon Monoisotopic Weight 164.0966163 ChemAxon SMILES [H][C@](C)(O[P@]([H])(C)=O)C(C)(C)C ChemAxon Molecular Formula C7H17O2P ChemAxon InChI InChI=1S/C7H17O2P/c1-6(7(2,3)4)9-10(5)8/h6,10H,1-5H3/t6-/m1/s1 ChemAxon InChIKey InChIKey=QZUGWOMGKDLYKO-ZCFIWIBFSA-N ChemAxon Polar Surface Area (PSA) 26.3 ChemAxon Refractivity 43 ChemAxon Polarizability 17.52 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest basic) -6.6 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937095 PubChem Substance 99444292 PDB GD7 BE0002705 Liver carboxylesterase 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Liver carboxylesterase 1 Lipid transport and metabolism Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl CoA ester CES1 16q13-q22.1 Endoplasmic reticulum None 6.58 62522.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1863 GenAtlas CES1 GenBank Gene Database M73499 UniProtKB P23141 UniProt Accession EST1_HUMAN ACAT Acyl coenzyme A:cholesterol acyltransferase Brain carboxylesterase hBr1 EC 3.1.1.1 Egasyn HMSE Liver carboxylesterase 1 precursor Monocyte/macrophage serine esterase Serine esterase 1 TGH Triacylglycerol hydrolase >Liver carboxylesterase 1 MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPL GPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLN IYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLF HRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLK MKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIP MQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDL IADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPF LKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLK DKEVAFWTNLFAKKAVEKPPQTEHIEL >1704 bp ATGTGGCTCCGTGCCTTTATCCTGGCCACTCTCTCTGCTTCCGCGGCTTGGGGGCATCCG TCCTCGCCACCTGTGGTGGACACCGTGCATGGCAAAGTGCTGGGGAAGTTCGTCAGCTTA GAAGGATTTGCACAGCCTGTGGCCATTTTCCTGGGAATCCCTTTTGCCAAGCCGCCTCTT GGACCCCTGAGGTTTACTCCACCGCAGCCTGCAGAACCATGGAGCTTTGTGAAGAATGCC ACCTCGTACCCTCCTATGTGCACCCAAGATCCCAAGGCGGGGCAGTTACTCTCAGAGCTA TTTACAAACCGAAAGGAGAACATTCCTCTCAAGCTTTCTGAAGACTGTCTTTACCTCAAT ATTTACACTCCTGCTGACTTGACCAAGAAAAACAGGCTGCCGGTGATGGTGTGGATCCAC GGAGGGGGGCTGATGGTGGGTGCGGCATCAACCTATGATGGGCTGGCCCTTGCTGCCCAT GAAAACGTGGTGGTGGTGACCATTCAATATCGCCTGGGCATCTGGGGATTCTTCAGCACA GGGGATGAACACAGCCGGGGGAACTGGGGTCACCTGGACCAGGTGGCTGCCCTGCGCTGG GTCCAGGACAACATTGCCAGCTTTGGAGGGAACCCAGGCTCTGTGACCATCTTTGGAGAG TCAGCGGGAGGAGAAAGTGTCTCTGTTCTTGTTTTGTCTCCATTGGCCAAGAACCTCTTC CACCGGGCCATTTCTGAGAGTGGCGTGGCCCTCACTTCTGTTCTGGTGAAGAAAGGTGAT GTCAAGCCCTTGGCTGAGCAAATTGCTATCACTGCTGGGTGCAAAACCACCACCTCTGCT GTCATGGTTCACTGCCTGCGACAGAAGACGGAAGAGGAGCTCTTGGAGACGACATTGAAA ATGAAATTCTTATCTCTGGACTTACAGGGAGACCCCAGAGAGAGTCAACCCCTTCTGGGC ACTGTGATTGATGGGATGCTGCTGCTGAAAACACCTGAAGAGCTTCAAGCTGAAAGGAAT TTCCACACTGTCCCCTACATGGTCGGAATTAACAAGCAGGAGTTTGGCTGGTTGATTCCA ATGCAGTTGATGAGCTATCCACTCTCCGAAGGGCAACTGGACCAGAAGACAGCCATGTCA CTCCTGTGGAAGTCCTATCCCCTTGTTTGCATTGCTAAGGAACTGATTCCAGAAGCCACT GAGAAATACTTAGGAGGAACAGACGACACTGTCAAAAAGAAAGACCTGTTCCTGGACTTG ATAGCAGATGTGATGTTTGGTGTCCCATCTGTGATTGTGGCCCGGAACCACAGAGATGCT GGAGCACCCACCTACATGTATGAGTTTCAGTACCGTCCAAGCTTCTCATCAGACATGAAA CCCAAGACGGTGATAGGAGACCACGGGGATGAGCTCTTCTCCGTCTTTGGGGCCCCATTT TTAAAAGAGGGTGCCTCAGAAGAGGAGATCAGACTTAGCAAGATGGTGATGAAATTCTGG GCCAACTTTGCTCGCAATGGAAACCCCAATGGGGAAGGGCTGCCCCACTGGCCAGAGTAC AACCAGAAGGAAGGGTATCTGCAGATTGGTGCCAACACCCAGGCGGCCCAGAAGCTGAAG GACAAAGAAGTAGCTTTCTGGACCAACCTCTTTGCCAAGAAGGCAGTGGAGAAGCCACCC CAGACAGAACACATAGAGCTGTGA PF00135 COesterase BE0004103 Platelet-activating factor acetylhydrolase IB subunit gamma Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Platelet-activating factor acetylhydrolase IB subunit gamma Involved in 1-alkyl-2-acetylglycerophosphocholine ester Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain PAFAH1B3 19q13.1 Cytoplasm None 6.84 25734.1 Human HUGO Gene Nomenclature Committee (HGNC) GNC:8576 GeneCards PAFAH1B3 GenBank Gene Database D63391 GenBank Protein Database 1122219 UniProtKB Q15102 UniProt Accession PA1B3_HUMAN PAF acetylhydrolase 29 kDa subunit PAF-AH 29 kDa subunit PAF-AH subunit gamma PAFAH subunit gamma >Platelet-activating factor acetylhydrolase IB subunit gamma MSGEENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRE LFSPLHALNFGIGGDGTQHVLWRLENGELEHIRPKIVVVWVGTNNHGHTAEQVTGGIKAI VQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGHPRAHFLDADPGFVH SDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGAPLLEPAP >696 bp ATGAGTGGAGAGGAGAACCCAGCCAGCAAGCCCACGCCGGTGCAGGACGTACAGGGCGAC GGGCGCTGGATGTCCCTGCACCATCGGTTCGTGGCTGACAGCAAAGATAAGGAACCCGAA GTCGTCTTCATCGGGGACTCCTTGGTCCAGCTCATGCACCAGTGCGAGATCTGGCGCGAG CTCTTCTCTCCTCTGCATGCACTTAACTTTGGCATTGGTGGTGACGGCACACAGCATGTA CTGTGGCGGCTGGAGAATGGGGAGCTGGAACACATCCGGCCCAAGATTGTGGTGGTCTGG GTGGGCACCAACAACCACGGACACACAGCAGAGCAGGTGACTGGTGGCATCAAGGCCATT GTGCAACTGGTGAATGAGCGACAGCCCCAGGCCCGGGTTGTGGTGCTGGGCCTGCTTCCG CGAGGCCAACATCCCAACCCACTTCGGGAGAAGAACCGACAGGTGAACGAGCTGGTACGG GCGGCACTGGCTGGCCACCCTCGGGCCCACTTCCTAGATGCCGACCCTGGCTTTGTGCAC TCAGATGGCACCATCAGCCATCATGACATGTATGATTACCTGCATCTGAGCCGCCTGGGC TACACACCTGTTTGCCGGGCTCTGCACTCCCTGCTTCTGCGTCTGCTGGCCCAAGACCAG GGCCAAGGTGCTCCCCTGCTGGAGCCCGCACCCTAA PF00657 Lipase_GDSL function hydrolase activity function hydrolase activity, acting on ester bonds function carboxylic ester hydrolase activity function lipase activity function catalytic activity process metabolism process primary metabolism process lipid metabolism process physiological process BE0002409 Platelet-activating factor acetylhydrolase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Platelet-activating factor acetylhydrolase Involved in catalytic activity Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids PLA2G7 6p21.2-p12 Secreted protein None 7.61 50078.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9040 GenAtlas PLA2G7 GenBank Gene Database U20157 UniProtKB Q13093 UniProt Accession PAFA_HUMAN 1-alkyl-2-acetylglycerophosphocholine esterase 2-acetyl-1-alkylglycerophosphocholine esterase EC 3.1.1.47 LDL-associated phospholipase A2 LDL-PLA(2) PAF 2-acylhydrolase PAF acetylhydrolase Platelet-activating factor acetylhydrolase precursor >Platelet-activating factor acetylhydrolase MVPPKLHVLFCLCGCLAVVYPFDWQYINPVAHMKSSAWVNKIQVLMAAASFGQTKIPRGN GPYSVGCTDLMFDHTNKGTFLRLYYPSQDNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNI LRLLFGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHR DRSASATYYFKDQSAAEIGDKSWLYLRTLKQEEETHIRNEQVRQRAKECSQALSLILDID HGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLSEDQRFRCGIALDAWMF PLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFA TGKIIGHMLKLKGDIDSNVAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENLIPGT NINTTNQHIMLQNSSGIEKYN >1326 bp ATGGTGCCACCCAAATTGCATGTGCTTTTCTGCCTCTGCGGCTGCCTGGCTGTGGTTTAT CCTTTTGACTGGCAATACATAAATCCTGTTGCCCATATGAAATCATCAGCATGGGTCAAC AAAATACAAGTACTGATGGCTGCTGCAAGCTTTGGCCAAACTAAAATCCCCCGGGGAAAT GGGCCTTATTCCGTTGGTTGTACAGACTTAATGTTTGATCACACTAATAAGGGCACCTTC TTGCGTTTATATTATCCATCCCAAGATAATGATCGCCTTGACACCCTTTGGATCCCAAAT AAAGAATATTTTTGGGGTCTTAGCAAATTTCTTGGAACACACTGGCTTATGGGCAACATT TTGAGGTTACTCTTTGGTTCAATGACAACTCCTGCAAACTGGAATTCCCCTCTGAGGCCT GGTGAAAAATATCCACTTGTTGTTTTTTCTCATGGTCTTGGGGCATTCAGGACACTTTAT TCTGCTATTGGCATTGACCTGGCATCTCATGGGTTTATAGTTGCTGCTGTAGAACACAGA GATAGATCTGCATCTGCAACTTACTATTTCAAGGACCAATCTGCTGCAGAAATAGGGGAC AAGTCTTGGCTCTACCTTAGAACCCTGAAACAAGAGGAGGAGACACATATACGAAATGAG CAGGTACGGCAAAGAGCAAAAGAATGTTCCCAAGCTCTCAGTCTGATTCTTGACATTGAT CATGGAAAGCCAGTGAAGAATGCATTAGATTTAAAGTTTGATATGGAACAACTGAAGGAC TCTATTGATAGGGAAAAAATAGCAGTAATTGGACATTCTTTTGGTGGAGCAACGGTTATT CAGACTCTTAGTGAAGATCAGAGATTCAGATGTGGTATTGCCCTGGATGCATGGATGTTT CCACTGGGTGATGAAGTATATTCCAGAATTCCTCAGCCCCTCTTTTTTATCAACTCTGAA TATTTCCAATATCCTGCTAATATCATAAAAATGAAAAAATGCTACTCACCTGATAAAGAA AGAAAGATGATTACAATCAGGGGTTCAGTCCACCAGAATTTTGCTGACTTCACTTTTGCA ACTGGCAAAATAATTGGACACATGCTCAAATTAAAGGGAGACATAGATTCAAATGTAGCT ATTGATCTTAGCAACAAAGCTTCATTAGCATTCTTACAAAAGCATTTAGGACTTCATAAA GATTTTGATCAGTGGGACTGCTTGATTGAAGGAGATGATGAGAATCTTATTCCAGGGACC AACATTAACACAACCAATCAACACATCATGTTACAGAACTCTTCAGGAATAGAGAAATAC AATTAG PF03403 PAF-AH_p_II component 2-acetyl-1-alkylglycerophosphocholine esterase complex component protein complex component unlocalized protein complex function catalytic activity function hydrolase activity function hydrolase activity, acting on ester bonds function carboxylic ester hydrolase activity function 1-alkyl-2-acetylglycerophosphocholine esterase activity process metabolism process primary metabolism process lipid metabolism process lipid catabolism process physiological process "
drug:(1R)-1,2,2-TRIMETHYLPROPYL (R)-METHYLPHOSPHINATErdfs:label"(1R)-1,2,2-TRIMETHYLPROPYL (R)-METHYLPHOSPHINATE"
drug:(1R)-1,2,2-TRIMETHYLPROPYL (R)-METHYLPHOSPHINATErdf:typedrugbank:drugs
drug:(1R)-1,2,2-TRIMETHYLPROPYL (S)-METHYLPHOSPHINATEdrugbank:description" experimental This compound belongs to the polyamines. These are compounds containing more than one amine group. Polyamines Organic Compounds Organonitrogen Compounds Amines Polyamines logP 1.42 ALOGPS logS -1.9 ALOGPS Water Solubility 1.87e+00 g/l ALOGPS logP 1.67 ChemAxon IUPAC Name (2R)-3,3-dimethylbutan-2-yl methylphosphinate ChemAxon Traditional IUPAC Name (2R)-3,3-dimethylbutan-2-yl methylphosphinate ChemAxon Molecular Weight 164.1824 ChemAxon Monoisotopic Weight 164.0966163 ChemAxon SMILES [H][C@](C)(O[P@@]([H])(C)=O)C(C)(C)C ChemAxon Molecular Formula C7H17O2P ChemAxon InChI InChI=1S/C7H17O2P/c1-6(7(2,3)4)9-10(5)8/h6,10H,1-5H3/t6-/m1/s1 ChemAxon InChIKey InChIKey=QZUGWOMGKDLYKO-ZCFIWIBFSA-N ChemAxon Polar Surface Area (PSA) 26.3 ChemAxon Refractivity 43 ChemAxon Polarizability 17.55 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest basic) -6.6 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937096 PubChem Substance 99444293 PDB GD8 BE0000426 Acetylcholinesterase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Acetylcholinesterase Lipid transport and metabolism Rapidly hydrolyzes choline released into the synapse ACHE 7q22 Cytoplasmic None 6.24 67797.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:108 GenAtlas ACHE GeneCards ACHE GenBank Gene Database M55040 GenBank Protein Database 177975 UniProtKB P22303 UniProt Accession ACES_HUMAN Acetylcholinesterase precursor AChE EC 3.1.1.7 >Acetylcholinesterase precursor MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN QFDHYSKQDRCSDL >1845 bp ATGAGGCCCCCGCAGTGTCTGCTGCACACGCCTTCCCTGGCTTCCCCACTCCTTCTCCTC CTCCTCTGGCTCCTGGGTGGAGGAGTGGGGGCTGAGGGCCGGGAGGATGCAGAGCTGCTG GTGACGGTGCGTGGGGGCCGGCTGCGGGGCATTCGCCTGAAGACCCCCGGGGGCCCTGTC TCTGCTTTCCTGGGCATCCCCTTTGCGGAGCCACCCATGGGACCCCGTCGCTTTCTGCCA CCGGAGCCCAAGCAGCCTTGGTCAGGGGTGGTAGACGCTACAACCTTCCAGAGTGTCTGC TACCAATATGTGGACACCCTATACCCAGGTTTTGAGGGCACCGAGATGTGGAACCCCAAC CGTGAGCTGAGCGAGGACTGCCTGTACCTCAACGTGTGGACACCATACCCCCGGCCTACA TCCCCCACCCCTGTCCTCGTCTGGATCTATGGGGGTGGCTTCTACAGTGGGGCCTCCTCC TTGGACGTGTACGATGGCCGCTTCTTGGTACAGGCCGAGAGGACTGTGCTGGTGTCCATG AACTACCGGGTGGGAGCCTTTGGCTTCCTGGCCCTGCCGGGGAGCCGAGAGGCCCCGGGC AATGTGGGTCTCCTGGATCAGAGGCTGGCCCTGCAGTGGGTGCAGGAGAACGTGGCAGCC TTCGGGGGTGACCCGACATCAGTGACGCTGTTTGGGGAGAGCGCGGGAGCCGCCTCGGTG GGCATGCACCTGCTGTCCCCGCCCAGCCGGGGCCTGTTCCACAGGGCCGTGCTGCAGAGC GGTGCCCCCAATGGACCCTGGGCCACGGTGGGCATGGGAGAGGCCCGTCGCAGGGCCACG CAGCTGGCCCACCTTGTGGGCTGTCCTCCAGGCGGCACTGGTGGGAATGACACAGAGCTG GTAGCCTGCCTTCGGACACGACCAGCGCAGGTCCTGGTGAACCACGAATGGCACGTGCTG CCTCAAGAAAGCGTCTTCCGGTTCTCCTTCGTGCCTGTGGTAGATGGAGACTTCCTCAGT GACACCCCAGAGGCCCTCATCAACGCGGGAGACTTCCACGGCCTGCAGGTGCTGGTGGGT GTGGTGAAGGATGAGGGCTCGTATTTTCTGGTTTACGGGGCCCCAGGCTTCAGCAAAGAC AACGAGTCTCTCATCAGCCGGGCCGAGTTCCTGGCCGGGGTGCGGGTCGGGGTTCCCCAG GTAAGTGACCTGGCAGCCGAGGCTGTGGTCCTGCATTACACAGACTGGCTGCATCCCGAG GACCCGGCACGCCTGAGGGAGGCCCTGAGCGATGTGGTGGGCGACCACAATGTCGTGTGC CCCGTGGCCCAGCTGGCTGGGCGACTGGCTGCCCAGGGTGCCCGGGTCTACGCCTACGTC TTTGAACACCGTGCTTCCACGCTCTCCTGGCCCCTGTGGATGGGGGTGCCCCACGGCTAC GAGATCGAGTTCATCTTTGGGATCCCCCTGGACCCCTCTCGAAACTACACGGCAGAGGAG AAAATCTTCGCCCAGCGACTGATGCGATACTGGGCCAACTTTGCCCGCACAGGGGATCCC AATGAGCCCCGAGACCCCAAGGCCCCACAATGGCCCCCGTACACGGCGGGGGCTCAGCAG TACGTTAGTCTGGACCTGCGGCCGCTGGAGGTGCGGCGGGGGCTGCGCGCCCAGGCCTGC GCCTTCTGGAACCGCTTCCTCCCCAAATTGCTCAGCGCCACCGACACGCTCGACGAGGCG GAGCGCCAGTGGAAGGCCGAGTTCCACCGCTGGAGCTCCTACATGGTGCACTGGAAGAAC CAGTTCGACCACTACAGCAAGCAGGATCGCTGCTCAGACCTGTGA PF00135 COesterase function hydrolase activity function hydrolase activity, acting on ester bonds function carboxylic ester hydrolase activity function cholinesterase activity function catalytic activity "
drug:(1R)-1,2,2-TRIMETHYLPROPYL (S)-METHYLPHOSPHINATErdfs:label"(1R)-1,2,2-TRIMETHYLPROPYL (S)-METHYLPHOSPHINATE"
drug:(1R)-1,2,2-TRIMETHYLPROPYL (S)-METHYLPHOSPHINATErdf:typedrugbank:drugs
drug:(1R)-1-(2-THIENYLACETYLAMINO)-1-(3-CARBOXYPHENYL)METHYLBORONIC ACIDdrugbank:description" experimental This compound belongs to the benzoic acids. These are organic Compounds containing a benzene ring which bears at least one carboxyl group. Benzoic Acids Organic Compounds Benzenoids Benzene and Substituted Derivatives Benzoic Acid and Derivatives Benzoyl Derivatives Boronic Acids Thiophenes Secondary Carboxylic Acid Amides Enolates Polyamines Carboxylic Acids Organoboron Compounds benzoyl boronic acid thiophene secondary carboxylic acid amide carboxamide group boronic acid derivative enolate polyamine carboxylic acid derivative carboxylic acid organic metalloid moeity organonitrogen compound amine organoboron compound logP 1.22 ALOGPS logS -4 ALOGPS Water Solubility 2.97e-02 g/l ALOGPS logP 2.3 ChemAxon IUPAC Name 3-[(R)-(dihydroxyboranyl)[2-(thiophen-2-yl)acetamido]methyl]benzoic acid ChemAxon Traditional IUPAC Name 3-[(R)-(dihydroxyboranyl)[2-(thiophen-2-yl)acetamido]methyl]benzoic acid ChemAxon Molecular Weight 319.141 ChemAxon Monoisotopic Weight 319.068573719 ChemAxon SMILES [H][C@@](NC(=O)CC1=CC=CS1)(B(O)O)C1=CC(=CC=C1)C(O)=O ChemAxon Molecular Formula C14H14BNO5S ChemAxon InChI InChI=1S/C14H14BNO5S/c17-12(8-11-5-2-6-22-11)16-13(15(20)21)9-3-1-4-10(7-9)14(18)19/h1-7,13,20-21H,8H2,(H,16,17)(H,18,19)/t13-/m0/s1 ChemAxon InChIKey InChIKey=HQLQTGGLHBYZSA-ZDUSSCGKSA-N ChemAxon Polar Surface Area (PSA) 106.86 ChemAxon Refractivity 76.53 ChemAxon Polarizability 31.81 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 4.03 ChemAxon pKa (strongest basic) -3 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5289377 PubChem Substance 99445022 ChemSpider 4451363 PDB SM2 BE0001358 Beta-lactamase Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-lactamase Defense mechanisms and antibiotic degradation This protein is a serine beta-lactamase with a substrate specificity for cephalosporins ampC Periplasm None 9.07 41556.0 Escherichia coli (strain K12) GenBank Gene Database J01611 GenBank Protein Database 145267 UniProtKB P00811 UniProt Accession AMPC_ECOLI Beta-lactamase precursor Cephalosporinase EC 3.5.2.6 >Beta-lactamase precursor MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWG YADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGI TLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVK PSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVK STIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSII NGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNY PNPARVDAAWQILNALQ >1134 bp ATGTTCAAAACGACGCTCTGCGCCTTATTAATTACCGCCTCTTGCTCCACATTTGCTGCC CCTCAACAAATCAACGATATTGTGCATCGCACAATTACCCCGCTTATAGAGCAACAAAAG ATCCCGGGTATGGCGGTGGCGGTAATTTATCAGGGTAAACCTTATTACTTTACCTGGGGC TATGCGGACATCGCCAAAAAGCAGCCCGTCACACAGCAAACGTTGTTTGAGTTAGGTTCG GTCAGCAAAACATTTACTGGCGTGCTTGGTGGCGACGCTATTGCTCGAGGGGAAATCAAG TTAAGCGATCCCACAACAAAATACTGGCCTGAACTTACCGCTAAACAGTGGAATGGGATC ACACTATTACATCTCGCAACCTACACTGCTGGCGGCCTGCCATTGCAGGTGCCGGATGAG GTGAAATCCTCAAGCGACTTGCTGCGCTTCTATCAAAACTGGCAGCCTGCATGGGCTCCA GGAACACAACGTCTGTATGCCAACTCCAGTATCGGTTTGTTCGGCGCACTGGCTGTGAAG CCGTCTGGTTTGAGTTTTGAGCAGGCGATGCAAACTCGTGTCTTCCAGCCACTCAAACTC AACCATACGTGGATTAATGTACCGCCCGCAGAAGAAAAGAATTACGCCTGGGGATATCGC GAAGGTAAGGCAGTGCATGTTTCGCCTGGGGCGTTAGATGCTGAAGCTTATGGTGTGAAG TCGACCATTGAAGATATGGCCCGCTGGGTGCAAAGCAATTTAAAACCCCTTGATATCAAT GAGAAAACGCTTCAACAAGGGATACAACTGGCACAATCTCGCTACTGGCAAACCGGCGAT ATGTATCAGGGCCTGGGCTGGGAAATGCTGGACTGGCCGGTAAATCCTGACAGCATCATT AACGGCAGTGACAATAAAATTGCACTGGCAGCACGCCCCGTAAAAGCGATTACGCCCCCA ACTCCTGCAGTACGCGCATCATGGGTACATAAAACAGGGGCGACCGGCGGATTTGGTAGC TATGTCGCGTTTATTCCAGAAAAAGAGCTGGGTATCGTGATGCTGGCAAACAAAAACTAT CCCAATCCAGCGAGAGTCGACGCCGCCTGGCAGATTCTTAACGCTCTACAGTAA PF00144 Beta-lactamase component cell component periplasmic space component periplasmic space (sensu Gram-negative Bacteria) function catalytic activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides function beta-lactamase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds process metabolism process cellular metabolism process drug metabolism process antibiotic metabolism process antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process physiological process process response to antibiotic BE0003894 Beta-lactamase TEM Escherichia coli # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-lactamase TEM Defense mechanisms TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta- lactamase inhibitors bla Cytoplasmic None 5.92 31514.9 Escherichia coli GeneCards bla GenBank Gene Database J01749 GenBank Protein Database 208959 UniProtKB P62593 UniProt Accession BLAT_ECOLX IRT-4 Penicillinase TEM-1 TEM-16/CAZ-7 TEM-2 TEM-24/CAZ-6 TEM-3 TEM-4 TEM-5 TEM-6 TEM-8/CAZ-2 >Beta-lactamase TEM MSIQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRP EERFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVREL CSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTM PAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGS RGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW >1191 bp ATGAAATCTAACAATGCGCTCATCGTCATCCTCGGCACCGTCACCCTGGATGCTGTAGGC ATAGGCTTGGTTATGCCGGTACTGCCGGGCCTCTTGCGGGATATCGTCCATTCCGACAGC ATCGCCAGTCACTATGGCGTGCTGCTAGCGCTATATGCGTTGATGCAATTTCTATGCGCA CCCGTTCTCGGAGCACTGTCCGACCGCTTTGGCCGCCGCCCAGTCCTGCTCGCTTCGCTA CTTGGAGCCACTATCGACTACGCGATCATGGCGACCACACCCGTCCTGTGGATCCTCTAC GCCGGACGCATCGTGGCCGGCATCACCGGCGCCACAGGTGCGGTTGCTGGCGCCTATATC GCCGACATCACCGATGGGGAAGATCGGGCTCGCCACTTCGGGCTCATGAGCGCTTGTTTC GGCGTGGGTATGGTGGCAGGCCCCGTGGCCGGGGGACTGTTGGGCGCCATCTCCTTGCAT GCACCATTCCTTGCGGCGGCGGTGCTCAACGGCCTCAACCTACTACTGGGCTGCTTCCTA ATGCAGGAGTCGCATAAGGGAGAGCGTCGACCGATGCCCTTGAGAGCCTTCAACCCAGTC AGCTCCTTCCGGTGGGCGCGGGGCATGACTATCGTCGCCGCACTTATGACTGTCTTCTTT ATCATGCAACTCGTAGGACAGGTGCCGGCAGCGCTCTGGGTCATTTTCGGCGAGGACCGC TTTCGCTGGAGCGCGACGATGATCGGCCTGTCGCTTGCGGTATTCGGAATCTTGCACGCC CTCGCTCAAGCCTTCGTCACTGGTCCCGCCACCAAACGTTTCGGCGAGAAGCAGGCCATT ATCGCCGGCATGGCGGCCGACGCGCTGGGCTACGTCTTGCTGGCGTTCGCGACGCGAGGC TGGATGGCCTTCCCCATTATGATTCTTCTCGCTTCCGGCGGCATCGGGATGCCCGCGTTG CAGGCCATGCTGTCCAGGCAGGTAGATGACGACCATCAGGGACAGCTTCAAGGATCGCTC GCGGCTCTTACCAGCCTAACTTCGATCACTGGACCGCTGATCGTCACGGCGATTTATGCC GCCTCGGCGAGCACATGGAACGGGTTGGCATGGATTGTAGGCGCCGCCCTATACCTTGTC TGCCTCCCCGCGTTGCGTCGCGGTGCATGGAGCCGGGCCACCTCGACCTGA PF00144 Beta-lactamase function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides function catalytic activity function beta-lactamase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds process response to chemical stimulus process response to drug process response to antibiotic process physiological process process metabolism process drug metabolism process cellular metabolism process antibiotic metabolism process antibiotic catabolism process beta-lactam antibiotic catabolism process response to stimulus process response to abiotic stimulus BE0002718 Beta-lactamase Escherichia coli # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-lactamase Involved in beta-lactamase activity blaCTX-M-9a Cytoplasmic None 9.38 30952.0 Escherichia coli GenBank Gene Database AF252621 UniProtKB Q9L5C8 UniProt Accession Q9L5C8_ECOLX Beta-lactamase Betalactamase CTX-M-9 CTX-M-9 beta-lactamase >Beta-lactamase CTX-M-9a MVTKRVQRMMFAAAACIPLLLGSAPLYAQTSAVQQKLAALEKSSGGRLGVALIDTADNTQ VLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTM TLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDP RDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTAGDKTGS GDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVLASAARIIAEGL >876 bp ATGGTGACAAAGAGAGTGCAACGGATGATGTTCGCGGCGGCGGCGTGCATTCCGCTGCTG CTGGGCAGCGCGCCGCTTTATGCGCAGACGAGTGCGGTGCAGCAAAAGCTGGCGGCGCTG GAGAAAAGCAGCGGAGGGCGGCTGGGCGTCGCGCTCATCGATACCGCAGATAATACGCAG GTGCTTTATCGCGGTGATGAACGCTTTCCAATGTGCAGTACCAGTAAAGTTATGGCGGCC GCGGCGGTGCTTAAGCAGAGTGAAACGCAAAAGCAGCTGCTTAATCAGCCTGTCGAGATC AAGCCTGCCGATCTGGTTAACTACAATCCGATTGCCGAAAAACACGTCAACGGCACAATG ACGCTGGCAGAGCTGAGCGCGGCCGCGTTGCAGTACAGCGACAATACCGCCATGAACAAA TTGATTGCCCAGCTCGGTGGCCCGGGAGGCGTGACGGCTTTTGCCCGCGCGATCGGCGAT GAGACGTTTCGTCTGGATCGCACTGAACCTACGCTGAATACCGCCATTCCCGGCGACCCG AGAGACACCACCACGCCGCGGGCGATGGCACAGACGTTGCGTCAGCTTACGCTGGGTCAT GCGCTGGGCGAAACCCAGCGGGCGCAGTTGGTGACGTGGCTCAAAGGCAATACGACCGGC GCAGCCAGCATTCGGGCCGGCTTACCGACGTCGTGGACTGCAGGTGATAAGACCGGCAGC GGCGACTACGGCACCACCAATGATATTGCGGTGATCTGGCCGCAGGGTCGTGCGCCGCTG GTTCTGGTGACCTATTTTACCCAGCCGCAACAGAACGCAGAGAGCCGCCGCGATGTGCTG GCTTCAGCGGCGAGAATCATCGCCGAAGGGCTGTAA PF00144 Beta-lactamase function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides function catalytic activity function beta-lactamase activity process metabolism process drug metabolism process cellular metabolism process antibiotic metabolism process antibiotic catabolism process beta-lactam antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process response to antibiotic process physiological process "
drug:(1R)-1-(2-THIENYLACETYLAMINO)-1-(3-CARBOXYPHENYL)METHYLBORONIC ACIDrdfs:label"(1R)-1-(2-THIENYLACETYLAMINO)-1-(3-CARBOXYPHENYL)METHYLBORONIC ACID"
drug:(1R)-1-(2-THIENYLACETYLAMINO)-1-(3-CARBOXYPHENYL)METHYLBORONIC ACIDrdf:typedrugbank:drugs
drug:(1R)-1-(2-THIENYLACETYLAMINO)-1-PHENYLMETHYLBORONIC ACIDdrugbank:description" experimental This compound belongs to the benzene and substituted derivatives. These are aromatic compounds containing at least one benzene ring. Benzene and Substituted Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Boronic Acids Thiophenes Secondary Carboxylic Acid Amides Polyamines Carboxylic Acids Enolates Organoboron Compounds thiophene boronic acid derivative secondary carboxylic acid amide carboxamide group enolate carboxylic acid derivative carboxylic acid polyamine organic metalloid moeity amine organonitrogen compound organoboron compound logP 1.78 ALOGPS logS -3.9 ALOGPS Water Solubility 3.73e-02 g/l ALOGPS logP 2.78 ChemAxon IUPAC Name [(R)-phenyl[2-(thiophen-2-yl)acetamido]methyl]boronic acid ChemAxon Traditional IUPAC Name (R)-phenyl[2-(thiophen-2-yl)acetamido]methylboronic acid ChemAxon Molecular Weight 275.131 ChemAxon Monoisotopic Weight 275.078744475 ChemAxon SMILES [H][C@@](NC(=O)CC1=CC=CS1)(B(O)O)C1=CC=CC=C1 ChemAxon Molecular Formula C13H14BNO3S ChemAxon InChI InChI=1S/C13H14BNO3S/c16-12(9-11-7-4-8-19-11)15-13(14(17)18)10-5-2-1-3-6-10/h1-8,13,17-18H,9H2,(H,15,16)/t13-/m0/s1 ChemAxon InChIKey InChIKey=LGJCDEZMANATFA-ZDUSSCGKSA-N ChemAxon Polar Surface Area (PSA) 69.56 ChemAxon Refractivity 69.27 ChemAxon Polarizability 28.59 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 12.72 ChemAxon pKa (strongest basic) -3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5289378 PubChem Substance 99445023 ChemSpider 4451364 PDB SM3 BE0001358 Beta-lactamase Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-lactamase Defense mechanisms and antibiotic degradation This protein is a serine beta-lactamase with a substrate specificity for cephalosporins ampC Periplasm None 9.07 41556.0 Escherichia coli (strain K12) GenBank Gene Database J01611 GenBank Protein Database 145267 UniProtKB P00811 UniProt Accession AMPC_ECOLI Beta-lactamase precursor Cephalosporinase EC 3.5.2.6 >Beta-lactamase precursor MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWG YADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGI TLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVK PSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVK STIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSII NGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNY PNPARVDAAWQILNALQ >1134 bp ATGTTCAAAACGACGCTCTGCGCCTTATTAATTACCGCCTCTTGCTCCACATTTGCTGCC CCTCAACAAATCAACGATATTGTGCATCGCACAATTACCCCGCTTATAGAGCAACAAAAG ATCCCGGGTATGGCGGTGGCGGTAATTTATCAGGGTAAACCTTATTACTTTACCTGGGGC TATGCGGACATCGCCAAAAAGCAGCCCGTCACACAGCAAACGTTGTTTGAGTTAGGTTCG GTCAGCAAAACATTTACTGGCGTGCTTGGTGGCGACGCTATTGCTCGAGGGGAAATCAAG TTAAGCGATCCCACAACAAAATACTGGCCTGAACTTACCGCTAAACAGTGGAATGGGATC ACACTATTACATCTCGCAACCTACACTGCTGGCGGCCTGCCATTGCAGGTGCCGGATGAG GTGAAATCCTCAAGCGACTTGCTGCGCTTCTATCAAAACTGGCAGCCTGCATGGGCTCCA GGAACACAACGTCTGTATGCCAACTCCAGTATCGGTTTGTTCGGCGCACTGGCTGTGAAG CCGTCTGGTTTGAGTTTTGAGCAGGCGATGCAAACTCGTGTCTTCCAGCCACTCAAACTC AACCATACGTGGATTAATGTACCGCCCGCAGAAGAAAAGAATTACGCCTGGGGATATCGC GAAGGTAAGGCAGTGCATGTTTCGCCTGGGGCGTTAGATGCTGAAGCTTATGGTGTGAAG TCGACCATTGAAGATATGGCCCGCTGGGTGCAAAGCAATTTAAAACCCCTTGATATCAAT GAGAAAACGCTTCAACAAGGGATACAACTGGCACAATCTCGCTACTGGCAAACCGGCGAT ATGTATCAGGGCCTGGGCTGGGAAATGCTGGACTGGCCGGTAAATCCTGACAGCATCATT AACGGCAGTGACAATAAAATTGCACTGGCAGCACGCCCCGTAAAAGCGATTACGCCCCCA ACTCCTGCAGTACGCGCATCATGGGTACATAAAACAGGGGCGACCGGCGGATTTGGTAGC TATGTCGCGTTTATTCCAGAAAAAGAGCTGGGTATCGTGATGCTGGCAAACAAAAACTAT CCCAATCCAGCGAGAGTCGACGCCGCCTGGCAGATTCTTAACGCTCTACAGTAA PF00144 Beta-lactamase component cell component periplasmic space component periplasmic space (sensu Gram-negative Bacteria) function catalytic activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides function beta-lactamase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds process metabolism process cellular metabolism process drug metabolism process antibiotic metabolism process antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process physiological process process response to antibiotic "
drug:(1R)-1-(2-THIENYLACETYLAMINO)-1-PHENYLMETHYLBORONIC ACIDrdfs:label"(1R)-1-(2-THIENYLACETYLAMINO)-1-PHENYLMETHYLBORONIC ACID"
drug:(1R)-1-(2-THIENYLACETYLAMINO)-1-PHENYLMETHYLBORONIC ACIDrdf:typedrugbank:drugs
drug:(1R)-1-PHENYLETHYL 4-(ACETYLAMINO)BENZYLPHOSPHONATEdrugbank:description" experimental This compound belongs to the anilides. These are organic heterocyclic compounds derived from oxoacids RkE(=O)l(OH)m (l not 0) by replacing an OH group by the NHPh group or derivative formed by ring substitution. Anilides Organic Compounds Benzenoids Benzene and Substituted Derivatives Anilides Phosphonic Acid Esters Secondary Carboxylic Acid Amides Polyamines Enolates Carboxylic Acids phosphonic acid ester phosphonic acid derivative secondary carboxylic acid amide carboxamide group carboxylic acid derivative polyamine carboxylic acid enolate amine organonitrogen compound logP 2.51 ALOGPS logS -3.8 ALOGPS Water Solubility 5.69e-02 g/l ALOGPS logP 2.56 ChemAxon IUPAC Name (R)-((1R)-1-phenylethyl [(4-acetamidophenyl)methyl]phosphonate) ChemAxon Traditional IUPAC Name (R)-((1R)-1-phenylethyl (4-acetamidophenyl)methylphosphonate) ChemAxon Molecular Weight 332.3108 ChemAxon Monoisotopic Weight 332.105169613 ChemAxon SMILES [H][C@](C)(O[P@]([O-])(=O)CC1=CC=C(NC(C)=O)C=C1)C1=CC=CC=C1 ChemAxon Molecular Formula C17H19NO4P ChemAxon InChI InChI=1S/C17H20NO4P/c1-13(16-6-4-3-5-7-16)22-23(20,21)12-15-8-10-17(11-9-15)18-14(2)19/h3-11,13H,12H2,1-2H3,(H,18,19)(H,20,21)/p-1/t13-/m1/s1 ChemAxon InChIKey InChIKey=YPTMOJMDCPUCJT-CYBMUJFWSA-M ChemAxon Polar Surface Area (PSA) 78.46 ChemAxon Refractivity 89.17 ChemAxon Polarizability 33.51 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 1.89 ChemAxon pKa (strongest basic) -4.4 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937159 PubChem Substance 99445016 PDB SH4 BE0004339 Hepatitis B virus receptor binding protein Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Hepatitis B virus receptor binding protein Involved in receptor activity None 8.14 38162.0 Human HUGO Gene Nomenclature Committee (HGNC) GNC:5525 GenBank Gene Database AY570731 GenBank Protein Database 46326410 UniProtKB Q6PYX1 UniProt Accession Q6PYX1_HUMAN >Hepatitis B virus receptor binding protein YYYGMDVWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWN SGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKS CDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKA KGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLD SDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK PF07654 C1-set "
drug:(1R)-1-PHENYLETHYL 4-(ACETYLAMINO)BENZYLPHOSPHONATErdfs:label"(1R)-1-PHENYLETHYL 4-(ACETYLAMINO)BENZYLPHOSPHONATE"
drug:(1R)-1-PHENYLETHYL 4-(ACETYLAMINO)BENZYLPHOSPHONATErdf:typedrugbank:drugs
drug:(1R)-1-{[(4'-METHOXY-1,1'-BIPHENYL-4-YL)SULFONYL]AMINO}-2-METHYLPROPYLPHOSPHONIC ACIDdrugbank:description" experimental This compound belongs to the biphenyls and derivatives. These are organic compounds containing to benzene rings linked together by a C-C bond. Biphenyls and Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Biphenyls and Derivatives Benzenesulfonamides Anisoles Alkyl Aryl Ethers Organic Phosphonic Acids Sulfonyls Sulfonamides Polyamines benzenesulfonamide anisole phenol ether alkyl aryl ether sulfonic acid derivative sulfonamide sulfonyl phosphonic acid derivative phosphonic acid polyamine ether amine organonitrogen compound logP 1.43 ALOGPS logS -2.9 ALOGPS Water Solubility 4.61e-01 g/l ALOGPS logP 2.43 ChemAxon IUPAC Name [(1R)-1-{[4-(4-methoxyphenyl)benzene]sulfonamido}-2-methylpropyl]phosphonic acid ChemAxon Traditional IUPAC Name (1R)-1-[4-(4-methoxyphenyl)benzenesulfonamido]-2-methylpropylphosphonic acid ChemAxon Molecular Weight 399.398 ChemAxon Monoisotopic Weight 399.090544643 ChemAxon SMILES [H][C@](NS(=O)(=O)C1=CC=C(C=C1)C1=CC=C(OC)C=C1)(C(C)C)P(O)(O)=O ChemAxon Molecular Formula C17H22NO6PS ChemAxon InChI InChI=1S/C17H22NO6PS/c1-12(2)17(25(19,20)21)18-26(22,23)16-10-6-14(7-11-16)13-4-8-15(24-3)9-5-13/h4-12,17-18H,1-3H3,(H2,19,20,21)/t17-/m1/s1 ChemAxon InChIKey InChIKey=BZVYQWLRCHLAGK-QGZVFWFLSA-N ChemAxon Polar Surface Area (PSA) 112.93 ChemAxon Refractivity 98.92 ChemAxon Polarizability 39.12 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 1.48 ChemAxon pKa (strongest basic) -4.8 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 6852147 PubChem Substance 99444243 ChemSpider 5254604 PDB FIN BE0001182 Neutrophil collagenase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Neutrophil collagenase Involved in protease activity and collagen degradation Can degrade fibrillar type I, II, and III collagens MMP8 11q22.3 Cytoplasmic granule. Note=Stored in intracellular granules None 6.86 53413.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7175 GenAtlas MMP8 GeneCards MMP8 GenBank Gene Database J05556 GenBank Protein Database 180618 UniProtKB P22894 UniProt Accession MMP8_HUMAN EC 3.4.24.34 Matrix metalloproteinase-8 MMP-8 Neutrophil collagenase precursor PMNL collagenase PMNL-CL >Neutrophil collagenase precursor MFSLKTLPFLLLLHVQISKAFPVSSKEKNTKTVQDYLEKFYQLPSNQYQSTRKNGTNVIV EKLKEMQRFFGLNVTGKPNEETLDMMKKPRCGVPDSGGFMLTPGNPKWERTNLTYRIRNY TPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGIL AHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYA FRETSNYSLPQDDIDGIQAIYGLSSNPIQPTGPSTPKPCDPSLTFDAITTLRGEILFFKD RYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGYDILQG YPKDISNYGFPSSVQAIDAAVFYRSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGI ESKVDAVFQQEHFFHVFSGPRYYAFDLIAQRVTRVARGNKWLNCRYG >1404 bp ATGTTCTCCCTGAAGACGCTTCCATTTCTGCTCTTACTCCATGTGCAGATTTCCAAGGCC TTTCCTGTATCTTCTAAAGAGAAAAATACAAAAACTGTTCAGGACTACCTGGAAAAGTTC TACCAATTACCAAGCAACCAGTATCAGTCTACAAGGAAGAATGGCACTAATGTGATCGTT GAAAAGCTTAAAGAAATGCAGCGATTTTTTGGGTTGAATGTGACGGGGAAGCCAAATGAG GAAACTCTGGACATGATGAAAAAGCCTCGCTGTGGAGTGCCTGACAGTGGTGGTTTTATG TTAACCCCAGGAAACCCCAAGTGGGAACGCACTAACTTGACCTACAGGATTCGAAACTAT ACCCCACAGCTGTCAGAGGCTGAGGTAGAAAGAGCTATCAAGGATGCCTTTGAACTCTGG AGTGTTGCATCACCTCTCATCTTCACCAGGATCTCACAGGGAGAGGCAGATATCAACATT GCTTTTTACCAAAGAGATCACGGTGACAATTCTCCATTTGATGGACCCAATGGAATCCTT GCTCATGCCTTTCAGCCAGGCCAAGGTATTGGAGGAGATGCTCATTTTGATGCCGAAGAA ACATGGACCAACACCTCCGCAAATTACAACTTGTTTCTTGTTGCTGCTCATGAATTTGGC CATTCTTTGGGGCTCGCTCACTCCTCTGACCCTGGTGCCTTGATGTATCCCAACTATGCT TTCAGGGAAACCAGCAACTACTCACTCCCTCAAGATGACATCGATGGCATTCAGGCCATC TATGGACTTTCAAGCAACCCTATCCAACCTACTGGACCAAGCACACCCAAACCCTGTGAC CCCAGTTTGACATTTGATGCTATCACCACACTCCGTGGAGAAATACTTTTCTTTAAAGAC AGGTACTTCTGGAGAAGGCATCCTCAGCTACAAAGAGTCGAAATGAATTTTATTTCTCTA TTCTGGCCATCCCTTCCAACTGGTATACAGGCTGCTTATGAAGATTTTGACAGAGACCTC ATTTTCCTATTTAAAGGCAACCAATACTGGGCTCTGAGTGGCTATGATATTCTGCAAGGT TATCCCAAGGATATATCAAACTATGGCTTCCCCAGCAGCGTCCAAGCAATTGACGCAGCT GTTTTCTACAGAAGTAAAACATACTTCTTTGTAAATGACCAATTCTGGAGATATGATAAC CAAAGACAATTCATGGAGCCAGGTTATCCCAAAAGCATATCAGGTGCCTTTCCAGGAATA GAGAGTAAAGTTGATGCAGTTTTCCAGCAAGAACATTTCTTCCATGTCTTCAGTGGACCA AGATATTACGCATTTGATCTTATTGCTCAGAGAGTTACCAGAGTTGCAAGAGGCAATAAA TGGCTTAACTGTAGATATGGCTGA PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix component extracellular matrix (sensu Metazoa) function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding function catalytic activity function hydrolase activity process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism "
drug:(1R)-1-{[(4'-METHOXY-1,1'-BIPHENYL-4-YL)SULFONYL]AMINO}-2-METHYLPROPYLPHOSPHONIC ACIDrdfs:label"(1R)-1-{[(4'-METHOXY-1,1'-BIPHENYL-4-YL)SULFONYL]AMINO}-2-METHYLPROPYLPHOSPHONIC ACID"
drug:(1R)-1-{[(4'-METHOXY-1,1'-BIPHENYL-4-YL)SULFONYL]AMINO}-2-METHYLPROPYLPHOSPHONIC ACIDrdf:typedrugbank:drugs
drug:(1R)-2-METHYL-1-(PHENYLMETHYL)PROPYL[(1S)-1-FORMYLPENTYL]CARBAMATEdrugbank:description" experimental This compound belongs to the benzene and substituted derivatives. These are aromatic compounds containing at least one benzene ring. Benzene and Substituted Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Carbamic Acids and Derivatives Ethers Polyamines Enolates Aldehydes carbamic acid derivative enolate polyamine ether organonitrogen compound amine aldehyde logP 3.7 ALOGPS logS -4.5 ALOGPS Water Solubility 9.58e-03 g/l ALOGPS logP 4.43 ChemAxon IUPAC Name (2R)-3-methyl-1-phenylbutan-2-yl N-[(2S)-1-oxohexan-2-yl]carbamate ChemAxon Traditional IUPAC Name (2R)-3-methyl-1-phenylbutan-2-yl N-[(2S)-1-oxohexan-2-yl]carbamate ChemAxon Molecular Weight 305.4119 ChemAxon Monoisotopic Weight 305.199093735 ChemAxon SMILES [H][C@@](CCCC)(NC(=O)O[C@]([H])(CC1=CC=CC=C1)C(C)C)C=O ChemAxon Molecular Formula C18H27NO3 ChemAxon InChI InChI=1S/C18H27NO3/c1-4-5-11-16(13-20)19-18(21)22-17(14(2)3)12-15-9-7-6-8-10-15/h6-10,13-14,16-17H,4-5,11-12H2,1-3H3,(H,19,21)/t16-,17+/m0/s1 ChemAxon InChIKey InChIKey=ZLZXUNHJWVLGTE-DLBZAZTESA-N ChemAxon Polar Surface Area (PSA) 55.4 ChemAxon Refractivity 87.15 ChemAxon Polarizability 34.78 ChemAxon Rotatable Bond Count 10 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 14.01 ChemAxon pKa (strongest basic) -7.3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 10062713 PubChem Substance 99444063 ChemSpider 8238256 PDB CT1 BE0003417 Cathepsin K Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cathepsin K Involved in cysteine-type endopeptidase activity Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation CTSK 1q21 Lysosome None 8.65 36966.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:2536 GenAtlas CTSK GenBank Gene Database U13665 UniProtKB P43235 UniProt Accession CATK_HUMAN Cathepsin K precursor Cathepsin O Cathepsin O2 Cathepsin X EC 3.4.22.38 >Cathepsin K MWGLKVLLLPVVSFALYPEEILDTHWELWKKTHRKQYNNKVDEISRRLIWEKNLKYISIH NLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPLSHSRSNDTLYIPEWEGRAPDSVD YRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGG YMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVA RVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGE NWGNKGYILMARNKNNACGIANLASFPKM >990 bp ATGTGGGGGCTCAAGGTTCTGCTGCTACCTGTGGTGAGCTTTGCTCTGTACCCTGAGGAG ATACTGGACACCCACTGGGAGCTATGGAAGAAGACCCACAGGAAGCAATATAACAACAAG GTGGATGAAATCTCTCGGCGTTTAATTTGGGAAAAAAACCTGAAGTATATTTCCATCCAT AACCTTGAGGCTTCTCTTGGTGTCCATACATATGAACTGGCTATGAACCACCTGGGGGAC ATGACCAGTGAAGAGGTGGTTCAGAAGATGACTGGACTCAAAGTACCCCTGTCTCATTCC CGCAGTAATGACACCCTTTATATCCCAGAATGGGAAGGTAGAGCCCCAGACTCTGTCGAC TATCGAAAGAAAGGATATGTTACTCCTGTCAAAAATCAGGGTCAGTGTGGTTCCTGTTGG GCTTTTAGCTCTGTGGGTGCCCTGGAGGGCCAACTCAAGAAGAAAACTGGCAAACTCTTA AATCTGAGTCCCCAGAACCTAGTGGATTGTGTGTCTGAGAATGATGGCTGTGGAGGGGGC TACATGACCAATGCCTTCCAATATGTGCAGAAGAACCGGGGTATTGACTCTGAAGATGCC TACCCATATGTGGGACAGGAAGAGAGTTGTATGTACAACCCAACAGGCAAGGCAGCTAAA TGCAGAGGGTACAGAGAGATCCCCGAGGGGAATGAGAAAGCCCTGAAGAGGGCAGTGGCC CGAGTGGGACCTGTCTCTGTGGCCATTGATGCAAGCCTGACCTCCTTCCAGTTTTACAGC AAAGGTGTGTATTATGATGAAAGCTGCAATAGCGATAATCTGAACCATGCGGTTTTGGCA GTGGGATATGGAATCCAGAAGGGAAACAAGCACTGGATAATTAAAAACAGCTGGGGAGAA AACTGGGGAAACAAAGGATATATCCTCATGGCTCGAAATAAGAACAACGCCTGTGGCATT GCCAACCTGGCCAGCTTCCCCAAGATGTGA PF00112 Peptidase_C1 PF08246 Inhibitor_I29 function endopeptidase activity function cysteine-type endopeptidase activity function cysteine-type peptidase activity function catalytic activity function hydrolase activity function peptidase activity process proteolysis process physiological process process metabolism process macromolecule metabolism process protein metabolism process cellular protein metabolism "
drug:(1R)-2-METHYL-1-(PHENYLMETHYL)PROPYL[(1S)-1-FORMYLPENTYL]CARBAMATErdfs:label"(1R)-2-METHYL-1-(PHENYLMETHYL)PROPYL[(1S)-1-FORMYLPENTYL]CARBAMATE"
drug:(1R)-2-METHYL-1-(PHENYLMETHYL)PROPYL[(1S)-1-FORMYLPENTYL]CARBAMATErdf:typedrugbank:drugs
drug:(1R)-2-PHENYLACETAMIDO-2-(3-CARBOXYPHENYL)ETHYL BORONIC ACIDdrugbank:description" experimental This compound belongs to the benzoic acids. These are organic Compounds containing a benzene ring which bears at least one carboxyl group. Benzoic Acids Organic Compounds Benzenoids Benzene and Substituted Derivatives Benzoic Acid and Derivatives Benzoyl Derivatives Boronic Acids Secondary Carboxylic Acid Amides Enolates Polyamines Carboxylic Acids Organoboron Compounds benzoyl boronic acid boronic acid derivative secondary carboxylic acid amide carboxamide group polyamine carboxylic acid derivative enolate carboxylic acid amine organic metalloid moeity organonitrogen compound organoboron compound logP 1.37 ALOGPS logS -4.2 ALOGPS Water Solubility 2.11e-02 g/l ALOGPS logP 2.73 ChemAxon IUPAC Name 3-[(2R)-2-(dihydroxyboranyl)-2-(2-phenylacetamido)ethyl]benzoic acid ChemAxon Traditional IUPAC Name 3-[(2R)-2-(dihydroxyboranyl)-2-(2-phenylacetamido)ethyl]benzoic acid ChemAxon Molecular Weight 327.14 ChemAxon Monoisotopic Weight 327.127803157 ChemAxon SMILES [H][C@@](CC1=CC=CC(=C1)C(O)=O)(NC(=O)CC1=CC=CC=C1)B(O)O ChemAxon Molecular Formula C17H18BNO5 ChemAxon InChI InChI=1S/C17H18BNO5/c20-16(11-12-5-2-1-3-6-12)19-15(18(23)24)10-13-7-4-8-14(9-13)17(21)22/h1-9,15,23-24H,10-11H2,(H,19,20)(H,21,22)/t15-/m0/s1 ChemAxon InChIKey InChIKey=ZAHVYMBTUDWUAX-HNNXBMFYSA-N ChemAxon Polar Surface Area (PSA) 106.86 ChemAxon Refractivity 84.4 ChemAxon Polarizability 33.99 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 4.04 ChemAxon pKa (strongest basic) -2.1 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5287796 PubChem Substance 99443937 ChemSpider 4450094 PDB BJP BE0003894 Beta-lactamase TEM Escherichia coli # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-lactamase TEM Defense mechanisms TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta- lactamase inhibitors bla Cytoplasmic None 5.92 31514.9 Escherichia coli GeneCards bla GenBank Gene Database J01749 GenBank Protein Database 208959 UniProtKB P62593 UniProt Accession BLAT_ECOLX IRT-4 Penicillinase TEM-1 TEM-16/CAZ-7 TEM-2 TEM-24/CAZ-6 TEM-3 TEM-4 TEM-5 TEM-6 TEM-8/CAZ-2 >Beta-lactamase TEM MSIQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRP EERFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVREL CSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTM PAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGS RGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW >1191 bp ATGAAATCTAACAATGCGCTCATCGTCATCCTCGGCACCGTCACCCTGGATGCTGTAGGC ATAGGCTTGGTTATGCCGGTACTGCCGGGCCTCTTGCGGGATATCGTCCATTCCGACAGC ATCGCCAGTCACTATGGCGTGCTGCTAGCGCTATATGCGTTGATGCAATTTCTATGCGCA CCCGTTCTCGGAGCACTGTCCGACCGCTTTGGCCGCCGCCCAGTCCTGCTCGCTTCGCTA CTTGGAGCCACTATCGACTACGCGATCATGGCGACCACACCCGTCCTGTGGATCCTCTAC GCCGGACGCATCGTGGCCGGCATCACCGGCGCCACAGGTGCGGTTGCTGGCGCCTATATC GCCGACATCACCGATGGGGAAGATCGGGCTCGCCACTTCGGGCTCATGAGCGCTTGTTTC GGCGTGGGTATGGTGGCAGGCCCCGTGGCCGGGGGACTGTTGGGCGCCATCTCCTTGCAT GCACCATTCCTTGCGGCGGCGGTGCTCAACGGCCTCAACCTACTACTGGGCTGCTTCCTA ATGCAGGAGTCGCATAAGGGAGAGCGTCGACCGATGCCCTTGAGAGCCTTCAACCCAGTC AGCTCCTTCCGGTGGGCGCGGGGCATGACTATCGTCGCCGCACTTATGACTGTCTTCTTT ATCATGCAACTCGTAGGACAGGTGCCGGCAGCGCTCTGGGTCATTTTCGGCGAGGACCGC TTTCGCTGGAGCGCGACGATGATCGGCCTGTCGCTTGCGGTATTCGGAATCTTGCACGCC CTCGCTCAAGCCTTCGTCACTGGTCCCGCCACCAAACGTTTCGGCGAGAAGCAGGCCATT ATCGCCGGCATGGCGGCCGACGCGCTGGGCTACGTCTTGCTGGCGTTCGCGACGCGAGGC TGGATGGCCTTCCCCATTATGATTCTTCTCGCTTCCGGCGGCATCGGGATGCCCGCGTTG CAGGCCATGCTGTCCAGGCAGGTAGATGACGACCATCAGGGACAGCTTCAAGGATCGCTC GCGGCTCTTACCAGCCTAACTTCGATCACTGGACCGCTGATCGTCACGGCGATTTATGCC GCCTCGGCGAGCACATGGAACGGGTTGGCATGGATTGTAGGCGCCGCCCTATACCTTGTC TGCCTCCCCGCGTTGCGTCGCGGTGCATGGAGCCGGGCCACCTCGACCTGA PF00144 Beta-lactamase function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides function catalytic activity function beta-lactamase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds process beta-lactam antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process response to antibiotic process physiological process process metabolism process drug metabolism process cellular metabolism process antibiotic metabolism process antibiotic catabolism "
drug:(1R)-2-PHENYLACETAMIDO-2-(3-CARBOXYPHENYL)ETHYL BORONIC ACIDrdfs:label"(1R)-2-PHENYLACETAMIDO-2-(3-CARBOXYPHENYL)ETHYL BORONIC ACID"
drug:(1R)-2-PHENYLACETAMIDO-2-(3-CARBOXYPHENYL)ETHYL BORONIC ACIDrdf:typedrugbank:drugs
drug:(1R)-2-[(CYANOMETHYL)AMINO]-1-({[2-(DIFLUOROMETHOXY)BENZYL]SULFONYL}METHYL)-2-OXOETHYL MORPHOLINE-4-CARBOXYLATEdrugbank:description" experimental This compound belongs to the morpholine carboxylic acids. These are heterocyclic compounds containing a morpholine ring substituted by one or more carboxylic acid groups. Morpholine Carboxylic Acids Organic Compounds Heterocyclic Compounds Oxazinanes Morpholines Phenol Ethers Alkyl Aryl Ethers Sulfones Tertiary Amines Secondary Carboxylic Acid Amides Sulfoxides Carbamic Acids and Derivatives Polyamines Nitriles Carboxylic Acids Enolates Alkyl Fluorides Organofluorides phenol ether alkyl aryl ether benzene sulfone sulfonyl carboxamide group secondary carboxylic acid amide sulfoxide carbamic acid derivative tertiary amine polyamine ether enolate carboxylic acid derivative carbonitrile nitrile carboxylic acid amine organohalogen organofluoride alkyl halide alkyl fluoride organonitrogen compound logP 0.95 ALOGPS logS -3.2 ALOGPS Water Solubility 3.20e-01 g/l ALOGPS logP -0.21 ChemAxon IUPAC Name (1R)-1-[(cyanomethyl)carbamoyl]-2-({[2-(difluoromethoxy)phenyl]methane}sulfonyl)ethyl morpholine-4-carboxylate ChemAxon Traditional IUPAC Name (1R)-1-(cyanomethylcarbamoyl)-2-{[2-(difluoromethoxy)phenyl]methanesulfonyl}ethyl morpholine-4-carboxylate ChemAxon Molecular Weight 461.437 ChemAxon Monoisotopic Weight 461.106827141 ChemAxon SMILES [H][C@@](CS(=O)(=O)CC1=C(OC(F)F)C=CC=C1)(OC(=O)N1CCOCC1)C(=O)NCC#N ChemAxon Molecular Formula C18H21F2N3O7S ChemAxon InChI InChI=1S/C18H21F2N3O7S/c19-17(20)29-14-4-2-1-3-13(14)11-31(26,27)12-15(16(24)22-6-5-21)30-18(25)23-7-9-28-10-8-23/h1-4,15,17H,6-12H2,(H,22,24)/t15-/m0/s1 ChemAxon InChIKey InChIKey=YKWHKILAGONYKL-HNNXBMFYSA-N ChemAxon Polar Surface Area (PSA) 135.03 ChemAxon Refractivity 101.64 ChemAxon Polarizability 40.88 ChemAxon Rotatable Bond Count 10 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 6.95 ChemAxon pKa (strongest basic) -4.1 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 9547943 PubChem Substance 99444666 ChemSpider 7826878 PDB MO9 BE0001646 Cathepsin S Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cathepsin S Involved in cysteine-type endopeptidase activity Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N CTSS 1q21 Lysosome None 8.45 37496.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:2545 GenAtlas CTSS GeneCards CTSS GenBank Gene Database S93414 GenBank Protein Database 248406 UniProtKB P25774 UniProt Accession CATS_HUMAN Cathepsin S precursor EC 3.4.22.27 >Cathepsin S precursor MKRLVCVLLVCSSAVAQLHKDPTLDHHWHLWKKTYGKQYKEKNEEAVRRLIWEKNLKFVM LHNLEHSMGMHSYDLGMNHLGDMTSEEVMSLMSSLRVPSQWQRNITYKSNPNRILPDSVD WREKGCVTEVKYQGSCGACWAFSAVGALEAQLKLKTGKLVSLSAQNLVDCSTEKYGNKGC NGGFMTTAFQYIIDNKGIDSDASYPYKAMDQKCQYDSKYRAATCSKYTELPYGREDVLKE AVANKGPVSVGVDARHPSFFLYRSGVYYEPSCTQNVNHGVLVVGYGDLNGKEYWLVKNSW GHNFGEEGYIRMARNKGNHCGIASFPSYPEI >996 bp ATGAAACGGCTGGTTTGTGTGCTCTTGGTGTGCTCCTCTGCAGTGGCACAGTTGCATAAA GATCCTACCCTGGATCACCACTGGCATCTCTGGAAGAAAACCTATGGCAAACAATACAAG GAAAAGAATGAAGAAGCAGTACGACGTCTCATCTGGGAAAAGAATCTAAAGTTTGTGATG CTTCACAACCTGGAGCATTCAATGGGAATGCACTCATACGATCTGGGCATGAACCACCTG GGAGACATGACCAGTGAAGAAGTGATGTCTTTGACGAGTTCCCTGAGAGTTCCCAGCCAG TGGCAGAGAAATATCACATATAAGTCAAACCCTAATCGGATATTGCCTGATTCTGTGGAC TGGAGAGAGAAAGGGTGTGTTACTGAAGTGAAATATCAAGGTTCTTGTGGTGCTTGCTGG GCTTTCAGTGCTGTGGGGGCCCTGGAAGCACAGCTGAAGCTGAAAACAGGAAAGCTGGTG ACTCTCAGTGCCCAGAACCTGGTGGATTGCTCAACTGAAAAATATGGAAACAAAGGCTGC AATGGTGGCTTCATGACAACGGCTTTCCAGTACATCATTGATAACAAGGGCATCGACTCA GACGCTTCCTATCCCTACAAAGCCATGGATCAGAAATGTCAATATGACTCAAAATATCGT GCTGCCACATGTTCAAAGTACACTGAACTTCCTTATGGGAGAGAAGATGTCCTGAAAGAA GCTGTGGCCAATAAAGGCCCAGTGTCTGTTGGTGTAGATGCGCGTCATCCTTCTTTCTTC CTCTACAGAAGTGGTGTCTACTATGAACCATCCTGTACTCAGAATGTGAATCATGGTGTA CTTGTGGTTGGCTATGGTGATCTTAATGGGAAAGAATACTGGCTTGTGAAAAACAGCTGG GGCCACAACTTTGGTGAAGAAGGATATATTCGGATGGCAAGAAATAAAGGAAATCATTGT GGGATTGCTAGCTTTCCCTCTTACCCAGAAATCTAG PF00112 Peptidase_C1 PF08246 Inhibitor_I29 function catalytic activity function hydrolase activity function peptidase activity function endopeptidase activity function cysteine-type endopeptidase activity function cysteine-type peptidase activity process metabolism process macromolecule metabolism process protein metabolism process cellular protein metabolism process proteolysis process physiological process "
drug:(1R)-2-[(CYANOMETHYL)AMINO]-1-({[2-(DIFLUOROMETHOXY)BENZYL]SULFONYL}METHYL)-2-OXOETHYL MORPHOLINE-4-CARBOXYLATErdfs:label"(1R)-2-[(CYANOMETHYL)AMINO]-1-({[2-(DIFLUOROMETHOXY)BENZYL]SULFONYL}METHYL)-2-OXOETHYL MORPHOLINE-4-CARBOXYLATE"
drug:(1R)-2-[(CYANOMETHYL)AMINO]-1-({[2-(DIFLUOROMETHOXY)BENZYL]SULFONYL}METHYL)-2-OXOETHYL MORPHOLINE-4-CARBOXYLATErdf:typedrugbank:drugs
drug:(1R)-2-amino-1-[3-(trifluoromethyl)phenyl]ethanoldrugbank:description" experimental This compound belongs to the benzene and substituted derivatives. These are aromatic compounds containing at least one benzene ring. Benzene and Substituted Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Secondary Alcohols 1,2-Aminoalcohols Polyamines Monoalkylamines Alkyl Fluorides Organofluorides 1,2-aminoalcohol secondary alcohol polyamine primary aliphatic amine amine alcohol primary amine organofluoride organohalogen alkyl halide alkyl fluoride organonitrogen compound logP 1.06 ALOGPS logS -1.4 ALOGPS Water Solubility 7.80e+00 g/l ALOGPS logP 1.35 ChemAxon IUPAC Name (1R)-2-amino-1-[3-(trifluoromethyl)phenyl]ethan-1-ol ChemAxon Traditional IUPAC Name (1R)-2-amino-1-[3-(trifluoromethyl)phenyl]ethanol ChemAxon Molecular Weight 205.177 ChemAxon Monoisotopic Weight 205.071448562 ChemAxon SMILES [H][C@](O)(CN)C1=CC=CC(=C1)C(F)(F)F ChemAxon Molecular Formula C9H10F3NO ChemAxon InChI InChI=1S/C9H10F3NO/c10-9(11,12)7-3-1-2-6(4-7)8(14)5-13/h1-4,8,14H,5,13H2/t8-/m0/s1 ChemAxon InChIKey InChIKey=RRBRWAPWPGAJMA-QMMMGPOBSA-N ChemAxon Polar Surface Area (PSA) 46.25 ChemAxon Refractivity 46.47 ChemAxon Polarizability 17.63 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 14.05 ChemAxon pKa (strongest basic) 9.11 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 36688409 PubChem Substance 99444600 PDB LT5 BE0000865 Phenylethanolamine N-methyltransferase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Phenylethanolamine N-methyltransferase Involved in methyltransferase activity Converts noradrenaline to adrenaline PNMT 17q21-q22 None 5.96 30855.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9160 GenAtlas PNMT GeneCards PNMT GenBank Gene Database J03727 GenBank Protein Database 190142 UniProtKB P11086 UniProt Accession PNMT_HUMAN EC 2.1.1.28 Noradrenaline N-methyltransferase PNMTase >Phenylethanolamine N-methyltransferase MSGADRSPNAGAAPDSAPGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRC LAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEEPGA FNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPLPADALVS AFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVR EALVRSGYKVRDLRTYIMPAHLQTGVDDVKGVFFAWAQKVGL >849 bp ATGAGCGGCGCAGACCGTAGCCCCAATGCGGGCGCAGCCCCTGACTCGGCCCCGGGCCAG GCGGCGGTGGCTTCGGCCTACCAGCGCTTCGAGCCGCGCGCCTACCTCCGCAACAACTAC GCGCCCCCTCGCGGGGACCTGTGCAACCCGAACGGCGTCGGGCCGTGGAAGCTGCGCTGC TTGGCGCAGACCTTCGCCACCGGTGAAGTGTCCGGACGCACCCTCATCGACATTGGTTCA GGCCCCACCGTGTACCAGCTGCTCAGTGCCTGCAGCCACTTTGAGGACATCACCATGACA GATTTCCTGGAGGTCAACCGCCAGGAGCTGGGGCGCTGGCTGCAGGAGGAGCCGGGGGCC TTCAACTGGAGCATGTACAGCCAACATGCCTGCCTCATTGAGGGCAAGGGGGAATGCTGG CAGGATAAGGAGCGCCAGCTGCGAGCCAGGGTGAAACGGGTCCTGCCCATCGACGTGCAC CAGCCCCAGCCCCTGGGTGCTGGGAGCCCAGCTCCCCTGCCTGCTGACGCCCTGGTCTCT GCCTTCTGCTTGGAGGCTGTGAGCCCAGATCTTGCCAGCTTTCAGCGGGCCCTGGACCAC ATCACCACGCTGCTGAGGCCTGGGGGGCACCTCCTCCTCATCGGGGCCCTGGAGGAGTCG TGGTACCTGGCTGGGGAGGCCAGGCTGACGGTGGTGCCAGTGTCTGAGGAGGAGGTGAGG GAGGCCCTGGTGCGTAGTGGCTACAAGGTCCGGGACCTCCGCACCTATATCATGCCTGCC CACCTTCAGACAGGCGTAGATGATGTCAAGGGCGTCTTCTTCGCCTGGGCTCAGAAGGTT GGGCTGTGA PF01234 NNMT_PNMT_TEMT function transferase activity, transferring one-carbon groups function methyltransferase activity function catalytic activity function transferase activity "
drug:(1R)-2-amino-1-[3-(trifluoromethyl)phenyl]ethanolrdfs:label"(1R)-2-amino-1-[3-(trifluoromethyl)phenyl]ethanol"
drug:(1R)-2-amino-1-[3-(trifluoromethyl)phenyl]ethanolrdf:typedrugbank:drugs
drug:(1R)-2-{[AMINO(IMINO)METHYL]AMINO}-1-{4-[(4R)-4-(HYDROXYMETHYL)-1,3,2-DIOXABOROLAN-2-YL]PHENYL}ETHYL NICOTINATEdrugbank:description" experimental This compound belongs to the benzyloxycarbonyls. These are organic compounds containing a carbonyl group substituted with a benzyloxyl group. Benzyloxycarbonyls Organic Compounds Benzenoids Benzene and Substituted Derivatives Benzyloxycarbonyls Pyridinecarboxylic Acids Benzylethers Boronic Acid Esters Dioxaborolanes Guanidines Carboxylic Acid Esters Enolates Dialkyl Ethers Amidines Primary Alcohols Polyamines Organoboron Compounds pyridine boronic acid ester 1,3,2-dioxaborolane guanidine carboxylic acid ester boronic acid derivative amidine primary alcohol dialkyl ether carboxylic acid derivative enolate ether polyamine organic metalloid moeity amine alcohol organonitrogen compound organoboron compound logP 0.79 ALOGPS logS -3.4 ALOGPS Water Solubility 1.52e-01 g/l ALOGPS logP 2.37 ChemAxon IUPAC Name (1R)-2-carbamimidamido-1-{4-[(4R)-4-(hydroxymethyl)-1,3,2-dioxaborolan-2-yl]phenyl}ethyl pyridine-3-carboxylate ChemAxon Traditional IUPAC Name (1R)-2-carbamimidamido-1-{4-[(4R)-4-(hydroxymethyl)-1,3,2-dioxaborolan-2-yl]phenyl}ethyl pyridine-3-carboxylate ChemAxon Molecular Weight 384.194 ChemAxon Monoisotopic Weight 384.160500268 ChemAxon SMILES [H][C@@](CNC(N)=N)(OC(=O)C1=CC=CN=C1)C1=CC=C(C=C1)B1OC[C@@]([H])(CO)O1 ChemAxon Molecular Formula C18H21BN4O5 ChemAxon InChI InChI=1S/C18H21BN4O5/c20-18(21)23-9-16(27-17(25)13-2-1-7-22-8-13)12-3-5-14(6-4-12)19-26-11-15(10-24)28-19/h1-8,15-16,24H,9-11H2,(H4,20,21,23)/t15-,16+/m1/s1 ChemAxon InChIKey InChIKey=HGLWHYRZHMOCMC-CVEARBPZSA-N ChemAxon Polar Surface Area (PSA) 139.78 ChemAxon Refractivity 106.38 ChemAxon Polarizability 40.72 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 8 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 14.65 ChemAxon pKa (strongest basic) 11.7 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 6857688 PubChem Substance 99443494 ChemSpider 5257022 PDB 368 BE0001021 Coagulation factor XI Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Coagulation factor XI Involved in serine-type endopeptidase activity Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX F11 4q35 Secreted protein None 8.14 70110.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3529 GenAtlas F11 GeneCards F11 GenBank Gene Database M13142 GenBank Protein Database 182833 UniProtKB P03951 UniProt Accession FA11_HUMAN Coagulation factor XI precursor EC 3.4.21.27 FXI Plasma thromboplastin antecedent PTA >Coagulation factor XI precursor MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFT FTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDM KGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITK LDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFT FFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTD FLGEELDIVAAKSHEACQKLCTNAVRCQFFTYTPAQASCNEGKGKCYLKLSSNGSPTKIL HGRGGISGYTLRLCKMDNECTTKIKPRIVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSI IGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYD IALLKLETTVNYTDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLV TNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCA QRERPGVYTNVVEYVDWILEKTQAV >1878 bp ATGATTTTCTTATATCAAGTGGTACATTTCATTTTATTTACTTCAGTTTCTGGTGAATGT GTGACTCAGTTGTTGAAGGACACCTGCTTTGAAGGAGGGGACATTACTACGGTCTTCACA CCAAGCGCCAAGTACTGCCAGGTAGTCTGCACTTACCACCCAAGATGTTTACTCTTCACT TTCACGGCGGAATCACCATCTGAGGATCCCACCCGATGGTTTACTTGTGTCCTGAAAGAC AGTGTTACAGAAACACTGCCAAGAGTGAATAGGACAGCAGCGATTTCTGGGTATTCTTTC AAGCAATGCTCACACCAAATAAGCGCTTGCAACAAAGACATTTATGTGGACCTAGACATG AAGGGCATAAACTATAACAGCTCAGTTGCCAAGAGTGCTCAAGAATGCCAAGAAAGATGC ACGGATGACGTCCACTGCCACTTTTTCACGTACGCCACAAGGCAGTTTCCCAGCCTGGAG CATCGTAACATTTGTCTACTGAAGCACACCCAAACAGGGACACCAACCAGAATAACGAAG CTCGATAAAGTGGTGTCTGGATTTTCACTGAAATCCTGTGCACTTTCTAATCTGGCTTGT ATTAGGGACATTTTCCCTAATACGGTGTTTGCAGACAGCAACATCGACAGTGTCATGGCT CCCGATGCTTTTGTCTGTGGCCGAATCTGCACTCATCATCCCGGTTGCTTGTTTTTTACC TTCTTTTCCCAGGAATGGCCCAAAGAATCTCAAAGAAATCTTTGTCTCCTTAAAACATCT GAGAGTGGATTGCCCAGTACACGCATTAAAAAGAGCAAAGCTCTTTCTGGTTTCAGTCTA CAAAGCTGCAGGCACAGCATCCCAGTGTTCTGCCATTCTTCATTTTACCATGACACTGAT TTCTTGGGAGAAGAACTGGATATTGTTGCTGCAAAAAGTCACGAGGCCTGCCAGAAACTG TGCACCAATGCCGTCCGCTGCCAGTTTTTTACCTATACCCCAGCCCAAGCATCCTGCAAC GAAGGGAAGGGCAAGTGTTACTTAAAGCTTTCTTCAAACGGATCTCCAACTAAAATACTT CACGGGAGAGGAGGCATCTCTGGATACACATTAAGGTTGTGTAAAATGGATAATGAGTGT ACCACCAAAATCAAGCCCAGGATCGTTGGAGGAACTGCGTCTGTTCGTGGTGAGTGGCCG TGGCAGGTGACCCTGCACACAACCTCACCCACTCAGAGACACCTGTGTGGAGGCTCCATC ATTGGAAACCAGTGGATATTAACAGCCGCTCACTGTTTCTATGGGGTAGAGTCACCTAAG ATTTTGCGTGTCTACAGTGGCATTTTAAATCAATCTGAAATAAAAGAGGACACATCTTTC TTTGGGGTTCAAGAAATAATAATCCATGATCAGTATAAAATGGCAGAAAGCGGGTATGAT ATTGCCTTGTTGAAACTGGAAACCACAGTGAATTACACAGATTCTCAACGACCCATATGC CTGCCTTCCAAAGGAGATAGAAATGTAATATACACTGATTGCTGGGTGACTGGATGGGGG TACAGAAAACTAAGAGACAAAATACAAAATACTCTCCAGAAAGCCAAGATACCCTTAGTG ACCAACGAAGAGTGCCAGAAGAGATACAGAGGACATAAAATAACCCATAAGATGATCTGT GCCGGCTACAGGGAAGGAGGGAAGGACGCTTGCAAGGGAGATTCGGGAGGCCCTCTGTCC TGCAAACACAATGAGGTCTGGCATCTGGTAGGCATCACGAGCTGGGGCGAAGGCTGTGCT CAAAGGGAGCGGCCAGGTGTTTACACCAACGTGGTCGAGTACGTGGACTGGATTCTGGAG AAAACTCAAGCAGTGTGA PF00089 Trypsin PF00024 PAN_1 component extracellular region function serine-type endopeptidase activity function hydrolase activity function peptidase activity function catalytic activity function endopeptidase activity process metabolism process proteolysis process macromolecule metabolism process protein metabolism process cellular protein metabolism process organismal physiological process process regulation of body fluids process hemostasis process blood coagulation process physiological process "
drug:(1R)-2-{[AMINO(IMINO)METHYL]AMINO}-1-{4-[(4R)-4-(HYDROXYMETHYL)-1,3,2-DIOXABOROLAN-2-YL]PHENYL}ETHYL NICOTINATErdfs:label"(1R)-2-{[AMINO(IMINO)METHYL]AMINO}-1-{4-[(4R)-4-(HYDROXYMETHYL)-1,3,2-DIOXABOROLAN-2-YL]PHENYL}ETHYL NICOTINATE"
drug:(1R)-2-{[AMINO(IMINO)METHYL]AMINO}-1-{4-[(4R)-4-(HYDROXYMETHYL)-1,3,2-DIOXABOROLAN-2-YL]PHENYL}ETHYL NICOTINATErdf:typedrugbank:drugs
drug:(1R)-3-chloro-1-phenylpropan-1-oldrugbank:description" experimental This compound belongs to the benzene and substituted derivatives. These are aromatic compounds containing at least one benzene ring. Benzene and Substituted Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Secondary Alcohols Polyamines Organochlorides Alkyl Chlorides secondary alcohol polyamine organochloride alcohol organohalogen alkyl halide alkyl chloride logP 2.28 ALOGPS logS -1.9 ALOGPS Water Solubility 2.12e+00 g/l ALOGPS logP 1.99 ChemAxon IUPAC Name (1R)-3-chloro-1-phenylpropan-1-ol ChemAxon Traditional IUPAC Name (1R)-3-chloro-1-phenylpropan-1-ol ChemAxon Molecular Weight 170.636 ChemAxon Monoisotopic Weight 170.049842681 ChemAxon SMILES [H][C@@](O)(CCCl)C1=CC=CC=C1 ChemAxon Molecular Formula C9H11ClO ChemAxon InChI InChI=1S/C9H11ClO/c10-7-6-9(11)8-4-2-1-3-5-8/h1-5,9,11H,6-7H2/t9-/m1/s1 ChemAxon InChIKey InChIKey=JZFUHAGLMZWKTF-SECBINFHSA-N ChemAxon Polar Surface Area (PSA) 20.23 ChemAxon Refractivity 46.75 ChemAxon Polarizability 17.96 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 14.44 ChemAxon pKa (strongest basic) -3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 642409 PubChem Substance 99443405 ChemSpider 557611 PDB 269 BE0001248 Lysozyme Enterobacteria phage T4 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Lysozyme Involved in lysozyme activity Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan E Cytoplasmic None 10.08 18636.0 Enterobacteria phage T4 GenBank Gene Database X04567 GenBank Protein Database 15261 UniProtKB P00720 UniProt Accession LYS_BPT4 EC 3.2.1.17 Endolysin Lysis protein Muramidase >Lysozyme MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITK DEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRM LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL >495 bp ATGAATATATTTGAAATGTTACGTATAGATGAACGTCTTAGACTTAAAATCTATAAAGAC ACAGAAGGCTATTACACTATTGGCATCGGTCATTTGCTTACAAAAAGTCCATCACTTAAT GCTGCTAAATCTGAATTAGATAAAGCTATTGGGCGTAATTGCAATGGTGTAATTACAAAA GATGAGGCTGAAAAACTCTTTAATCAGGATGTTGATGCTGCTGTTCGCGGAATTCTGAGA AATGCTAAATTAAAACCGGTTTATGATTCTCTTGATGCGGTTCGTCGCTGTGCATTGATT AATATGGTTTTCCAAATGGGAGAAACCGGTGTGGCAGGATTTACTAACTCTTTACGTATG CTTCAACAAAAACGCTGGGATGAAGCAGCAGTTAACTTAGCTAAAAGTATATGGTATAAT CAAACACCTAATCGCGCAAAACGAGTCATTACAACGTTTAGAACTGGCACTTGGGACGCG TATAAAAATCTATAA PF00959 Phage_lysozyme function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function lysozyme activity function catalytic activity function hydrolase activity process peptidoglycan metabolism process physiological process process catabolism process cellular catabolism process metabolism process cell wall catabolism process peptidoglycan catabolism process macromolecule metabolism process carbohydrate metabolism process cellular carbohydrate metabolism "
drug:(1R)-3-chloro-1-phenylpropan-1-olrdfs:label"(1R)-3-chloro-1-phenylpropan-1-ol"
drug:(1R)-3-chloro-1-phenylpropan-1-olrdf:typedrugbank:drugs
drug:(1R)-4-(3-phenoxyphenyl)-1-phosphonobutane-1-sulfonic aciddrugbank:description" experimental This compound belongs to the diarylethers. These are organic compounds containing the dialkyl ether functional group, with the formula ROR', where R and R' are aryl groups. Diarylethers Organic Compounds Organooxygen Compounds Ethers Diarylethers Phenol Ethers Sulfonic Acids Organic Sulfites Sulfonyls Organic Phosphonic Acids Polyamines phenol ether benzene sulfonic acid sulfonic acid derivative sulfonyl phosphonic acid derivative organic sulfite phosphonic acid polyamine logP 0.94 ALOGPS logS -2.9 ALOGPS Water Solubility 5.35e-01 g/l ALOGPS logP 2.27 ChemAxon IUPAC Name (1R)-4-(3-phenoxyphenyl)-1-phosphonobutane-1-sulfonic acid ChemAxon Traditional IUPAC Name (1R)-4-(3-phenoxyphenyl)-1-phosphonobutane-1-sulfonic acid ChemAxon Molecular Weight 386.357 ChemAxon Monoisotopic Weight 386.058910164 ChemAxon SMILES [H][C@@](CCCC1=CC=CC(OC2=CC=CC=C2)=C1)(P(O)(O)=O)S(O)(=O)=O ChemAxon Molecular Formula C16H19O7PS ChemAxon InChI InChI=1S/C16H19O7PS/c17-24(18,19)16(25(20,21)22)11-5-7-13-6-4-10-15(12-13)23-14-8-2-1-3-9-14/h1-4,6,8-10,12,16H,5,7,11H2,(H2,17,18,19)(H,20,21,22)/t16-/m1/s1 ChemAxon InChIKey InChIKey=RCGCZPXSRLLKCK-MRXNPFEDSA-N ChemAxon Polar Surface Area (PSA) 121.13 ChemAxon Refractivity 92.11 ChemAxon Polarizability 35.9 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) -1.1 ChemAxon pKa (strongest basic) -8.7 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 24748047 PubChem Substance 99443891 PDB B65 BE0003866 Dehydrosqualene synthase Staphylococcus aureus # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dehydrosqualene synthase Lipid transport and metabolism Catalyzes the head-to-head condensation of two molecules of farnesyl diphosphate (FPP) into the colorless C(30) carotenoid dehydrosqualene (4,4'-diapophytoene). This is the initial step in the biosynthesis of staphyloxanthin, an orange carotenoid present in most staphylococci strains crtM None 6.05 34312.8 Staphylococcus aureus GeneCards crtM GenBank Gene Database AM920687 GenBank Protein Database 161788394 UniProtKB A9JQL9 UniProt Accession CRTM_STAAU 4,4'-diapophytoene synthase DAP synthase Diapophytoene synthase >Dehydrosqualene synthase MTMMDMNFKYCHKIMKKHSKSFSYAFDLLPEDQRKAVWAIYAVCRKIDDSIDVYGDIQFL NQIKEDIQSIEKYPYEYHHFQSDRRIMMALQHVAQHKNIAFQSFYNLIDTVYKDQHFTMF ETDAELFGYCYGVAGTVGEVLTPILSDHETHQTYDVARRLGESLQLINILRDVGEDFENE RIYFSKQRLKQYEVDIAEVYQNGVNNHYIDLWEYYAAIAEKDFRDVMDQIKVFSIEAQPI IELAARIYIEILDEVRQANYTLHERVFVEKRKKAKLFHEINSKYHRI PF00494 SQS_PSY function transferase activity function catalytic activity process metabolism process biosynthesis process physiological process "
drug:(1R)-4-(3-phenoxyphenyl)-1-phosphonobutane-1-sulfonic acidrdfs:label"(1R)-4-(3-phenoxyphenyl)-1-phosphonobutane-1-sulfonic acid"
drug:(1R)-4-(3-phenoxyphenyl)-1-phosphonobutane-1-sulfonic acidrdf:typedrugbank:drugs
drug:(1R)-MENTHYL HEXYL PHOSPHONATE GROUPdrugbank:description" experimental This compound belongs to the monocyclic monoterpenes. These are monoterpenes containing 1 ring in the isoprene chain. Monocyclic Monoterpenes Organic Compounds Lipids Prenol Lipids Monoterpenes Phosphonic Acid Esters Organic Phosphonic Acids Polyamines phosphonic acid ester phosphonic acid derivative phosphonic acid polyamine logP 4.34 ALOGPS logS -3.9 ALOGPS Water Solubility 3.84e-02 g/l ALOGPS logP 4.58 ChemAxon IUPAC Name hexyl({[(1R,2S,5R)-5-methyl-2-(propan-2-yl)cyclohexyl]oxy})phosphinic acid ChemAxon Traditional IUPAC Name hexyl[(1R,2S,5R)-2-isopropyl-5-methylcyclohexyl]oxyphosphinic acid ChemAxon Molecular Weight 304.4052 ChemAxon Monoisotopic Weight 304.216731434 ChemAxon SMILES [H][C@@]1(C)CC[C@@]([H])(C(C)C)[C@@]([H])(C1)O[P@](O)(=O)CCCCCC ChemAxon Molecular Formula C16H33O3P ChemAxon InChI InChI=1S/C16H33O3P/c1-5-6-7-8-11-20(17,18)19-16-12-14(4)9-10-15(16)13(2)3/h13-16H,5-12H2,1-4H3,(H,17,18)/t14-,15+,16-/m1/s1 ChemAxon InChIKey InChIKey=WAVIZOVSJOXCKT-OWCLPIDISA-N ChemAxon Polar Surface Area (PSA) 46.53 ChemAxon Refractivity 84.04 ChemAxon Polarizability 35.58 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 1.93 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 446980 PubChem Substance 99444671 ChemSpider 394197 PDB MPA BE0002180 Cholinesterase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cholinesterase Lipid transport and metabolism An acylcholine + H(2)O = choline + a carboxylate BCHE 3q26.1-q26.2 Cytoplasmic None 7.47 68419.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:983 GenAtlas BCHE GeneCards BCHE GenBank Gene Database M32391 GenBank Protein Database 1311630 UniProtKB P06276 UniProt Accession CHLE_HUMAN Acylcholine acylhydrolase Butyrylcholine esterase Choline esterase II Cholinesterase precursor EC 3.1.1.8 Pseudocholinesterase >Cholinesterase MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV GL >1809 bp ATGCATAGCAAAGTCACAATCATATGCATCAGATTTCTCTTTTGGTTTCTTTTGCTCTGC ATGCTTATTGGGAAGTCACATACTGAAGATGACATCATAATTGCAACAAAGAATGGAAAA GTCAGAGGGATGAACTTGACAGTTTTTGGTGGCACGGTAACAGCCTTTCTTGGAATTCCC TATGCACAGCCACCTCTTGGTAGACTTCGATTCAAAAAGCCACAGTCTCTGACCAAGTGG TCTGATATTTGGAATGCCACAAAATATGCAAATTCTTGCTGTCAGAACATAGATCAAAGT TTTCCAGGCTTCCATGGATCAGAGATGTGGAACCCAAACACTGACCTCAGTGAAGACTGT TTATATCTAAATGTATGGATTCCAGCACCTAAACCAAAAAATGCCACTGTATTGATATGG ATTTATGGTGGTGGTTTTCAAACTGGAACATCATCTTTACATGTTTATGATGGCAAGTTT CTGGCTCGGGTTGAAAGAGTTATTGTAGTGTCAATGAACTATAGGGTGGGTGCCCTAGGA TTCTTAGCTTTGCCAGGAAATCCTGAGGCTCCAGGGAACATGGGTTTATTTGATCAACAG TTGGCTCTTCAGTGGGTTCAAAAAAATATAGCAGCCTTTGGTGGAAATCCTAAAAGTGTA ACTCTCTTTGGAGAAAGTGCAGGAGCAGCTTCAGTTAGCCTGCATTTGCTTTCTCCTGGA AGCCATTCATTGTTCACCAGAGCCATTCTGCAAAGTGGATCCTTTAATGCTCCTTGGGCG GTAACATCTCTTTATGAAGCTAGGAACAGAACGTTGAACTTAGCTAAATTGACTGGTTGC TCTAGAGAGAATGAGACTGAAATAATCAAGTGTCTTAGAAATAAAGATCCCCAAGAAATT CTTCTGAATGAAGCATTTGTTGTCCCCTATGGGACTCCTTTGTCAGTAAACTTTGGTCCG ACCGTGGATGGTGATTTTCTCACTGACATGCCAGACATATTACTTGAACTTGGACAATTT AAAAAAACCCAGATTTTGGTGGGTGTTAATAAAGATGAAGGGACAGCTTTTTTAGTCTAT GGTGCTCCTGGCTTCAGCAAAGATAACAATAGTATCATAACTAGAAAAGAATTTCAGGAA GGTTTAAAAATATTTTTTCCAGGAGTGAGTGAGTTTGGAAAGGAATCCATCCTTTTTCAT TACACAGACTGGGTAGATGATCAGAGACCTGAAAACTACCGTGAGGCCTTGGGTGATGTT GTTGGGGATTATAATTTCATATGCCCTGCCTTGGAGTTCACCAAGAAGTTCTCAGAATGG GGAAATAATGCCTTTTTCTACTATTTTGAACACCGATCCTCCAAACTTCCGTGGCCAGAA TGGATGGGAGTGATGCATGGCTATGAAATTGAATTTGTCTTTGGTTTACCTCTGGAAAGA AGAGATAATTACACAAAAGCCGAGGAAATTTTGAGTAGATCCATAGTGAAACGTTGGGCA AATTTTGCAAAATATGGGAATCCAAATGAGACTCAGAACAATAGCACAAGCTGGCCTGTC TTCAAAAGCACTGAACAAAAATATCTAACCTTGAATACAGAGTCAACAAGAATAATGACG AAACTACGTGCTCAACAATGTCGATTCTGGACATCATTTTTTCCAAAAGTCTTGGAAATG ACAGGAAATATTGATGAAGCAGAATGGGAGTGGAAAGCAGGATTCCATCGCTGGAACAAT TACATGATGGACTGGAAAAATCAATTTAACGATTACACTAGCAAGAAAGAAAGTTGTGTG GGTCTCTAA PF00135 COesterase PF08674 AChE_tetra function hydrolase activity function hydrolase activity, acting on ester bonds function carboxylic ester hydrolase activity function cholinesterase activity function catalytic activity "
drug:(1R)-MENTHYL HEXYL PHOSPHONATE GROUPrdfs:label"(1R)-MENTHYL HEXYL PHOSPHONATE GROUP"
drug:(1R)-MENTHYL HEXYL PHOSPHONATE GROUPrdf:typedrugbank:drugs
drug:(1R)-N,6-DIHYDROXY-7-METHOXY-2-[(4-METHOXYPHENYL)SULFONYL]-1,2,3,4-TETRAHYDROISOQUINOLINE-1-CARBOXAMIDEdrugbank:description" experimental This compound belongs to the isoquinolines and derivatives. These are aromatic polycyclic compounds containing an isoquinoline moiety, which consists of a benzene ring fused to a pyridine ring and forming benzo[c]pyridine. Isoquinolines and Derivatives Organic Compounds Heterocyclic Compounds Isoquinolines and Derivatives Methoxyphenols and Derivatives Benzenesulfonamides Anisoles Alkyl Aryl Ethers Sulfonyls Sulfonamides Hydroxamic Acids Polyamines Enolates Enols phenol ether anisole alkyl aryl ether phenol derivative benzene sulfonamide sulfonyl sulfonic acid derivative hydroxamic acid carboxamide group polyamine enolate carboxylic acid derivative enol ether amine organonitrogen compound logP 1.02 ALOGPS logS -2.8 ALOGPS Water Solubility 6.02e-01 g/l ALOGPS logP 1.05 ChemAxon IUPAC Name (1R)-N,6-dihydroxy-7-methoxy-2-[(4-methoxybenzene)sulfonyl]-1,2,3,4-tetrahydroisoquinoline-1-carboxamide ChemAxon Traditional IUPAC Name (1R)-N,6-dihydroxy-7-methoxy-2-(4-methoxybenzenesulfonyl)-3,4-dihydro-1H-isoquinoline-1-carboxamide ChemAxon Molecular Weight 408.426 ChemAxon Monoisotopic Weight 408.099121694 ChemAxon SMILES [H][C@]1(N(CCC2=CC(O)=C(OC)C=C12)S(=O)(=O)C1=CC=C(OC)C=C1)C(=O)NO ChemAxon Molecular Formula C18H20N2O7S ChemAxon InChI InChI=1S/C18H20N2O7S/c1-26-12-3-5-13(6-4-12)28(24,25)20-8-7-11-9-15(21)16(27-2)10-14(11)17(20)18(22)19-23/h3-6,9-10,17,21,23H,7-8H2,1-2H3,(H,19,22)/t17-/m1/s1 ChemAxon InChIKey InChIKey=AYFCYVLVRYQGME-QGZVFWFLSA-N ChemAxon Polar Surface Area (PSA) 125.4 ChemAxon Refractivity 100.26 ChemAxon Polarizability 40.33 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 8.64 ChemAxon pKa (strongest basic) -4.6 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 15942651 PubChem Substance 99444641 ChemSpider 13085320 PDB MDW BE0003690 Matrilysin Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Matrilysin Involved in calcium ion binding Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase MMP7 11q21-q22 Secreted, extracellular space, extracellular matrix (Probable) None 8.09 29676.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:7174 GeneCards MMP7 GenBank Gene Database X07819 GenBank Protein Database 35799 UniProtKB P09237 UniProt Accession MMP7_HUMAN Matrin Matrix metalloproteinase-7 MMP-7 Pump-1 protease Uterine metalloproteinase >Matrilysin MRLTVLCAVCLLPGSLALPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLK EMQKFFGLPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYTRDL PHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAF APGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGD PQNFKLSQDDIKGIQKLYGKRSNSRKK >804 bp ATGCGACTCACCGTGCTGTGTGCTGTGTGCCTGCTGCCTGGCAGCCTGGCCCTGCCGCTG CCTCAGGAGGCGGGAGGCATGAGTGAGCTACAGTGGGAACAGGCTCAGGACTATCTCAAG AGATTTTATCTCTATGACTCAGAAACAAAAAATGCCAACAGTTTAGAAGCCAAACTCAAG GAGATGCAAAAATTCTTTGGCCTACCTATAACTGGAATGTTAAACTCCCGCGTCATAGAA ATAATGCAGAAGCCCAGATGTGGAGTGCCAGATGTTGCAGAATACTCACTATTTCCAAAT AGCCCAAAATGGACTTCCAAAGTGGTCACCTACAGGATCGTATCATATACTCGAGACTTA CCGCATATTACAGTGGATCGATTAGTGTCAAAGGCTTTAAACATGTGGGGCAAAGAGATC CCCCTGCATTTCAGGAAAGTTGTATGGGGAACTGCTGACATCATGATTGGCTTTGCGCGA GGAGCTCATGGGGACTCCTACCCATTTGATGGGCCAGGAAACACGCTGGCTCATGCCTTT GCGCCTGGGACAGGTCTCGGAGGAGATGCTCACTTCGATGAGGATGAACGCTGGACGGAT GGTAGCAGTCTAGGGATTAACTTCCTGTATGCTGCAACTCATGAACTTGGCCATTCTTTG GGTATGGGACATTCCTCTGATCCTAATGCAGTGATGTATCCAACCTATGGAAATGGAGAT CCCCAAAATTTTAAACTTTCCCAGGATGATATTAAAGGCATTCAGAAACTATATGGAAAG AGAAGTAATTCAAGAAAGAAATAG PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix component extracellular matrix (sensu Metazoa) function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding function catalytic activity function hydrolase activity process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism "
drug:(1R)-N,6-DIHYDROXY-7-METHOXY-2-[(4-METHOXYPHENYL)SULFONYL]-1,2,3,4-TETRAHYDROISOQUINOLINE-1-CARBOXAMIDErdfs:label"(1R)-N,6-DIHYDROXY-7-METHOXY-2-[(4-METHOXYPHENYL)SULFONYL]-1,2,3,4-TETRAHYDROISOQUINOLINE-1-CARBOXAMIDE"
drug:(1R)-N,6-DIHYDROXY-7-METHOXY-2-[(4-METHOXYPHENYL)SULFONYL]-1,2,3,4-TETRAHYDROISOQUINOLINE-1-CARBOXAMIDErdf:typedrugbank:drugs
drug:(1R, 2S)-CIS 1,2 DIHYDROXY-1,2-DIHYDRONAPHTHALENEdrugbank:description" experimental This compound belongs to the naphthalenes. These are compounds containing a naphthalene moiety, which consists of two fused benzene rings. Naphthalenes Organic Compounds Benzenoids Acenes and Derivatives Naphthalenes Benzene and Substituted Derivatives Secondary Alcohols 1,2-Diols Polyamines benzene 1,2-diol secondary alcohol polyamine alcohol logP 0.63 ALOGPS logS -0.86 ALOGPS Water Solubility 2.25e+01 g/l ALOGPS logP 1 ChemAxon IUPAC Name (1R,2S)-1,2-dihydronaphthalene-1,2-diol ChemAxon Traditional IUPAC Name (1R,2S)-1,2-dihydronaphthalene-1,2-diol ChemAxon Molecular Weight 162.1852 ChemAxon Monoisotopic Weight 162.068079564 ChemAxon SMILES [H][C@]1(O)C=CC2=C(C=CC=C2)[C@@]1([H])O ChemAxon Molecular Formula C10H10O2 ChemAxon InChI InChI=1S/C10H10O2/c11-9-6-5-7-3-1-2-4-8(7)10(9)12/h1-6,9-12H/t9-,10+/m0/s1 ChemAxon InChIKey InChIKey=QPUHWUSUBHNZCG-VHSXEESVSA-N ChemAxon Polar Surface Area (PSA) 40.46 ChemAxon Refractivity 47.38 ChemAxon Polarizability 16.89 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 13.2 ChemAxon pKa (strongest basic) -3.4 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon ChEBI 44343 PubChem Compound 440294 PubChem Substance 99444735 ChemSpider 389268 PDB NDH BE0004259 Naphthalene 1,2-dioxygenase subunit alpha Pseudomonas putida # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Naphthalene 1,2-dioxygenase subunit alpha Inorganic ion transport and metabolism Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis- naphthalene dihydrodiol ndoB None 5.86 49607.2 Pseudomonas putida GeneCards ndoB GenBank Gene Database M23914 GenBank Protein Database 151393 UniProtKB P0A110 UniProt Accession NDOB_PSEPU Naphthalene 1,2-dioxygenase ISP alpha >Naphthalene 1,2-dioxygenase subunit alpha MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMG IDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFE KDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGL ELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGL QMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTV FPNNSMLTCSGVFKVWNPIDANTTEVWTYAIVEKDMPEDLKRRLADSVQRTFGPAGFWES DDNDNMETASQNGKKYQSRDSDLLSNLGFGEDVYGDAVYPGVVGKSAIGETSYRGFYRAY QAHVSSSNWAEFEHASSTWHTELTKTTDR >315 bp TACCCCATCTGAGGATTGCTTTATGACAGTAAAGTGGATTGAAGCAGTCGCTCTTTCTGA CATCCTTGAAGGTGACGTCCTCGGCGTGACTGTCGAGGGCAAGGAGCTGGCGCTGTATGA AGTTGAAGGCGAAATCTACGCTACCGACAACCTGTGCACGCATGGTTCCGCCCGCATGAG TGATGGTTATCTCGAGGGTAGAGAAATCGAATGCCCCTTGCATCAAGGTCGGTTTGACGT TTGCACAGGCAAAGCCCTGTGCGCACCCGTGACACAGAACATCAAAACATATCCAGTCAA GATTGAGAACCTGCG PF00355 Rieske PF00848 Ring_hydroxyl_A function binding function ion binding function cation binding function transition metal ion binding function iron ion binding process generation of precursor metabolites and energy process electron transport process aromatic compound metabolism process physiological process process metabolism process cellular metabolism BE0004260 Naphthalene 1,2-dioxygenase subunit beta Pseudomonas putida # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Naphthalene 1,2-dioxygenase subunit beta Involved in naphthalene 1,2-dioxygenase activity Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis- naphthalene dihydrodiol. The beta subunit may be responsible for the substrate specificity of the enzyme ndoC None 7.73 22934.9 Pseudomonas putida GeneCards ndoC GenBank Gene Database M23914 GenBank Protein Database 151393 UniProtKB P0A112 UniProt Accession NDOC_PSEPU Naphthalene 1,2-dioxygenase ISP beta >Naphthalene 1,2-dioxygenase subunit beta MMINIQEDKLVSAHDAEEILRFFNCHDSALQQEATTLLTQEAHLLDIQAYRAWLEHCVGS EVQYQVISRELRAASERRYKLNEAMNVYNENFQQLKVRVEHQLDPQNWGNSPKLRFTRFI TNVQAAMDVNDKELLHIRSNVILHRARRGNQVDVFYAAREDKWKRGEGGVRKLVQRFVDY PERILQTHNLMVFL >315 bp TACCCCATCTGAGGATTGCTTTATGACAGTAAAGTGGATTGAAGCAGTCGCTCTTTCTGA CATCCTTGAAGGTGACGTCCTCGGCGTGACTGTCGAGGGCAAGGAGCTGGCGCTGTATGA AGTTGAAGGCGAAATCTACGCTACCGACAACCTGTGCACGCATGGTTCCGCCCGCATGAG TGATGGTTATCTCGAGGGTAGAGAAATCGAATGCCCCTTGCATCAAGGTCGGTTTGACGT TTGCACAGGCAAAGCCCTGTGCGCACCCGTGACACAGAACATCAAAACATATCCAGTCAA GATTGAGAACCTGCG PF00866 Ring_hydroxyl_B function catalytic activity process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process aromatic compound metabolism process physiological process "
drug:(1R, 2S)-CIS 1,2 DIHYDROXY-1,2-DIHYDRONAPHTHALENErdfs:label"(1R, 2S)-CIS 1,2 DIHYDROXY-1,2-DIHYDRONAPHTHALENE"
drug:(1R, 2S)-CIS 1,2 DIHYDROXY-1,2-DIHYDRONAPHTHALENErdf:typedrugbank:drugs
drug:(1R,2R)-N-(2-AMINOETHYL)-2-{[(4-METHOXYPHENYL)SULFONYL]METHYL}CYCLOHEXANECARBOXAMIDEdrugbank:description" experimental This compound belongs to the anisoles. These are organic compounds contaiing a methoxybenzene or a derivative thereof. Anisoles Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenol Ethers Alkyl Aryl Ethers Sulfones Sulfoxides Secondary Carboxylic Acid Amides Enolates Polyamines Carboxylic Acids Monoalkylamines alkyl aryl ether sulfonyl sulfone sulfoxide secondary carboxylic acid amide carboxamide group enolate carboxylic acid derivative ether carboxylic acid polyamine primary aliphatic amine amine primary amine organonitrogen compound logP 0.96 ALOGPS logS -3 ALOGPS Water Solubility 3.15e-01 g/l ALOGPS logP 0.76 ChemAxon IUPAC Name (1R,2R)-N-(2-aminoethyl)-2-{[(4-methoxybenzene)sulfonyl]methyl}cyclohexane-1-carboxamide ChemAxon Traditional IUPAC Name (1R,2R)-N-(2-aminoethyl)-2-[(4-methoxybenzenesulfonyl)methyl]cyclohexane-1-carboxamide ChemAxon Molecular Weight 354.464 ChemAxon Monoisotopic Weight 354.16132802 ChemAxon SMILES [H][C@@]1(CS(=O)(=O)C2=CC=C(OC)C=C2)CCCC[C@@]1([H])C(=O)NCCN ChemAxon Molecular Formula C17H26N2O4S ChemAxon InChI InChI=1S/C17H26N2O4S/c1-23-14-6-8-15(9-7-14)24(21,22)12-13-4-2-3-5-16(13)17(20)19-11-10-18/h6-9,13,16H,2-5,10-12,18H2,1H3,(H,19,20)/t13-,16+/m0/s1 ChemAxon InChIKey InChIKey=QTGNVZPFJQOWFL-XJKSGUPXSA-N ChemAxon Polar Surface Area (PSA) 98.49 ChemAxon Refractivity 93.1 ChemAxon Polarizability 38.31 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 14.96 ChemAxon pKa (strongest basic) 8.76 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11840970 PubChem Substance 99444758 ChemSpider 10015473 PDB NOQ BE0003417 Cathepsin K Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cathepsin K Involved in cysteine-type endopeptidase activity Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation CTSK 1q21 Lysosome None 8.65 36966.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:2536 GenAtlas CTSK GenBank Gene Database U13665 UniProtKB P43235 UniProt Accession CATK_HUMAN Cathepsin K precursor Cathepsin O Cathepsin O2 Cathepsin X EC 3.4.22.38 >Cathepsin K MWGLKVLLLPVVSFALYPEEILDTHWELWKKTHRKQYNNKVDEISRRLIWEKNLKYISIH NLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPLSHSRSNDTLYIPEWEGRAPDSVD YRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGG YMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVA RVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGE NWGNKGYILMARNKNNACGIANLASFPKM >990 bp ATGTGGGGGCTCAAGGTTCTGCTGCTACCTGTGGTGAGCTTTGCTCTGTACCCTGAGGAG ATACTGGACACCCACTGGGAGCTATGGAAGAAGACCCACAGGAAGCAATATAACAACAAG GTGGATGAAATCTCTCGGCGTTTAATTTGGGAAAAAAACCTGAAGTATATTTCCATCCAT AACCTTGAGGCTTCTCTTGGTGTCCATACATATGAACTGGCTATGAACCACCTGGGGGAC ATGACCAGTGAAGAGGTGGTTCAGAAGATGACTGGACTCAAAGTACCCCTGTCTCATTCC CGCAGTAATGACACCCTTTATATCCCAGAATGGGAAGGTAGAGCCCCAGACTCTGTCGAC TATCGAAAGAAAGGATATGTTACTCCTGTCAAAAATCAGGGTCAGTGTGGTTCCTGTTGG GCTTTTAGCTCTGTGGGTGCCCTGGAGGGCCAACTCAAGAAGAAAACTGGCAAACTCTTA AATCTGAGTCCCCAGAACCTAGTGGATTGTGTGTCTGAGAATGATGGCTGTGGAGGGGGC TACATGACCAATGCCTTCCAATATGTGCAGAAGAACCGGGGTATTGACTCTGAAGATGCC TACCCATATGTGGGACAGGAAGAGAGTTGTATGTACAACCCAACAGGCAAGGCAGCTAAA TGCAGAGGGTACAGAGAGATCCCCGAGGGGAATGAGAAAGCCCTGAAGAGGGCAGTGGCC CGAGTGGGACCTGTCTCTGTGGCCATTGATGCAAGCCTGACCTCCTTCCAGTTTTACAGC AAAGGTGTGTATTATGATGAAAGCTGCAATAGCGATAATCTGAACCATGCGGTTTTGGCA GTGGGATATGGAATCCAGAAGGGAAACAAGCACTGGATAATTAAAAACAGCTGGGGAGAA AACTGGGGAAACAAAGGATATATCCTCATGGCTCGAAATAAGAACAACGCCTGTGGCATT GCCAACCTGGCCAGCTTCCCCAAGATGTGA PF00112 Peptidase_C1 PF08246 Inhibitor_I29 function endopeptidase activity function cysteine-type endopeptidase activity function cysteine-type peptidase activity function catalytic activity function hydrolase activity function peptidase activity process proteolysis process physiological process process metabolism process macromolecule metabolism process protein metabolism process cellular protein metabolism "
drug:(1R,2R)-N-(2-AMINOETHYL)-2-{[(4-METHOXYPHENYL)SULFONYL]METHYL}CYCLOHEXANECARBOXAMIDErdfs:label"(1R,2R)-N-(2-AMINOETHYL)-2-{[(4-METHOXYPHENYL)SULFONYL]METHYL}CYCLOHEXANECARBOXAMIDE"
drug:(1R,2R)-N-(2-AMINOETHYL)-2-{[(4-METHOXYPHENYL)SULFONYL]METHYL}CYCLOHEXANECARBOXAMIDErdf:typedrugbank:drugs
drug:(1R,2R,3R,4S,5R)-4-(BENZYLAMINO)-5-(METHYLTHIO)CYCLOPENTANE-1,2,3-TRIOLdrugbank:description" experimental This compound belongs to the aminocyclitols and derivatives. These are cyclitols with at least one hydroxyl group replace by an amino group. Aminocyclitols and Derivatives Organic Compounds Organooxygen Compounds Alcohols and Polyols Cyclic Alcohols and Derivatives Benzene and Substituted Derivatives Secondary Alcohols 1,2-Diols 1,2-Aminoalcohols Dialkylamines Polyamines Thioethers benzene 1,2-diol secondary alcohol 1,2-aminoalcohol polyol thioether secondary amine polyamine secondary aliphatic amine amine organonitrogen compound logP -0.01 ALOGPS logS -1.7 ALOGPS Water Solubility 5.64e+00 g/l ALOGPS logP 0.24 ChemAxon IUPAC Name (1R,2R,3R,4S,5R)-4-(benzylamino)-5-(methylsulfanyl)cyclopentane-1,2,3-triol ChemAxon Traditional IUPAC Name (1R,2R,3R,4S,5R)-4-(benzylamino)-5-(methylsulfanyl)cyclopentane-1,2,3-triol ChemAxon Molecular Weight 269.36 ChemAxon Monoisotopic Weight 269.108564169 ChemAxon SMILES [H][C@@]1(O)[C@]([H])(O)[C@]([H])(NCC2=CC=CC=C2)[C@@]([H])(SC)[C@]1([H])O ChemAxon Molecular Formula C13H19NO3S ChemAxon InChI InChI=1S/C13H19NO3S/c1-18-13-9(10(15)11(16)12(13)17)14-7-8-5-3-2-4-6-8/h2-6,9-17H,7H2,1H3/t9-,10+,11+,12+,13+/m0/s1 ChemAxon InChIKey InChIKey=CHTYSDQNKZIWBZ-ZOLYEBIHSA-N ChemAxon Polar Surface Area (PSA) 72.72 ChemAxon Refractivity 71.72 ChemAxon Polarizability 28.75 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 12.88 ChemAxon pKa (strongest basic) 8.25 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 6914612 PubChem Substance 99443455 ChemSpider 5290492 PDB 2SK BE0003505 Alpha-mannosidase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Alpha-mannosidase 2 Carbohydrate transport and metabolism Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway MAN2A1 Golgi apparatus membrane 6-26 7.61 131142.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6824 GenAtlas MAN2A1 GenBank Gene Database D63998 UniProtKB Q16706 UniProt Accession MA2A1_HUMAN Alpha-mannosidase II EC 3.2.1.114 Golgi alpha- mannosidase II MAN II Mannosidase alpha class 2A member 1 Mannosyl- oligosaccharide 1,3-1,6-alpha-mannosidase >Alpha-mannosidase 2 MKLSRQFTVFGSAIFCVVIFSLYLMLDRGHLDYPRNPRREGSFPQGQLSMLQEKIDHLER LLAENNEIISNIRDSVINLSESVEDGPKSSQSNFSQGAGSHLLPSQLSLSVDTADCLFAS QSGSHNSDVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGW LKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIEN GQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYL LNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTC GPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLL APLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRD KGQSMFPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAH KYKINKFLSSSLYTALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKIIG NSAFLLILKDKLTYDSYSPDTFLEMDLKQKSQDSLPQKNIIRLSAEPRYLVVYNPLEQDR ISLVSVYVSSPTVQVFSASGKPVEVQVSAVWDTANTISETAYEISFRAHIPPLGLKVYKI LESASSNSHLADYVLYKNKVEDSGIFTIKNMINTEEGITLENSFVLLRFDQTGLMKQMMT KEDGKHHEVNVQFSWYGTTIKRDKSGAYLFLPDGNAKPYVYTTPPFVRVTHGRIYSEVTC FFDHVTHRVRLYHIQGIEGQSVEVSNIVDIRKVYNREIAMKISSDIKSQNRFYTDLNGYQ IQPRMTLSKLPLQANVYPMTTMAYIQDAKHRLTLLSAQSLGVSSLNSGQIEVIMDRRLMQ DDNRGLEQGIQDNKITANLFRILLEKRSAVNTEEEKKSVSYPSLLSHITSSLMNHPVIPM ANKFSSPTLELQGEFSPLQSSLPCDIHLVNLRTIQSKVGNGHSNEAALILHRKGFDCRFS SKGTGLFCSTTQGKILVQKLLNKFIVESLTPSSLSLMHSPPGTQNISEINLSPMEISTFR IQLR PF09261 Alpha-mann_mid PF01074 Glyco_hydro_38 PF07748 Glyco_hydro_38C function mannosidase activity function alpha-mannosidase activity function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity process metabolism process cellular metabolism process macromolecule metabolism process carbohydrate metabolism process alcohol metabolism process monosaccharide metabolism process hexose metabolism process physiological process process mannose metabolism "
drug:(1R,2R,3R,4S,5R)-4-(BENZYLAMINO)-5-(METHYLTHIO)CYCLOPENTANE-1,2,3-TRIOLrdfs:label"(1R,2R,3R,4S,5R)-4-(BENZYLAMINO)-5-(METHYLTHIO)CYCLOPENTANE-1,2,3-TRIOL"
drug:(1R,2R,3R,4S,5R)-4-(BENZYLAMINO)-5-(METHYLTHIO)CYCLOPENTANE-1,2,3-TRIOLrdf:typedrugbank:drugs
drug:(1R,2S)-2-(5-thioxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)cyclohexanecarboxylic aciddrugbank:description" experimental This compound belongs to the triazoles. These are compounds containing a five-member aromatic ring of two carbon atoms and three nitrogen atoms. Triazoles Organic Compounds Heterocyclic Compounds Azoles Triazoles Polyamines Enolates Carboxylic Acids carboxylic acid derivative enolate carboxylic acid polyamine organonitrogen compound logP 1.31 ALOGPS logS -2.8 ALOGPS Water Solubility 3.32e-01 g/l ALOGPS logP 1.67 ChemAxon IUPAC Name (1R,2S)-2-(5-sulfanylidene-4,5-dihydro-1H-1,2,4-triazol-3-yl)cyclohexane-1-carboxylic acid ChemAxon Traditional IUPAC Name (1R,2S)-2-(5-sulfanylidene-1,4-dihydro-1,2,4-triazol-3-yl)cyclohexane-1-carboxylic acid ChemAxon Molecular Weight 227.283 ChemAxon Monoisotopic Weight 227.072847365 ChemAxon SMILES [H][C@]1(CCCC[C@]1([H])C1=NNC(=S)N1)C(O)=O ChemAxon Molecular Formula C9H13N3O2S ChemAxon InChI InChI=1S/C9H13N3O2S/c13-8(14)6-4-2-1-3-5(6)7-10-9(15)12-11-7/h5-6H,1-4H2,(H,13,14)(H2,10,11,12,15)/t5-,6+/m0/s1 ChemAxon InChIKey InChIKey=DYLXWYPNDHPRPQ-NTSWFWBYSA-N ChemAxon Polar Surface Area (PSA) 73.72 ChemAxon Refractivity 58.6 ChemAxon Polarizability 23.14 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 4.51 ChemAxon pKa (strongest basic) -2.4 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 976666 PubChem Substance 99444321 ChemSpider 846438 PDB GTC BE0001358 Beta-lactamase Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-lactamase Defense mechanisms and antibiotic degradation This protein is a serine beta-lactamase with a substrate specificity for cephalosporins ampC Periplasm None 9.07 41556.0 Escherichia coli (strain K12) GenBank Gene Database J01611 GenBank Protein Database 145267 UniProtKB P00811 UniProt Accession AMPC_ECOLI Beta-lactamase precursor Cephalosporinase EC 3.5.2.6 >Beta-lactamase precursor MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWG YADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGI TLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVK PSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVK STIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSII NGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNY PNPARVDAAWQILNALQ >1134 bp ATGTTCAAAACGACGCTCTGCGCCTTATTAATTACCGCCTCTTGCTCCACATTTGCTGCC CCTCAACAAATCAACGATATTGTGCATCGCACAATTACCCCGCTTATAGAGCAACAAAAG ATCCCGGGTATGGCGGTGGCGGTAATTTATCAGGGTAAACCTTATTACTTTACCTGGGGC TATGCGGACATCGCCAAAAAGCAGCCCGTCACACAGCAAACGTTGTTTGAGTTAGGTTCG GTCAGCAAAACATTTACTGGCGTGCTTGGTGGCGACGCTATTGCTCGAGGGGAAATCAAG TTAAGCGATCCCACAACAAAATACTGGCCTGAACTTACCGCTAAACAGTGGAATGGGATC ACACTATTACATCTCGCAACCTACACTGCTGGCGGCCTGCCATTGCAGGTGCCGGATGAG GTGAAATCCTCAAGCGACTTGCTGCGCTTCTATCAAAACTGGCAGCCTGCATGGGCTCCA GGAACACAACGTCTGTATGCCAACTCCAGTATCGGTTTGTTCGGCGCACTGGCTGTGAAG CCGTCTGGTTTGAGTTTTGAGCAGGCGATGCAAACTCGTGTCTTCCAGCCACTCAAACTC AACCATACGTGGATTAATGTACCGCCCGCAGAAGAAAAGAATTACGCCTGGGGATATCGC GAAGGTAAGGCAGTGCATGTTTCGCCTGGGGCGTTAGATGCTGAAGCTTATGGTGTGAAG TCGACCATTGAAGATATGGCCCGCTGGGTGCAAAGCAATTTAAAACCCCTTGATATCAAT GAGAAAACGCTTCAACAAGGGATACAACTGGCACAATCTCGCTACTGGCAAACCGGCGAT ATGTATCAGGGCCTGGGCTGGGAAATGCTGGACTGGCCGGTAAATCCTGACAGCATCATT AACGGCAGTGACAATAAAATTGCACTGGCAGCACGCCCCGTAAAAGCGATTACGCCCCCA ACTCCTGCAGTACGCGCATCATGGGTACATAAAACAGGGGCGACCGGCGGATTTGGTAGC TATGTCGCGTTTATTCCAGAAAAAGAGCTGGGTATCGTGATGCTGGCAAACAAAAACTAT CCCAATCCAGCGAGAGTCGACGCCGCCTGGCAGATTCTTAACGCTCTACAGTAA PF00144 Beta-lactamase component cell component periplasmic space component periplasmic space (sensu Gram-negative Bacteria) function catalytic activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides function beta-lactamase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds process metabolism process cellular metabolism process drug metabolism process antibiotic metabolism process antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process physiological process process response to antibiotic "
drug:(1R,2S)-2-(5-thioxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)cyclohexanecarboxylic acidrdfs:label"(1R,2S)-2-(5-thioxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)cyclohexanecarboxylic acid"
drug:(1R,2S)-2-(5-thioxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)cyclohexanecarboxylic acidrdf:typedrugbank:drugs
drug:(1R,3R)-5-[(2E)-3-{(1S,3R)-2,2,3-trimethyl-3-[6,6,6-trifluoro-5-hydroxy-5-(trifluoromethyl)hex-3-yn-1-yl]cyclopentyl}prop-2-en-1-ylidene]cyclohexane-1,3-dioldrugbank:description" experimental This compound belongs to the iridoids and derivatives. These are monoterpenes containing a skeleton structurally characterized by the presence of a cylopentane fused to a pyran ( forming a 4,7-dimethylcyclopenta[c]pyran), or a derivative where the pentane moiety is open. Iridoids and Derivatives Organic Compounds Lipids Prenol Lipids Monoterpenes Cyclohexanols Ynones Tertiary Alcohols Cyclic Alcohols and Derivatives Fluorohydrins Polyamines Organofluorides Alkyl Fluorides cyclohexanol ynone tertiary alcohol cyclic alcohol halohydrin fluorohydrin secondary alcohol polyamine organohalogen organofluoride alcohol alkyl halide alkyl fluoride logP 5.22 ALOGPS logS -5.7 ALOGPS Water Solubility 1.07e-03 g/l ALOGPS logP 4.98 ChemAxon IUPAC Name (1R,3R)-5-[(2E)-3-[(1S,3R)-2,2,3-trimethyl-3-[6,6,6-trifluoro-5-hydroxy-5-(trifluoromethyl)hex-3-yn-1-yl]cyclopentyl]prop-2-en-1-ylidene]cyclohexane-1,3-diol ChemAxon Traditional IUPAC Name (1R,3R)-5-[(2E)-3-[(1S,3R)-2,2,3-trimethyl-3-[6,6,6-trifluoro-5-hydroxy-5-(trifluoromethyl)hex-3-yn-1-yl]cyclopentyl]prop-2-en-1-ylidene]cyclohexane-1,3-diol ChemAxon Molecular Weight 482.4995 ChemAxon Monoisotopic Weight 482.22556412 ChemAxon SMILES [H][C@]1(CC[C@](C)(CCC#CC(O)(C(F)(F)F)C(F)(F)F)C1(C)C)\C=C\C=C1C[C@](O)([H])C[C@@](O)([H])C1 ChemAxon Molecular Formula C24H32F6O3 ChemAxon InChI InChI=1S/C24H32F6O3/c1-20(2)17(8-6-7-16-13-18(31)15-19(32)14-16)9-12-21(20,3)10-4-5-11-22(33,23(25,26)27)24(28,29)30/h6-8,17-19,31-33H,4,9-10,12-15H2,1-3H3/b8-6+/t17-,18-,19-,21+/m1/s1 ChemAxon InChIKey InChIKey=PCHUQQNKOFNVDU-OSXMSNBXSA-N ChemAxon Polar Surface Area (PSA) 60.69 ChemAxon Refractivity 115.82 ChemAxon Polarizability 45.78 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 6.43 ChemAxon pKa (strongest basic) -2.7 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 10457944 PubChem Substance 99444001 ChemSpider 8633358 PDB C5D BE0003728 Nuclear receptor coactivator 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Nuclear receptor coactivator 1 Involved in androgen receptor binding Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3 NCOA1 2p23 Nucleus (By similarity) None 6.1 156755.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:7668 GeneCards NCOA1 GenBank Gene Database U59302 GenBank Protein Database 1480646 UniProtKB Q15788 UniProt Accession NCOA1_HUMAN NCoA-1 Protein Hin-2 Renal carcinoma antigen NY-REN-52 RIP160 SRC-1 Steroid receptor coactivator 1 >Nuclear receptor coactivator 1 MSGLGDSSSDPANPDSHKRKGSPCDTLASSTEKRRREQENKYLEELAELLSANISDIDSL SVKPDKCKILKKTVDQIQLMKRMEQEKSTTDDDVQKSDISSSSQGVIEKESLGPLLLEAL DGFFFVVNCEGRIVFVSENVTSYLGYNQEELMNTSVYSILHVGDHAEFVKNLLPKSLVNG VPWPQEATRRNSHTFNCRMLIHPPDEPGTENQEACQRYEVMQCFTVSQPKSIQEDGEDFQ SCLICIARRLPRPPAITGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFF QPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTKCKLCYPQSPDMQPFIMG IHIIDREHSGLSPQDDTNSGMSIPRVNPSVNPSISPAHGVARSSTLPPSNSNMVSTRINR QQSSDLHSSSHSNSSNSQGSFGCSPGSQIVANVALNQGQASSQSSNPSLNLNNSPMEGTG ISLAQFMSPRRQVTSGLATRPRMPNNSFPPNISTLSSPVGMTSSACNNNNRSYSNIPVTS LQGMNEGPNNSVGFSASSPVLRQMSSQNSPSRLNIQPAKAESKDNKEIASILNEMIQSDN SSSDGKPLDSGLLHNNDRLSDGDSKYSQTSHKLVQLLTTTAEQQLRHADIDTSCKDVLSC TGTSNSASANSSGGSCPSSHSSLTERHKILHRLLQEGSPSDITTLSVEPDKKDSASTSVS VTGQVQGNSSIKLELDASKKKESKDHQLLRYLLDKDEKDLRSTPNLSLDDVKVKVEKKEQ MDPCNTNPTPMTKPTPEEIKLEAQSQFTADLDQFDQLLPTLEKAAQLPGLCETDRMDGAV TSVTIKSEILPASLQSATARPTSRLNRLPELELEAIDNQFGQPGTGDQIPWTNNTVTAIN QSKSEDQCISSQLDELLCPPTTVEGRNDEKALLEQLVSFLSGKDETELAELDRALGIDKL VQGGGLDVLSERFPPQQATPPLIMEERPNLYSQPYSSPSPTANLPSPFQGMVRQKPSLGT MPVQVTPPRGAFSPGMGMQPRQTLNRPPAAPNQLRLQLQQRLQGQQQLIHQNRQAILNQF AATAPVGINMRSGMQQQITPQPPLNAQMLAQRQRELYSQQHRQRQLIQQQRAMLMRQQSF GNNLPPSSGLPVQMGNPRLPQGAPQQFPYPPNYGTNPGTPPASTSPFSQLAANPEASLAN RNSMVSRGMTGNIGGQFGTGINPQMQQNVFQYPGAGMVPQGEANFAPSLSPGSSMVPMPI PPPQSSLLQQTPPASGYQSPDMKAWQQGAIGNNNVFSQAVQNQPTPAQPGVYNNMSITVS MAGGNTNVQNMNPMMAQMQMSSLQMPGMNTVCPEQINDPALRHTGLYCNQLSSTDLLKTE ADGTQQVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLT E >4323 bp ATGAGTGGCCTCGGGGACAGTTCATCCGACCCTGCTAACCCAGACTCACATAAGAGGAAA GGATCGCCATGTGACACACTGGCATCAAGCACGGAAAAGAGGCGCAGGGAGCAAGAAAAT AAATATTTAGAAGAACTAGCTGAGTTACTGTCTGCCAACATTAGTGACATTGACAGCTTG AGTGTAAAACCAGACAAATGCAAGATTTTGAAGAAAACAGTCGATCAGATACAGCTAATG AAGAGAATGGAACAAGAGAAATCAACAACTGATGACGATGTACAGAAATCAGACATCTCA TCAAGTAGTCAAGGAGTGATAGAAAAGGAATCCTTGGGACCCCTTCTTTTGGAGGCTTTG GATGGATTTTTCTTTGTTGTGAACTGTGAAGGGAGAATTGTATTTGTGTCAGAGAATGTA ACCAGCTACTTAGGTTACAATCAGGAGGAATTAATGAATACCAGCGTCTACAGCATACTG CACGTGGGGGATCATGCAGAATTTGTGAAGAATCTGCTACCAAAATCACTAGTAAATGGA GTTCCTTGGCCTCAAGAGGCAACACGACGAAATAGCCATACCTTTAACTGCAGGATGCTA ATTCACCCTCCAGATGAGCCAGGGACCGAGAACCAAGAAGCTTGCCAGCGTTATGAAGTA ATGCAGTGTTTCACTGTGTCACAGCCAAAATCAATTCAAGAGGATGGAGAAGATTTCCAG TCATGTCTGATTTGTATTGCACGGCGATTACCTCGGCCTCCAGCTATTACGGGTGTAGAA TCCTTTATGACCAAGCAAGATACTACAGGTAAAATCATCTCTATTGATACTAGTTCCCTG AGAGCTGCTGGCAGAACTGGTTGGGAAGATTTAGTGAGGAAGTGCATTTATGCTTTTTTC CAACCTCAGGGCAGAGAACCATCTTATGCCAGACAGCTGTTCCAAGAAGTGATGACTCGT GGCACTGCCTCCAGCCCCTCCTATAGATTCATATTGAATGATGGGACAATGCTTAGCGCC CACACCAAGTGTAAACTTTGCTACCCTCAAAGTCCAGACATGCAACCTTTCATCATGGGA ATTCATATCATCGACAGGGAGCACAGTGGGCTTTCTCCTCAAGATGACACTAATTCTGGA ATGTCAATTCCCCGAGTAAATCCCTCGGTCAATCCTAGTATCTCTCCAGCTCATGGTGTG GCTCGTTCATCCACATTGCCACCATCCAACAGCAACATGGTATCCACCAGAATAAACCGC CAGCAGAGCTCAGACCTTCATAGCAGCAGTCATAGTAATTCTAGCAACAGCCAAGGAAGT TTCGGATGCTCACCCGGAAGTCAGATTGTAGCCAATGTTGCCTTAAACCAAGGACAGGCC AGTTCACAGAGCAGTAATCCCTCTTTAAACCTCAATAATTCTCCTATGGAAGGTACAGGA ATATCCCTAGCACAGTTCATGTCTCCAAGGAGACAGGTTACTTCTGGATTGGCAACAAGG CCCAGGATGCCAAACAATTCCTTTCCTCCTAATATTTCGACATTAAGCTCTCCCGTTGGC ATGACAAGTAGTGCCTGTAATAATAATAACCGATCTTATTCAAACATCCCAGTAACATCT TTACAGGGTATGAATGAAGGACCCAATAACTCCGTTGGCTTCTCTGCCAGTTCTCCAGTC CTCAGGCAGATGAGCTCACAGAATTCACCTAGCAGATTAAATATACAACCAGCAAAAGCT GAGTCCAAAGATAACAAAGAGATTGCCTCAATTTTAAATGAAATGATTCAATCTGACAAC AGCTCTAGTGATGGCAAACCTCTGGATTCAGGGCTTCTGCATAACAATGACAGACTTTCA GATGGAGACAGTAAATACTCTCAAACCAGTCACAAACTAGTGCAGCTTTTGACAACAACT GCCGAACAGCAGTTACGGCATGCTGATATAGACACAAGCTGCAAAGATGTCCTGTCTTGC ACAGGCACTTCCAACTCTGCCTCTGCTAACTCTTCAGGAGGTTCTTGTCCCTCTTCTCAT AGCTCATTGACAGAACGGCATAAAATTCTACACCGGCTCTTACAGGAGGGTAGCCCCTCA GATATCACCACTTTGTCTGTCGAGCCTGATAAAAAGGACAGTGCATCTACTTCTGTGTCA GTGACTGGACAGGTACAAGGAAACTCCAGTATAAAACTAGAACTGGATGCTTCAAAGAAA AAAGAATCAAAAGACCATCAGCTCCTACGCTATCTTTTAGATAAAGATGAGAAAGATTTA AGATCAACTCCAAACCTGAGCCTGGATGATGTAAAGGTGAAAGTGGAAAAGAAAGAACAG ATGGATCCATGTAATACAAACCCAACCCCAATGACCAAACCCACTCCTGAGGAAATAAAA CTGGAGGCCCAGAGCCAGTTTACAGCTGACCTTGACCAGTTTGATCAGTTACTGCCCACG CTGGAGAAGGCAGCACAGTTGCCAGGCTTATGTGAGACAGACAGGATGGATGGTGCGGTC ACCAGTGTAACCATCAAATCGGAGATCCTGCCAGCTTCACTTCAGTCCGCCACTGCCAGA CCCACTTCCAGGCTAAATAGATTACCTGAGCTGGAATTGGAAGCAATTGATAACCAATTT GGACAACCAGGAACAGGCGATCAGATTCCATGGACAAATAATACAGTGACAGCTATAAAT CAGAGTAAATCAGAAGACCAGTGTATTAGCTCACAATTAGATGAGCTTCTCTGTCCACCC ACAACAGTAGAAGGGAGAAATGATGAGAAGGCTCTTCTTGAACAGCTGGTATCCTTCCTT AGTGGCAAAGATGAAACTGAGCTAGCTGAACTAGACAGAGCTCTGGGAATTGACAAACTT GTTCAGGGGGGTGGATTAGATGTATTATCAGAGAGATTTCCACCACAACAAGCAACGCCA CCTTTGATCATGGAAGAAAGACCCAACCTTTATTCCCAGCCTTACTCTTCTCCTTCTCCT ACTGCCAATCTCCCTAGCCCTTTCCAAGGCATGGTCAGGCAAAAACCTTCACTGGGGACG ATGCCTGTTCAAGTAACACCTCCCCGAGGTGCTTTTTCACCTGGCATGGGCATGCAGCCC AGGCAAACTCTAAACAGACCTCCGGCTGCACCTAACCAGCTTCGACTTCAACTACAGCAG CGATTACAGGGACAACAGCAGTTGATACACCAAAATCGGCAAGCTATCTTAAACCAGTTT GCAGCAACTGCTCCTGTTGGCATCAATATGAGATCAGGCATGCAACAGCAAATTACACCT CAGCCACCCCTGAATGCTCAAATGTTGGCACAACGTCAGCGGGAACTGTACAGTCAACAG CACCGACAGAGGCAGCTAATACAGCAGCAAAGAGCCATGCTTATGAGGCAGCAAAGCTTT GGGAACAACCTCCCTCCCTCATCTGGACTACCAGTTCAAATGGGGAACCCCCGTCTTCCT CAGGGTGCTCCACAGCAATTCCCCTATCCACCAAACTATGGTACAAATCCAGGAACCCCA CCTGCTTCTACCAGCCCGTTTTCACAACTAGCAGCAAATCCTGAAGCATCCTTGGCCAAC CGCAACAGCATGGTGAGCAGAGGCATGACAGGAAACATAGGAGGACAGTTTGGCACTGGA ATCAATCCTCAGATGCAGCAGAATGTCTTCCAGTATCCAGGAGCAGGAATGGTTCCCCAA GGTGAGGCCAACTTTGCTCCATCTCTAAGCCCTGGGAGCTCCATGGTGCCGATGCCAATC CCTCCTCCTCAGAGTTCTCTGCTCCAGCAAACTCCACCTGCCTCCGGGTATCAGTCACCA GACATGAAGGCCTGGCAGCAAGGAGCGATAGGAAACAACAATGTGTTCAGTCAAGCTGTC CAGAACCAGCCCACGCCTGCACAGCCAGGAGTATACAACAACATGAGCATCACCGTTTCC ATGGCAGGTGGAAATACGAATGTTCAGAACATGAACCCAATGATGGCCCAGATGCAGATG AGCTCTTTGCAGATGCCAGGAATGAACACTGTGTGCCCTGAGCAGATAAATGATCCCGCA CTGAGACACACAGGCCTCTACTGCAACCAGCTCTCATCCACTGACCTTCTCAAAACAGAA GCAGATGGAACCCAGGTGCAACAGGTTCAGGTGTTTGCTGACGTCCAGTGTACAGTGAAT CTGGTAGGCGGGGACCCTTACCTGAACCAGCCTGGTCCACTGGGAACTCAAAAGCCCACG TCAGGACCACAGACCCCCCAGGCCCAGCAGAAGAGCCTCCTTCAGCAGCTACTGACTGAA TAA PF00989 PAS PF00010 HLH PF07469 DUF1518 PF08815 Nuc_rec_co-act PF08832 SRC-1 component organelle component membrane-bound organelle component intracellular membrane-bound organelle component nucleus function signal transducer activity function transcription factor binding function transcription regulator activity function transcription cofactor activity function transcription coactivator activity function binding function protein binding process cellular process process cell communication process signal transduction process regulation of biological process process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription BE0000779 Vitamin D3 receptor Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Vitamin D3 receptor Involved in transcription factor activity Nuclear hormone receptor. VDR mediates the action of vitamin D3 by controlling the expression of hormone sensitive genes VDR 12q13.11 Nucleus None 6.5 48290.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:12679 GenAtlas VDR GeneCards VDR GenBank Gene Database J03258 GenBank Protein Database 340203 IUPHAR 605 Guide to Pharmacology 90 UniProtKB P11473 UniProt Accession VDR_HUMAN 1,25-dihydroxyvitamin D3 receptor VDR >Vitamin D3 receptor MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTC PFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSL RPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSG DSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQK VIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDV TKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAALIEAIQDRLS NTLQTYIRCRHPPPGSHLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPECSMKLTPLVLE VFGNEIS >1284 bp ATGGAGGCAATGGCGGCCAGCACTTCCCTGCCTGACCCTGGAGACTTTGACCGGAACGTG CCCCGGATCTGTGGGGTGTGTGGAGACCGAGCCACTGGCTTTCACTTCAATGCTATGACC TGTGAAGGCTGCAAAGGCTTCTTCAGGCGAAGCATGAAGCGGAAGGCACTATTCACCTGC CCCTTCAACGGGGACTGCCGCATCACCAAGGACAACCGACGCCACTGCCAGGCCTGCCGG CTCAAACGCTGTGTGGACATCGGCATGATGAAGGAGTTCATTCTGACAGATGAGGAAGTG CAGAGGAAGCGGGAGATGATCCTGAAGCGGAAGGAGGAGGAGGCCTTGAAGGACAGTCTG CGGCCCAAGCTGTCTGAGGAGCAGCAGCGCATCATTGCCATACTGCTGGACGCCCACCAT AAGACCTACGACCCCACCTACTCCGACTTCTGCCAGTTCCGGCCTCCAGTTCGTGTGAAT GATGGTGGAGGGAGCCATCCTTCCAGGCCCAACTCCAGACACACTCCCAGCTTCTCTGGG GACTCCTCCTCCTCCTGCTCAGATCACTGTATCACCTCTTCAGACATGATGGACTCGTCC AGCTTCTCCAATCTGGATCTGAGTGAAGAAGATTCAGATGACCCTTCTGTGACCCTAGAG CTGTCCCAGCTCTCCATGCTGCCCCACCTGGCTGACCTGGTCAGTTACAGCATCCAAAAG GTCATTGGCTTTGCTAAGATGATACCAGGATTCAGAGACCTCACCTCTGAGGACCAGATC GTACTGCTGAAGTCAAGTGCCATTGAGGTCATCATGTTGCGCTCCAATGAGTCCTTCACC ATGGACGACATGTCCTGGACCTGTGGCAACCAAGACTACAAGTACCGCGTCAGTGACGTG ACCAAAGCCGGACACAGCCTGGAGCTGATTGAGCCCCTCATCAAGTTCCAGGTGGGACTG AAGAAGCTGAACTTGCATGAGGAGGAGCATGTCCTGCTCATGGCCATCTGCATCGTCTCC CCAGATCGTCCTGGGGTGCAGGACGCCGCGCTGATTGAGGCCATCCAGGACCGCCTGTCC AACACACTGCAGACGTACATCCGCTGCCGCCACCCGCCCCCGGGCAGCCACCTGCTCTAT GCCAAGATGATCCAGAAGCTAGCCGACCTGCGCAGCCTCAATGAGGAGCACTCCAAGCAG TACCGCTGCCTCTCCTTCCAGCCTGAGTGCAGCATGAAGCTAACGCCCCTTGTGCTCGAA GTGTTTGGCAATGAGATCTCCTGA PF00104 Hormone_recep PF00105 zf-C4 component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function transcription factor activity function ligand-dependent nuclear receptor activity function DNA binding function binding function signal transducer activity function receptor activity function nucleic acid binding function steroid hormone receptor activity process regulation of biological process process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent "
drug:(1R,3R)-5-[(2E)-3-{(1S,3R)-2,2,3-trimethyl-3-[6,6,6-trifluoro-5-hydroxy-5-(trifluoromethyl)hex-3-yn-1-yl]cyclopentyl}prop-2-en-1-ylidene]cyclohexane-1,3-diolrdfs:label"(1R,3R)-5-[(2E)-3-{(1S,3R)-2,2,3-trimethyl-3-[6,6,6-trifluoro-5-hydroxy-5-(trifluoromethyl)hex-3-yn-1-yl]cyclopentyl}prop-2-en-1-ylidene]cyclohexane-1,3-diol"
drug:(1R,3R)-5-[(2E)-3-{(1S,3R)-2,2,3-trimethyl-3-[6,6,6-trifluoro-5-hydroxy-5-(trifluoromethyl)hex-3-yn-1-yl]cyclopentyl}prop-2-en-1-ylidene]cyclohexane-1,3-diolrdf:typedrugbank:drugs
drug:(1R,3S,5S,8R)-8-HYDROXY-2-OXABICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACIDdrugbank:description" experimental This compound belongs to the pyran carboxylic acids. These are compounds containing a pyran ring which bears a carboxylic acid group. Pyran Carboxylic Acids Organic Compounds Heterocyclic Compounds Pyrans Pyran Carboxylic Acids and Derivatives Oxanes Dicarboxylic Acids and Derivatives Secondary Alcohols Polyols Enolates Ethers Polyamines Carboxylic Acids dicarboxylic acid derivative oxane secondary alcohol polyol enolate carboxylic acid ether carboxylic acid derivative polyamine alcohol logP -0.14 ALOGPS logS -0.47 ALOGPS Water Solubility 7.81e+01 g/l ALOGPS logP -0.36 ChemAxon IUPAC Name (1R,3S,5S,8R)-8-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid ChemAxon Traditional IUPAC Name (1R,3S,5S,8R)-8-hydroxy-2-oxabicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid ChemAxon Molecular Weight 228.1987 ChemAxon Monoisotopic Weight 228.063388116 ChemAxon SMILES [H][C@@]1(O)C=C[C@]2(C[C@]([H])(O[C@]1([H])C2)C(O)=O)C(O)=O ChemAxon Molecular Formula C10H12O6 ChemAxon InChI InChI=1S/C10H12O6/c11-5-1-2-10(9(14)15)3-6(5)16-7(4-10)8(12)13/h1-2,5-7,11H,3-4H2,(H,12,13)(H,14,15)/t5-,6-,7+,10+/m1/s1 ChemAxon InChIKey InChIKey=KRZHNRULRHECRF-JQCUSGDOSA-N ChemAxon Polar Surface Area (PSA) 104.06 ChemAxon Refractivity 51.19 ChemAxon Polarizability 20.32 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 3.31 ChemAxon pKa (strongest basic) -3.3 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 445314 PubChem Substance 99445121 ChemSpider 392988 PDB TSO BE0004364 Intracellular chorismate mutase Mycobacterium tuberculosis # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Intracellular chorismate mutase Amino acid transport and metabolism Rv0948c None 6.97 11770.5 Mycobacterium tuberculosis GenBank Gene Database BX842575 GenBank Protein Database 2078076 UniProtKB P64767 UniProt Accession CHMU_MYCTU >Uncharacterized protein Rv0948c/MT0975 MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKA RMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH >1113 bp TTGAAACTCAACCGATTTGGTGCCGCCGTAGGTGTCCTGGCTGCGGGTGCGCTGGTGTTG TCCGCGTGTGGTAACGACGACAATGTGACCGGGGGAGGTGCAACCACTGGCCAGGCGTCG GCGAAGGTCGATTGCGGGGGGAAGAAGACACTCAAAGCCAGTGGGTCGACGGCGCAGGCC AACGCGATGACCCGCTTTGTCAACGTGTTCGAGCAGGCCTGCCCCGGCCAAACCCTGAAC TACACGGCCAATGGTTCGGGCGCTGGAATCAGCGAATTTAATGGCAACCAAACCGATTTC GGTGGCTCAGATGTACCCCTGAGCAAGGACGAGGCCGCAGCGGCGCAGCGGCGTTGCGGC TCGCCGGCGTGGAATCTGCCGGTGGTGTTCGGCCCGATCGCGGTTACCTACAACCTCAAC AGCGTTTCCTCGCTAAATTTGGACGGCCCCACGTTGGCGAAGATCTTCAACGGCTCCATT ACGCAGTGGAACAATCCCGCGATCCAGGCGCTGAACCGCGACTTCACGCTGCCAGGTGAG CGGATTCACGTGGTGTTCCGCAGCGATGAGTCGGGGACCACGGACAACTTCCAGAGGTAC CTGCAGGCCGCGTCCAACGGTGCGTGGGGTAAGGGCGCTGGAAAGTCGTTCCAAGGCGGC GTCGGTGAGGGCGCGCGGGGTAACGATGGCACGTCAGCGGCCGCGAAGAACACCCCGGGG TCGATCACCTACAACGAGTGGTCGTTCGCCCAGGCGCAGCACCTGACCATGGCCAACATC GTCACTTCGGCTGGTGGGGACCCGGTGGCGATTACTATCGACTCGGTCGGCCAGACGATC GCCGGGGCCACCATCTCCGGGGTGGGCAACGACCTGGTGCTCGACACGGACTCGTTCTAC CGGCCGAAGCGTCCCGGCTCCTATCCGATCGTGTTAGCGACATACGAAATCGTTTGCTCG AAGTATCCCGACTCGCAGGTTGGCACGGCTGTGAAGGCGTTCCTGCAGAGCACTATCGGC GCCGGTCAAAGCGGCCTGGGGGACAACGGATACATCCCAATTCCGGACGAGTTCAAATCG AGGCTGTCGACTGCGGTCAACGCGATCGCCTGA PF01817 CM_2 function intramolecular transferase activity function chorismate mutase activity function catalytic activity function isomerase activity process aromatic amino acid family biosynthesis process physiological process process metabolism process cellular metabolism process amino acid metabolism process amino acid and derivative metabolism process amino acid biosynthesis BE0004365 Phospho-2-dehydro-3-deoxyheptonate aldolase AroG Mycobacterium tuberculosis # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Phospho-2-dehydro-3-deoxyheptonate aldolase AroG aroG Mycobacterium tuberculosis UniProtKB O53512 UniProt Accession AROG_MYCTU "
drug:(1R,3S,5S,8R)-8-HYDROXY-2-OXABICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACIDrdfs:label"(1R,3S,5S,8R)-8-HYDROXY-2-OXABICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID"
drug:(1R,3S,5S,8R)-8-HYDROXY-2-OXABICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACIDrdf:typedrugbank:drugs
drug:(1R,4S,7AS)-1-(1-FORMYLPROP-1-EN-1-YL)-4-METHOXY-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACIDdrugbank:description" experimental This compound belongs to the isoindoles. These are heteropolycyclic compounds whose structure contain isoindole, a benzo-fused pyrrole. Isoindoles Organic Compounds Heterocyclic Compounds Isoindoles and Derivatives Isoindoles Pyrroline Carboxylic Acids Enals Enolates Ethers Enamines Polyamines Carboxylic Acids pyrroline carboxylic acid pyrroline carboxylic acid or derivative pyrroline alpha,beta-unsaturated aldehyde enal carboxylic acid derivative enolate polyamine ether enamine carboxylic acid organonitrogen compound aldehyde logP 1.65 ALOGPS logS -2.3 ALOGPS Water Solubility 1.34e+00 g/l ALOGPS logP 0.62 ChemAxon IUPAC Name (1R,4S,7aS)-4-methoxy-1-[(2E)-1-oxobut-2-en-2-yl]-2,4,5,6,7,7a-hexahydro-1H-isoindole-3-carboxylic acid ChemAxon Traditional IUPAC Name (3R,3aS,7S)-7-methoxy-3-[(2E)-1-oxobut-2-en-2-yl]-3,3a,4,5,6,7-hexahydro-2H-isoindole-1-carboxylic acid ChemAxon Molecular Weight 265.305 ChemAxon Monoisotopic Weight 265.131408101 ChemAxon SMILES [H][C@]1(NC(C(O)=O)=C2[C@]1([H])CCC[C@]2([H])OC)C(=C/C)\C=O ChemAxon Molecular Formula C14H19NO4 ChemAxon InChI InChI=1S/C14H19NO4/c1-3-8(7-16)12-9-5-4-6-10(19-2)11(9)13(15-12)14(17)18/h3,7,9-10,12,15H,4-6H2,1-2H3,(H,17,18)/b8-3-/t9-,10-,12-/m0/s1 ChemAxon InChIKey InChIKey=ZYKSDPVHVMSKIL-IIHMJNQGSA-N ChemAxon Polar Surface Area (PSA) 75.63 ChemAxon Refractivity 71.63 ChemAxon Polarizability 27.69 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 4.27 ChemAxon pKa (strongest basic) 0.9 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937125 PubChem Substance 99444581 PDB LK7 BE0001430 Beta-lactamase Enterobacter cloacae # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-lactamase Defense mechanisms and antibiotic degradation This protein is a serine beta-lactamase with a substrate specificity for cephalosporins ampC Periplasm None 8.67 41302.0 Enterobacter cloacae GenBank Gene Database X07274 GenBank Protein Database 42261 UniProtKB P05364 UniProt Accession AMPC_ENTCL Beta-lactamase precursor Cephalosporinase EC 3.5.2.6 >Beta-lactamase precursor MMRKSLCCALLLGISCSALATPVSEKQLAEVVANTITPLMKAQSVPGMAVAVIYQGKPHY YTFGKADIAANKPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDAVTRYWPQLTGKQ WQGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYANASIGLFGA LAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAWGYRDGKAVRVSPGMLDAQA YGVKTNVQDMANWVMANMAPENVADASLKQGIALAQSRYWRIGSMYQGLGWEMLNWPVEA NTVVEGSDSKVALAPLPVAEVNPPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLA NTSYPNPARVEAAYHILEALQ >1146 bp ATGATGAGAAAATCCCTTTGCTGCGCCCTGCTGCTCGGCATCTCTTGCTCTGCTCTCGCC ACGCCAGTGTCAGAAAAACAGCTGGCGGAGGTGGTCGCGAATACGATTACCCCGCTGATG AAAGCCCAGTCTGTTCCAGGCATGGCGGTGGCCGTTATTTATCAGGGAAAACCGCACTAT TACACATTTGGCAAGGCCGATATCGCGGCGAATAAACCCGTTACGCCTCAGACCCTGTTC GAGCTGGGTTCTATAAGTAAAACCTTCACCGGCGTTTTAGGTGGGGATGCCATTGCTCGC GGTGAAATTTCGCTGGACGATGCGGTGACCAGATACTGGCCACAGCTGACGGGCAAGCAG TGGCAGGGTATTCGTATGCTGGATCTCGCCACCTACACCGCTGGCGGCCTGCCGCTACAG GTACCGGATGAGGTCACGGATAACGCCTCCCTGCTGCGCTTTTATCAAAACTGGCAGCCG CAGTGGAAGCCTGGCACAACGCGTCTTTACGCCAACGCCAGCATCGGTCTTTTTGGTGCG CTGGCGGTCAAACCTTCTGGCATGCCCTATGAGCAGGCCATGACGACGCGGGTCCTTAAG CCGCTCAAGCTGGACCATACCTGGATTAACGTGCCGAAAGCGGAAGAGGCGCATTACGCC TGGGGCTATCGTGACGGTAAAGCGGTGCGCGTTTCGCCGGGTATGCTGGATGCACAAGCC TATGGCGTGAAAACCAACGTGCAGGATATGGCGAACTGGGTCATGGCAAACATGGCGCCG GAGAACGTTGCTGATGCCTCACTTAAGCAGGGCATCGCGCTGGCGCAGTCGCGCTACTGG CGTATCGGGTCAATGTATCAGGGTCTGGGCTGGGAGATGCTCAACTGGCCCGTGGAGGCC AACACGGTGGTCGAGGGCAGCGACAGTAAGGTAGCACTGGCGCCGTTGCCCGTGGCAGAA GTGAATCCACCGGCTCCCCCGGTCAAAGCGTCCTGGGTCCATAAAACGGGCTCTACTGGC GGGTTTGGCAGCTACGTGGCCTTTATTCCTGAAAAGCAGATCGGTATTGTGATGCTCGCG AATACAAGCTATCCGAACCCGGCACGCGTTGAGGCGGCATACCATATCCTCGAGGCGCTA CAGTAA PF00144 Beta-lactamase component cell component periplasmic space component periplasmic space (sensu Gram-negative Bacteria) function beta-lactamase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function catalytic activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides process metabolism process cellular metabolism process drug metabolism process antibiotic metabolism process antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process physiological process process response to antibiotic "
drug:(1R,4S,7AS)-1-(1-FORMYLPROP-1-EN-1-YL)-4-METHOXY-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACIDrdfs:label"(1R,4S,7AS)-1-(1-FORMYLPROP-1-EN-1-YL)-4-METHOXY-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACID"
drug:(1R,4S,7AS)-1-(1-FORMYLPROP-1-EN-1-YL)-4-METHOXY-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACIDrdf:typedrugbank:drugs
drug:(1S)-1,2,3,4-TETRAHYDRO-BENZO[C]PHENANTHRENE-2,3,4-TRIOLdrugbank:description" experimental This compound belongs to the phenanthrenes and derivatives. These are polycyclic compounds containing a phenanthrene moiety, which is a tricyclic aromatic compound with three non-linearly fused benzene. Phenanthrenes and Derivatives Organic Compounds Benzenoids Phenanthrenes and Derivatives Tetralins Naphthalenes Benzene and Substituted Derivatives Secondary Alcohols 1,2-Diols Polyamines naphthalene tetralin benzene polyol 1,2-diol secondary alcohol polyamine alcohol logP 1.95 ALOGPS logS -3.6 ALOGPS Water Solubility 6.74e-02 g/l ALOGPS logP 2.02 ChemAxon IUPAC Name (4R,5R,6R)-tetracyclo[8.8.0.0^{2,7}.0^{13,18}]octadeca-1,7,9,11,13,15,17-heptaene-4,5,6-triol ChemAxon Traditional IUPAC Name (4R,5R,6R)-tetracyclo[8.8.0.0^{2,7}.0^{13,18}]octadeca-1,7,9,11,13,15,17-heptaene-4,5,6-triol ChemAxon Molecular Weight 280.3178 ChemAxon Monoisotopic Weight 280.109944378 ChemAxon SMILES [H][C@@]1(O)CC2=C(C=CC3=C2C2=C(C=CC=C2)C=C3)[C@@]([H])(O)[C@]1([H])O ChemAxon Molecular Formula C18H16O3 ChemAxon InChI InChI=1S/C18H16O3/c19-15-9-14-13(17(20)18(15)21)8-7-11-6-5-10-3-1-2-4-12(10)16(11)14/h1-8,15,17-21H,9H2/t15-,17-,18-/m1/s1 ChemAxon InChIKey InChIKey=WCUHTHVUZQCBTI-KBAYOESNSA-N ChemAxon Polar Surface Area (PSA) 60.69 ChemAxon Refractivity 80.68 ChemAxon Polarizability 30.35 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 12.88 ChemAxon pKa (strongest basic) -3.3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5287834 PubChem Substance 99443950 ChemSpider 4450129 PDB BPI BE0000113 DNA polymerase beta Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown DNA polymerase beta Replication, recombination and repair Repair polymerase. Conducts "gap-filling" DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. Has a 5'-deoxyribose-5- phosphate lyase (dRP lyase) activity POLB 8p11.2 Nucleus None 9.41 38047.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9174 GenAtlas POLB GeneCards POLB GenBank Gene Database L11607 GenBank Protein Database 292397 UniProtKB P06746 UniProt Accession DPOLB_HUMAN EC 2.7.7.7 EC 4.2.99.- >DNA polymerase beta SKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKK LPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKT LEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSF RRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQL PSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPL GVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE >1008 bp ATGAGCAAACGGAAGGCGCCGCAGGAGACTCTCAACGGGGGAATCACCGACATGCTCACA GAACTCGCAAACTTTGAGAAGAACGTGAGCCAAGCTATCCACAAGTACAATGCTTACAGA AAAGCAGCATCTGTTATAGCAAAATACCCACACAAAATAAAGAGTGGAGCTGAAGCTAAG AAATTGCCTGGAGTAGGAACAAAAATTGCTGAAAAGATTGATGAGTTTTTAGCAACTGGA AAATTACGTAAACTGGAAAAGATTCGGCAGGATGATACGAGTTCATCCATCAATTTCCTG ACTCGAGTTAGTGGCATTGGTCCATCTGCTGCAAGGAAGTTTGTAGATGAAGGAATTAAA ACACTAGAAGATCTCAGAAAAAATGAAGATAAATTGAACCATCATCAGCGAATTGGGCTG AAATATTTTGGGGACTTTGAAAAAAGAATTCCTCGTGAAGAGATGTTACAAATGCAAGAT ATTGTACTAAATGAAGTTAAAAAAGTGGATTCTGAATACATTGCTACAGTCTGTGGCAGT TTCAGAAGAGGTGCAGAGTCCAGTGGTGACATGGATGTTCTCCTGACCCATCCCAGCTTC ACTTCAGAATCAACCAAACAGCCAAAACTGTTACATCAGGTTGTGGAGCAGTTACAAAAG GTTCATTTTATCACAGATACCCTGTCAAAGGGTGAGACAAAGTTCATGGGTGTTTGCCAG CTTCCCAGTAAAAATGATGAAAAAGAATATCCACACAGAAGAATTGATATCAGGTTGATA CCCAAAGATCAGTATTACTGTGGTGTTCTCTATTTCACTGGGAGTGATATTTTCAATAAG AATATGAGGGCTCATGCCCTAGAAAAGGGTTTCACAATCAATGAGTACACCATCCGTCCC TTGGGAGTCACTGGAGTTGCAGGAGAACCCCTGCCAGTGGATAGTGAAAAAGACATCTTT GATTACATCCAGTGGAAATACCGGGAACCCAAGGACCGGAGCGAATGA component cell component intracellular function DNA-directed DNA polymerase activity function transferase activity, transferring phosphorus-containing groups function nucleic acid binding function binding function DNA binding function catalytic activity function beta DNA polymerase activity function nucleotidyltransferase activity function transferase activity process DNA repair process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process physiological process process DNA replication process DNA metabolism process metabolism process cellular metabolism "
drug:(1S)-1,2,3,4-TETRAHYDRO-BENZO[C]PHENANTHRENE-2,3,4-TRIOLrdfs:label"(1S)-1,2,3,4-TETRAHYDRO-BENZO[C]PHENANTHRENE-2,3,4-TRIOL"
drug:(1S)-1,2,3,4-TETRAHYDRO-BENZO[C]PHENANTHRENE-2,3,4-TRIOLrdf:typedrugbank:drugs
drug:(1S)-1-(1H-INDOL-3-YLMETHYL)-2-(2-PYRIDIN-4-YL-[1,7]NAPHTYRIDIN-5-YLOXY)-EHYLAMINEdrugbank:description" experimental This compound belongs to the tryptamines and derivatives. These are compounds containing the tryptamine backbone, which is structurally characterized by an indole ring subsituted at the thrid position by an ethanamine. Tryptamines and Derivatives Organic Compounds Heterocyclic Compounds Indoles and Derivatives Tryptamines and Derivatives Bipyridines and Oligopyridines Naphthyridines Indoles Alkyl Aryl Ethers Substituted Pyrroles Benzene and Substituted Derivatives Polyamines Monoalkylamines naphthyridine indole alkyl aryl ether pyridine benzene substituted pyrrole pyrrole ether polyamine primary amine primary aliphatic amine amine organonitrogen compound logP 3.08 ALOGPS logS -5.1 ALOGPS Water Solubility 2.97e-03 g/l ALOGPS logP 2.95 ChemAxon IUPAC Name 5-[(2S)-2-amino-3-(1H-indol-3-yl)propoxy]-2-(pyridin-4-yl)-1,7-naphthyridine ChemAxon Traditional IUPAC Name 5-[(2S)-2-amino-3-(1H-indol-3-yl)propoxy]-2-(pyridin-4-yl)-1,7-naphthyridine ChemAxon Molecular Weight 395.4564 ChemAxon Monoisotopic Weight 395.174610319 ChemAxon SMILES [H][C@@](N)(COC1=C2C=CC(=NC2=CN=C1)C1=CC=NC=C1)CC1=CNC2=C1C=CC=C2 ChemAxon Molecular Formula C24H21N5O ChemAxon InChI InChI=1S/C24H21N5O/c25-18(11-17-12-28-22-4-2-1-3-19(17)22)15-30-24-14-27-13-23-20(24)5-6-21(29-23)16-7-9-26-10-8-16/h1-10,12-14,18,28H,11,15,25H2/t18-/m0/s1 ChemAxon InChIKey InChIKey=DQIXTEDFNFZMCM-SFHVURJKSA-N ChemAxon Polar Surface Area (PSA) 89.71 ChemAxon Refractivity 114.97 ChemAxon Polarizability 43.41 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 17.11 ChemAxon pKa (strongest basic) 9.24 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 5 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 6914614 PubChem Substance 99443675 ChemSpider 5290494 PDB 6EA BE0003762 cAMP-dependent protein kinase inhibitor alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown cAMP-dependent protein kinase inhibitor alpha Involved in cAMP-dependent protein kinase inhibitor act Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains PKIA 8q21.12 None 4.18 7988.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9017 GeneCards PKIA GenBank Gene Database S76965 GenBank Protein Database 243494 UniProtKB P61925 UniProt Accession IPKA_HUMAN cAMP-dependent protein kinase inhibitor, muscle/brain isoform PKI-alpha >cAMP-dependent protein kinase inhibitor alpha MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSS TEQSGEAQGEAAKSES >231 bp ATGACTGATGTGGAAACTACATATGCAGATTTTATTGCTTCAGGAAGAACAGGTAGAAGA AATGCAATACATGATATCCTGGTTTCCTCTGCAAGTGGCAACAGCAATGAATTAGCCTTG AAATTAGCAGGTCTTGATATCAACAAGACAGAAGGTGAAGAAGATGCACAACGAAGTTCT ACAGAACAAAGTGGGGAAGCCCAGGGAGAAGCAGCAAAATCTGAAAGCTAA PF02827 PKI function enzyme inhibitor activity function kinase inhibitor activity function protein kinase inhibitor activity function cAMP-dependent protein kinase inhibitor activity function enzyme regulator activity process regulation of enzyme activity process regulation of transferase activity process regulation of kinase activity process regulation of protein kinase activity process negative regulation of protein kinase activity process regulation of biological process BE0003761 cAMP-dependent protein kinase catalytic subunit alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown cAMP-dependent protein kinase catalytic subunit alpha Involved in ATP binding Phosphorylates a large number of substrates in the cytoplasm and the nucleus PRKACA 19p13.1 Cytoplasm (By similarity). Nucleus (By similarity) None 9.22 40589.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9380 GeneCards PRKACA GenBank Gene Database X07767 GenBank Protein Database 35479 UniProtKB P17612 UniProt Accession KAPCA_HUMAN PKA C-alpha >cAMP-dependent protein kinase catalytic subunit alpha MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVML VKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF >1056 bp ATGGGCAACGCCGCCGCCGCCAAGAAGGGCAGCGAGCAGGAGAGCGTGAAAGAATTCTTA GCCAAAGCCAAAGAAGATTTTCTTAAAAAATGGGAAAGTCCCGCTCAGAACACAGCCCAC TTGGATCAGTTTGAACGAATCAAGACCCTCGGCACGGGCTCCTTCGGGCGGGTGATGCTG GTGAAACACAAGGAGACCGGGAACCACTATGCCATGAAGATCCTCGACAAACAGAAGGTG GTGAAACTGAAACAGATCGAACACACCCTGAATGAAAAGCGCATCCTGCAAGCTGTCAAC TTTCCGTTCCTCGTCAAACTCGAGTTCTCCTTCAAGGACAACTCAAACTTATACATGGTC ATGGAGTACGTGCCCGGCGGGGAGATGTTCTCACACCTACGGCGGATCGGAAGGTTCAGT GAGCCCCATGCCCGTTTCTACGCGGCCCAGATCGTCCTGACCTTTGAGTATCTGCACTCG CTGGATCTCATCTACAGGGACCTGAAGCCGGAGAATCTGCTCATTGACCAGCAGGGCTAC ATTCAGGTGACAGACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGC GGCACCCCTGAGTACCTGGCCCCTGAGATTATCCTGAGCAAAGGCTACAACAAGGCCGTG GACTGGTGGGCCCTGGGGGTTCTTATCTATGAAATGGCCGCTGGCTACCCGCCCTTCTTC GCAGACCAGCCCATCCAGATCTATGAGAAGATCGTCTCTGGGAAGGTGCGCTTCCCTTCC CACTTCAGCTCTGACTTGAAGGACCTGCTGCGGAACCTCCTGCAGGTAGATCTCACCAAG CGCTTTGGGAACCTCAAGAATGGGGTCAACGATATCAAGAACCACAAGTGGTTTGCCACA ACTGACTGGATTGCCATCTACCAGAGGAAGGTGGAAGCTCCCTTCATACCAAAGTTTAAA GGCCCTGGGGATACGAGTAACTTTGACGACTATGAGGAAGAAGAAATCCGGGTCTCCATC AATGAGAAGTGTGGCAAGGAGTTTTCTGAGTTTTAG PF00069 Pkinase function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process "
drug:(1S)-1-(1H-INDOL-3-YLMETHYL)-2-(2-PYRIDIN-4-YL-[1,7]NAPHTYRIDIN-5-YLOXY)-EHYLAMINErdfs:label"(1S)-1-(1H-INDOL-3-YLMETHYL)-2-(2-PYRIDIN-4-YL-[1,7]NAPHTYRIDIN-5-YLOXY)-EHYLAMINE"
drug:(1S)-1-(1H-INDOL-3-YLMETHYL)-2-(2-PYRIDIN-4-YL-[1,7]NAPHTYRIDIN-5-YLOXY)-EHYLAMINErdf:typedrugbank:drugs
drug:(1S)-1-(3-chlorophenyl)-2-oxo-2-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]ethyl acetatedrugbank:description" experimental This compound belongs to the isoquinolones and derivatives. These are aromatic polycyclic compounds containing a ketone bearing isoquinoline moiety. Isoquinolones and Derivatives Organic Compounds Heterocyclic Compounds Isoquinolines and Derivatives Isoquinolones and Derivatives Anilides Benzyloxycarbonyls Benzylethers Chlorobenzenes Aryl Chlorides N-unsubstituted Carboxylic Acid Imides Secondary Carboxylic Acid Amides Ketones Carboxylic Acid Esters Enolates Carboxylic Acids Polyamines Dialkyl Ethers Organochlorides benzylether chlorobenzene aryl halide benzene aryl chloride carboxylic acid imide, n-unsubstituted carboxylic acid imide carboxamide group ketone secondary carboxylic acid amide carboxylic acid ester dialkyl ether ether polyamine carboxylic acid derivative carboxylic acid enolate amine organohalogen carbonyl group organonitrogen compound organochloride logP 2.5 ALOGPS logS -5.1 ALOGPS Water Solubility 3.30e-03 g/l ALOGPS logP 2.61 ChemAxon IUPAC Name (S)-(3-chlorophenyl)[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)carbamoyl]methyl acetate ChemAxon Traditional IUPAC Name (S)-(3-chlorophenyl)[(1,3,4-trioxo-2H-isoquinolin-5-yl)carbamoyl]methyl acetate ChemAxon Molecular Weight 400.769 ChemAxon Monoisotopic Weight 400.046213865 ChemAxon SMILES [H][C@@](OC(C)=O)(C(=O)NC1=CC=CC2=C1C(=O)C(=O)NC2=O)C1=CC=CC(Cl)=C1 ChemAxon Molecular Formula C19H13ClN2O6 ChemAxon InChI InChI=1S/C19H13ClN2O6/c1-9(23)28-16(10-4-2-5-11(20)8-10)19(27)21-13-7-3-6-12-14(13)15(24)18(26)22-17(12)25/h2-8,16H,1H3,(H,21,27)(H,22,25,26)/t16-/m0/s1 ChemAxon InChIKey InChIKey=OVSAMUIBGQSLDC-INIZCTEOSA-N ChemAxon Polar Surface Area (PSA) 118.64 ChemAxon Refractivity 99.14 ChemAxon Polarizability 37.08 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 5.51 ChemAxon pKa (strongest basic) -7 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937155 PubChem Substance 99444969 PDB RXC BE0001162 Caspase-3 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Caspase-3 Involved in caspase activity Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin CASP3 4q34 Cytoplasm None 6.51 31608.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1504 GenAtlas CASP3 GeneCards CASP3 GenBank Gene Database U13737 GenBank Protein Database 561666 UniProtKB P42574 UniProt Accession CASP3_HUMAN Apopain CASP-3 Caspase-3 precursor CPP-32 Cysteine protease CPP32 EC 3.4.22.56 SCA-1 SREBP cleavage activity 1 Yama protein >Caspase-3 precursor MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTG MTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLS HGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDD DMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVN RKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH >834 bp ATGGAGAACACTGAAAACTCAGTGGATTCAAAATCCATTAAAAATTTGGAACCAAAGATC ATACATGGAAGCGAATCAATGGACTCTGGAATATCCCTGGACAACAGTTATAAAATGGAT TATCCTGAGATGGGTTTATGTATAATAATTAATAATAAGAATTTTCATAAAAGCACTGGA ATGACATCTCGGTCTGGTACAGATGTCGATGCAGCAAACCTCAGGGAAACATTCAGAAAC TTGAAATATGAAGTCAGGAATAAAAATGATCTTACACGTGAAGAAATTGTGGAATTGATG CGTGATGTTTCTAAAGAAGATCACAGCAAAAGGAGCAGTTTTGTTTGTGTGCTTCTGAGC CATGGTGAAGAAGGAATAATTTTTGGAACAAATGGACCTGTTGACCTGAAAAAAATAACA AACTTTTTCAGAGGGGATCGTTGTAGAAGTCTAACTGGAAAACCCAAACTTTTCATTATT CAGGCCTGCCGTGGTACAGAACTGGACTGTGGCATTGAGACAGACAGTGGTGTTGATGAT GACATGGCGTGTCATAAAATACCAGTGGATGCCGACTTCTTGTATGCATACTCCACAGCA CCTGGTTATTATTCTTGGCGAAATTCAAAGGATGGCTCCTGGTTCATCCAGTCGCTTTGT GCCATGCTGAAACAGTATGCCGACAAGCTTGAATTTATGCACATTCTTACCCGGGTTAAC CGAAAGGTGGCAACAGAATTTGAGTCCTTTTCCTTTGACGCTACTTTTCATGCAAAGAAA CAGATTCCATGTATTGTTTCCATGCTCACAAAAGAACTCTATTTTTATCACTAA PF00656 Peptidase_C14 function peptidase activity function endopeptidase activity function cysteine-type endopeptidase activity function caspase activity function catalytic activity function hydrolase activity process protein metabolism process cellular protein metabolism process proteolysis process physiological process process metabolism process macromolecule metabolism "
drug:(1S)-1-(3-chlorophenyl)-2-oxo-2-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]ethyl acetaterdfs:label"(1S)-1-(3-chlorophenyl)-2-oxo-2-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]ethyl acetate"
drug:(1S)-1-(3-chlorophenyl)-2-oxo-2-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]ethyl acetaterdf:typedrugbank:drugs
drug:(1S)-1-(PHENOXYMETHYL)PROPYL METHYLPHOSPHONOCHLORIDOATEdrugbank:description" experimental This compound belongs to the phenol ethers. These are aromatic compounds containing an ether group substituted with a benzene ring. Phenol Ethers Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenol Ethers Alkyl Aryl Ethers Phosphonic Acid Esters Polyamines alkyl aryl ether phosphonic acid ester phosphonic acid derivative ether polyamine logP 2.24 ALOGPS logS -2.5 ALOGPS Water Solubility 8.22e-01 g/l ALOGPS logP 2.82 ChemAxon IUPAC Name (R)-((2S)-1-phenoxybutan-2-yl chloro(methyl)phosphinate) ChemAxon Traditional IUPAC Name (R)-((2S)-1-phenoxybutan-2-yl chloro(methyl)phosphinate) ChemAxon Molecular Weight 262.67 ChemAxon Monoisotopic Weight 262.052558597 ChemAxon SMILES [H][C@](CC)(COC1=CC=CC=C1)O[P@](C)(Cl)=O ChemAxon Molecular Formula C11H16ClO3P ChemAxon InChI InChI=1S/C11H16ClO3P/c1-3-10(15-16(2,12)13)9-14-11-7-5-4-6-8-11/h4-8,10H,3,9H2,1-2H3/t10-,16+/m0/s1 ChemAxon InChIKey InChIKey=YEIXDWIEYXZUBR-MGPLVRAMSA-N ChemAxon Polar Surface Area (PSA) 35.53 ChemAxon Refractivity 64.73 ChemAxon Polarizability 25.59 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest basic) -4.9 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937149 PubChem Substance 99444890 PDB POT BE0003764 Lipase Burkholderia cepacia # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Lipase Involved in calcium ion binding Catalyzes the hydrolysis of triglycerides lipA None 6.71 37493.9 Burkholderia cepacia GeneCards lipA GenBank Gene Database M58494 GenBank Protein Database 557867 UniProtKB P22088 UniProt Accession LIP_BURCE Triacylglycerol lipase >Lipase MARTMRSRVVAGAVACAMSIAPFAGTTAVMTLATTHAAMAATAPAAGYAATRYPIILVHG LSGTDKYAGVLEYWYGIQEDLQQNGATVYVANLSGFQSDDGPNGRGEQLLAYVKTVLAAT GATKVNLVGHSQGGLSSRYVAAVAPDLVASVTTIGTPHRGSEFADFVQDVLAYDPTGLSS SVIAAFVNVFGILTSSSHNTNQDALAALQTLTTARAATYNQNYPSAGLGAPGSCQTGAPT ETVGGNTHLLYSWAGTAIQPTLSVFGVTGATDTSTLPLVDPANVLDLSTLALFGTGTVMI NRGSGQNDGLVSKCSALYGKVLSTSYKWNHLDEINQLLGVRGAYAEDPVAVIRTHANRLK LAGV >1095 bp ATGGCCAGGACGATGCGTTCCAGGGTGGTGGCAGGGGCAGTGGCATGCGCGATGAGCATC GCGCCGTTCGCGGGGACGACCGCGGTGATGACGCTCGCGACGACGCACGCGGCAATGGCG GCCACCGCGCCCGCCGCTGGCTACGCGGCGACGCGTTACCCGATCATCCTCGTGCACGGG CTCTCGGGTACCGACAAGTACGCCGGCGTGCTCGAGTATTGGTACGGCATCCAGGAGGAC CTGCAACAGAACGGTGCGACCGTCTACGTCGCGAACCTGTCGGGTTTCCAGAGCGACGAC GGCCCGAACGGGCGCGGCGAACAGTTGCTCGCTTACGTGAAGACGGTGCTCGCGGCGACG GGGGCGACCAAGGTCAATCTCGTCGGTCACAGCCAGGGCGGCCTCTCGTCGCGCTATGTT GCTGCCGTCGCGCCCGATCTCGTTGCGTCGGTGACGACGATCGGCACGCCGCATCGCGGC TCCGAATTCGCCGACTTCGTGCAGGACGTGCTCGCGTACGATCCGACCGGGCTTTCGTCA TCGGTGATCGCCGCGTTCGTCAATGTGTTCGGGATCCTGACGAGCAGCAGCCACAACACC AACCAGGACGCGCTCGCCGCACTGCAGACGCTGACCACCGCACGGGCCGCCACGTACAAC CAGAACTATCCGAGCGCGGGCCTGGGTGCGCCGGGCAGTTGCCAGACCGGTGCGCCGACC GAAACCGTCGGCGGCAACACGCACCTGCTGTATTCGTGGGCCGGCACGGCGATCCAGCCG ACGCTCTCCGTGTTCGGCGTCACGGGCGCGACGGACACGAGCACCCTTCCGCTCGTCGAT CCGGCGAACGTGCTCGACCTGTCGACGCTCGCGCTGTTCGGCACCGGCACGGTGATGATC AACCGCGGCTCCGGGCAGAACGACGGGCTCGTGTCGAAGTGCAGTGCGCTGTACGGCAAG GTGCTGAGCACGAGCTACAAGTGGAACCACCTCGACGAGATCAACCAGCTGCTCGGCGTG CGCGGCGCGTATGCGGAAGATCCCGTCGCGGTGATCCGCACGCATGCGAACCGGCTGAAG CTGGCGGGCGTGTAA PF00561 Abhydrolase_1 function catalytic activity "
drug:(1S)-1-(PHENOXYMETHYL)PROPYL METHYLPHOSPHONOCHLORIDOATErdfs:label"(1S)-1-(PHENOXYMETHYL)PROPYL METHYLPHOSPHONOCHLORIDOATE"
drug:(1S)-1-(PHENOXYMETHYL)PROPYL METHYLPHOSPHONOCHLORIDOATErdf:typedrugbank:drugs
drug:(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOLdrugbank:description" experimental This compound belongs to the tryptamines and derivatives. These are compounds containing the tryptamine backbone, which is structurally characterized by an indole ring subsituted at the thrid position by an ethanamine. Tryptamines and Derivatives Organic Compounds Heterocyclic Compounds Indoles and Derivatives Tryptamines and Derivatives Indoles Substituted Pyrroles Benzene and Substituted Derivatives Hemiaminals Polyamines Monoalkylamines indole benzene substituted pyrrole pyrrole hemiaminal polyamine amine primary amine primary aliphatic amine organonitrogen compound logP 0.72 ALOGPS logS -1.5 ALOGPS Water Solubility 5.89e+00 g/l ALOGPS logP 0.89 ChemAxon IUPAC Name (1S)-1-amino-2-(1H-indol-3-yl)ethan-1-ol ChemAxon Traditional IUPAC Name (1S)-1-amino-2-(1H-indol-3-yl)ethanol ChemAxon Molecular Weight 176.2151 ChemAxon Monoisotopic Weight 176.094963016 ChemAxon SMILES [H][C@](N)(O)CC1=CNC2=CC=CC=C12 ChemAxon Molecular Formula C10H12N2O ChemAxon InChI InChI=1S/C10H12N2O/c11-10(13)5-7-6-12-9-4-2-1-3-8(7)9/h1-4,6,10,12-13H,5,11H2/t10-/m0/s1 ChemAxon InChIKey InChIKey=WNWJSYYPDDQIQV-JTQLQIEISA-N ChemAxon Polar Surface Area (PSA) 62.04 ChemAxon Refractivity 51.51 ChemAxon Polarizability 18.93 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 14.15 ChemAxon pKa (strongest basic) 8.92 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 20846113 PubChem Substance 99445120 ChemSpider 20163058 PDB TSC BE0004362 Aralkylamine dehydrogenase light chain Alcaligenes faecalis # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aralkylamine dehydrogenase light chain Involved in aralkylamine dehydrogenase activity Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor aauA Periplasm None 7.35 19651.9 Alcaligenes faecalis GeneCards aauA GenBank Gene Database AF302652 UniProtKB P84887 UniProt Accession AAUA_ALCFA AADH Aromatic amine dehydrogenase >Aralkylamine dehydrogenase light chain MRWLDKFGESLSRSVAHKTSRRSVLRSVGKLMVGSAFVLPVLPVARAAGGGGSSSGADHI SLNPDLANEDEVNSCDYWRHCAVDGFLCSCCGGTTTTCPPGSTPSPISWIGTCHNPHDGK DYLISYHDCCGKTACGRCQCNTQTRERPGYEFFLHNDVNWCMANENSTFHCTTSVLVGLA KN PF02975 Me-amine-dh_L BE0004363 Aralkylamine dehydrogenase heavy chain Alcaligenes faecalis # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aralkylamine dehydrogenase heavy chain Involved in amine dehydrogenase activity Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor aauB Periplasm None 7.36 42924.6 Alcaligenes faecalis GeneCards aauB GenBank Gene Database AF302652 UniProtKB P84888 UniProt Accession AAUB_ALCFA AADH Aromatic amine dehydrogenase >Aralkylamine dehydrogenase heavy chain MKSKFKLTTAAAMLGLMVLAGGAQAQDKPREVLTGGHSVSAPQENRIYVMDSVFMHLTES RVHVYDYTNGKFLGMVPTAFNGHVQVSNDGKKIYTMTTYHERITRGKRSDVVEVWDADKL TFEKEISLPPKRVQGLNYDGLFRQTTDGKFIVLQNASPATSIGIVDVAKGDYVEDVTAAA GCWSVIPQPNRPRSFMTICGDGGLLTINLGEDGKVASQSRSKQMFSVKDDPIFIAPALDK DKAHFVSYYGNVYSADFSGDEVKVDGPWSLLNDEDKAKNWVPGGYNLVGLHRASGRMYVF MHPDGKEGTHKFPAAEIWVMDTKTKQRVARIPGRDALSMTIDQQRNLMLTLDGGNVNVYD ISQPEPKLLRTIEGAAEASLQVQFHPVGGV PF06433 Me-amine-dh_H component cell component periplasmic space function oxidoreductase activity function oxidoreductase activity, acting on the CH-NH2 group of donors function amine dehydrogenase activity function catalytic activity process metabolism process nitrogen compound metabolism process amine metabolism process methylamine metabolism process physiological process "
drug:(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOLrdfs:label"(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL"
drug:(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOLrdf:typedrugbank:drugs
drug:(1S)-1-CYCLOPROPYL-2-[(2S)-4-(2,5-DIFLUOROPHENYL)-2-PHENYL-2,5-DIHYDRO-1H-PYRROL-1-YL]-2-OXOETHANAMINEdrugbank:description" experimental This compound belongs to the alpha amino acid amides. These are amide derivatives of alpha amino acids. Alpha Amino Acid Amides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Phenylpyrrolines Fluorobenzenes Aryl Fluorides Tertiary Carboxylic Acid Amides Pyrroles Tertiary Amines Enolates Polyamines Carboxylic Acids Monoalkylamines Organofluorides fluorobenzene aryl halide aryl fluoride benzene tertiary carboxylic acid amide pyrrole pyrroline carboxamide group tertiary amine enolate polyamine carboxylic acid amine organohalogen primary aliphatic amine organofluoride primary amine organonitrogen compound logP 3.04 ALOGPS logS -4.6 ALOGPS Water Solubility 8.84e-03 g/l ALOGPS logP 3.43 ChemAxon IUPAC Name (2S)-2-amino-2-cyclopropyl-1-[(2S)-4-(2,5-difluorophenyl)-2-phenyl-2,5-dihydro-1H-pyrrol-1-yl]ethan-1-one ChemAxon Traditional IUPAC Name (2S)-2-amino-2-cyclopropyl-1-[(2S)-4-(2,5-difluorophenyl)-2-phenyl-2,5-dihydropyrrol-1-yl]ethanone ChemAxon Molecular Weight 354.3931 ChemAxon Monoisotopic Weight 354.154369682 ChemAxon SMILES [H][C@](N)(C1CC1)C(=O)N1CC(=C[C@@]1([H])C1=CC=CC=C1)C1=CC(F)=CC=C1F ChemAxon Molecular Formula C21H20F2N2O ChemAxon InChI InChI=1S/C21H20F2N2O/c22-16-8-9-18(23)17(11-16)15-10-19(13-4-2-1-3-5-13)25(12-15)21(26)20(24)14-6-7-14/h1-5,8-11,14,19-20H,6-7,12,24H2/t19-,20-/m0/s1 ChemAxon InChIKey InChIKey=VCOUEHUEFUDZIS-PMACEKPBSA-N ChemAxon Polar Surface Area (PSA) 46.33 ChemAxon Refractivity 96.75 ChemAxon Polarizability 36.48 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 8.49 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 6102824 PubChem Substance 99444715 ChemSpider 4810325 PDB N4T BE0001852 Kinesin-like protein KIF11 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Kinesin-like protein KIF11 Replication, recombination and repair Motor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays KIF11 10q24.1 None 5.36 119160.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6388 GenAtlas KIF11 GeneCards KIF11 GenBank Gene Database X85137 GenBank Protein Database 1155084 UniProtKB P52732 UniProt Accession KIF11_HUMAN Kinesin-like protein 1 Kinesin-like spindle protein HKSP Kinesin-related motor protein Eg5 Thyroid receptor-interacting protein 5 TRIP-5 >Kinesin-like protein KIF11 MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADK SSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERS PNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSE RLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFS VTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVIT ALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNIL NKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIV ELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEY ITSALESTEEKLHDAASKLLNTVEETTKDVSGLHSKLDRKKAVDQHNAEAQDIFGKNLNS LFNNMEELIKDGSSKQKAMLEVHKTLFGNLLSSSVSALDTITTVALGSLTSIPENVSTHV SQIFNMILKEQSLAAESKTVLQELINVLKTDLLSSLEMILSPTVVSILKINSQLKHIFKT SLTVADKIEDQKKELDGFLSILCNNLHELQENTICSLVESQKQCGNLTEDLKTIKQTHSQ ELCKLMNLWTERFCALEEKCENIQKPLSSVQENIQQKSKDIVNKMTFHSQKFCADSDGFS QELRNFNQEGTKLVEESVKHSDKLNGNLEKISQETEQRCESLNTRTVYFSEQWVSSLNER EQELHNLLEVVSQCCEASSSDITEKSDGRKAAHEKQHNIFLDQMTIDEDKLIAQNLELNE TIKIGLTKLNCFLEQDLKLDIPTGTTPQRKSYLYPSTLVRTEPREHLLDQLKRKQPELLM MLNCSENNKEETIPDVDVEEAVLGQYTEEPLSQEPSVDAGVDCSSIGGVPFFQHKKSHGK DKENRGINTLERSKVEETTEHLVTKSRLPLRAQINL >3174 bp ATGGCGTCGCAGCCAAATTCGTCTGCGAAGAAGAAAGAGGAGAAGGGGAAGAACATCCAG GTGGTGGTGAGATGCAGACCATTTAATTTGGCAGAGCGGAAAGCTAGCGCCCATTCAATA GTAGAATGTGATCCTGTACGAAAAGAAGTTAGTGTACGAACTGGAGGATTGGCTGACAAG AGCTCAAGGAAAACATACACTTTTGATATGGTGTTTGGAGCATCTACTAAACAGATTGAT GTTTACCGAAGTGTTGTTTGTCCAATTCTGGATGAAGTTATTATGGGCTATAATTGCACT ATCTTTGCGTATGGCCAAACTGGCACTGGAAAAACTTTTACAATGGAAGGTGAAAGGTCA CCTAATGAAGAGTATACCTGGGAAGAGGATCCCTTGGCTGGTATAATTCCACGTACCCTT CATCAAATTTTTGAGAAACTTACTGATAATGGTACTGAATTTTCAGTCAAAGTGTCTCTG TTGGAGATCTATAATGAAGAGCTTTTTGATCTTCTTAATCCATCATCTGATGTTTCTGAG AGACTACAGATGTTTGATGATCCCCGTAACAAGAGAGGAGTGATAATTAAAGGTTTAGAA GAAATTACAGTACACAACAAGGATGAAGTCTATCAAATTTTAGAAAAGGGGGCAGCAAAA AGGACAACTGCAGCTACTCTGATGAATGCATACTCTAGTCGTTCCCACTCAGTTTTCTCT GTTACAATACATATGAAAGAAACTACGATTGATGGAGAAGAGCTTGTTAAAATCGGAAAG TTGAACTTGGTTGATCTTGCAGGAAGTGAAAACATTGGCCGTTCTGGAGCTGTTGATAAG AGAGCTCGGGAAGCTGGAAATATAAATCAATCCCTGTTGACTTTGGGAAGGGTCATTACT GCCCTTGTAGAAAGAACACCTCATGTTCCTTATCGAGAATCTAAACTAACTAGAATCCTC CAGGATTCTCTTGGAGGGCGTACAAGAACATCTATAATTGCAACAATTTCTCCTGCATCT CTCAATCTTGAGGAAACTCTGAGTACATTGGAATATGCTCATAGAGCAAAGAACATATTG AATAAGCCTGAAGTGAATCAGAAACTCACCAAAAAAGCTCTTATTAAGGAGTATACGGAG GAGATAGAACGTTTAAAACGAGATCTTGCTGCAGCCCGTGAGAAAAATGGAGTGTATATT TCTGAAGAAAATTTTAGAGTCATGAGTGGAAAATTAACTGTTCAAGAAGAGCAGATTGTA GAATTGATTGAAAAAATTGGTGCTGTTGAGGAGGAGCTGAATAGGGTTACAGAGTTGTTT ATGGATAATAAAAATGAACTTGACCAGTGTAAATCTGACCTGCAAAATAAAACACAAGAA CTTGAAACCACTCAAAAACATTTGCAAGAAACTAAATTACAACTTGTTAAAGAAGAATAT ATCACATCAGCTTTGGAAAGTACTGAGGAGAAACTTCATGATGCTGCCAGCAAGCTGCTT AACACAGTTGAAGAAACTACAAAAGATGTATCTGGTCTCCATTCCAAACTGGATCGTAAG AAGGCAGTTGACCAACACAATGCAGAAGCTCAGGATATTTTTGGCAAAAACCTGAATAGT CTGTTTAATAATATGGAAGAATTAATTAAGGATGGCAGCTCAAAGCAAAAGGCCATGCTA GAAGTACATAAGACCTTATTTGGTAATCTGCTGTCTTCCAGTGTCTCTGCATTAGATACC ATTACTACAGTAGCACTTGGATCTCTCACATCTATTCCAGAAAATGTGTCTACTCATGTT TCTCAGATTTTTAATATGATACTAAAAGAACAATCATTAGCAGCAGAAAGTAAAACTGTA CTACAGGAATTGATTAATGTACTCAAGACTGATCTTCTAAGTTCACTGGAAATGATTTTA TCCCCAACTGTGGTGTCTATACTGAAAATCAATAGTCAACTAAAGCATATTTTCAAGACT TCATTGACAGTGGCCGATAAGATAGAAGATCAAAAAAAAAGGAACTCAGATGGCTTTCTC AGTATACTGTGTAACAATCTACATGAACTACAAGAAAATACCATTTGTTCCTTGGTTGAG TCACAAAAGCAATGTGGAAACCTAACTGAAGACCTGAAGACAATAAAGCAGACCCATTCC CAGGAACTTTGCAAGTTAATGAATCTTTGGACAGAGAGATTCTGTGCTTTGGAGGAAAAG TGTGAAAATATACAGAAACCACTTAGTAGTGTCCAGGAAAATATACAGCAGAAATCTAAG GATATAGTCAACAAAATGACTTTTCACAGTCAAAAATTTTGTGCTGATTCTGATGGCTTC TCACAGGAACTCAGAAATTTTAACCAAGAAGGTACAAAATTGGTTGAAGAATCTGTGAAA CACTCTGATAAACTCAATGGCAACCTGGAAAAAATATCTCAAGAGACTGAACAGAGATGT GAATCTCTGAACACAAGAACAGTTTATTTTTCTGAACAGTGGGTATCTTCCTTAAATGAA AGGGAACAGGAACTTCACAACTTATTGGAGGTTGTAAGCCAATGTTGTGAGGCTTCAAGT TCAGACATCACTGAGAAATCAGATGGACGTAAGGCAGCTCATGAGAAACAGCATAACATT TTTCTTGATCAGATGACTATTGATGAAGATAAATTGATAGCACAAAATCTAGAACTTAAT GAAACCATAAAAATTGGTTTGACTAAGCTTAATTGCTTTCTGGAACAGGATCTGAAACTG GATATCCCAACAGGTACGACACCACAGAGGAAAAGTTATTTATACCCATCAACACTGGTA AGAACTGAACCACGTGAACATCTCCTTGATCAGCTGAAAAGGAAACAGCCTGAGCTGTTA ATGATGCTAAACTGTTCAGAAAACAACAAAGAAGAGACAATTCCGGATGTGGATGTAGAA GAGGCAGTTCTGGGGCAGTATACTGAAGAACCTCTAAGTCAAGAGCCATCTGTAGATGCT GGTGTGGATTGTTCATCAATTGGCGGGGTTCCATTTTTCCAGCATAAAAAATCACATGGA AAAGACAAAGAAAACAGAGGCATTAACACACTGGAGAGGTCTAAAGTGGAAGAAACTACA GAGCACTTGGTTACAAAGAGCAGATTACCTCTGCGAGCCCAGATCAACCTTTAA PF00225 Kinesin component microtubule associated complex component protein complex function ATP binding function binding function motor activity function microtubule motor activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding process organelle organization and biogenesis process cytoskeleton organization and biogenesis process microtubule-based process process physiological process process microtubule-based movement process cellular physiological process process cell organization and biogenesis "
drug:(1S)-1-CYCLOPROPYL-2-[(2S)-4-(2,5-DIFLUOROPHENYL)-2-PHENYL-2,5-DIHYDRO-1H-PYRROL-1-YL]-2-OXOETHANAMINErdfs:label"(1S)-1-CYCLOPROPYL-2-[(2S)-4-(2,5-DIFLUOROPHENYL)-2-PHENYL-2,5-DIHYDRO-1H-PYRROL-1-YL]-2-OXOETHANAMINE"
drug:(1S)-1-CYCLOPROPYL-2-[(2S)-4-(2,5-DIFLUOROPHENYL)-2-PHENYL-2,5-DIHYDRO-1H-PYRROL-1-YL]-2-OXOETHANAMINErdf:typedrugbank:drugs
drug:(1S)-1-{[(4'-METHOXY-1,1'-BIPHENYL-4-YL)SULFONYL]AMINO}-2-METHYLPROPYLPHOSPHONIC ACIDdrugbank:description" experimental This compound belongs to the biphenyls and derivatives. These are organic compounds containing to benzene rings linked together by a C-C bond. Biphenyls and Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Biphenyls and Derivatives Benzenesulfonamides Anisoles Alkyl Aryl Ethers Organic Phosphonic Acids Sulfonyls Sulfonamides Polyamines benzenesulfonamide anisole phenol ether alkyl aryl ether sulfonic acid derivative sulfonamide sulfonyl phosphonic acid derivative phosphonic acid polyamine ether amine organonitrogen compound logP 1.43 ALOGPS logS -2.9 ALOGPS Water Solubility 4.61e-01 g/l ALOGPS logP 2.43 ChemAxon IUPAC Name [(1S)-1-{[4-(4-methoxyphenyl)benzene]sulfonamido}-2-methylpropyl]phosphonic acid ChemAxon Traditional IUPAC Name (1S)-1-[4-(4-methoxyphenyl)benzenesulfonamido]-2-methylpropylphosphonic acid ChemAxon Molecular Weight 399.398 ChemAxon Monoisotopic Weight 399.090544643 ChemAxon SMILES [H][C@@](NS(=O)(=O)C1=CC=C(C=C1)C1=CC=C(OC)C=C1)(C(C)C)P(O)(O)=O ChemAxon Molecular Formula C17H22NO6PS ChemAxon InChI InChI=1S/C17H22NO6PS/c1-12(2)17(25(19,20)21)18-26(22,23)16-10-6-14(7-11-16)13-4-8-15(24-3)9-5-13/h4-12,17-18H,1-3H3,(H2,19,20,21)/t17-/m0/s1 ChemAxon InChIKey InChIKey=BZVYQWLRCHLAGK-KRWDZBQOSA-N ChemAxon Polar Surface Area (PSA) 112.93 ChemAxon Refractivity 98.92 ChemAxon Polarizability 38.92 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 1.48 ChemAxon pKa (strongest basic) -4.8 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 6540261 PubChem Substance 99444184 ChemSpider 5022660 PDB EIN BE0001182 Neutrophil collagenase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Neutrophil collagenase Involved in protease activity and collagen degradation Can degrade fibrillar type I, II, and III collagens MMP8 11q22.3 Cytoplasmic granule. Note=Stored in intracellular granules None 6.86 53413.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7175 GenAtlas MMP8 GeneCards MMP8 GenBank Gene Database J05556 GenBank Protein Database 180618 UniProtKB P22894 UniProt Accession MMP8_HUMAN EC 3.4.24.34 Matrix metalloproteinase-8 MMP-8 Neutrophil collagenase precursor PMNL collagenase PMNL-CL >Neutrophil collagenase precursor MFSLKTLPFLLLLHVQISKAFPVSSKEKNTKTVQDYLEKFYQLPSNQYQSTRKNGTNVIV EKLKEMQRFFGLNVTGKPNEETLDMMKKPRCGVPDSGGFMLTPGNPKWERTNLTYRIRNY TPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGIL AHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYA FRETSNYSLPQDDIDGIQAIYGLSSNPIQPTGPSTPKPCDPSLTFDAITTLRGEILFFKD RYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGYDILQG YPKDISNYGFPSSVQAIDAAVFYRSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGI ESKVDAVFQQEHFFHVFSGPRYYAFDLIAQRVTRVARGNKWLNCRYG >1404 bp ATGTTCTCCCTGAAGACGCTTCCATTTCTGCTCTTACTCCATGTGCAGATTTCCAAGGCC TTTCCTGTATCTTCTAAAGAGAAAAATACAAAAACTGTTCAGGACTACCTGGAAAAGTTC TACCAATTACCAAGCAACCAGTATCAGTCTACAAGGAAGAATGGCACTAATGTGATCGTT GAAAAGCTTAAAGAAATGCAGCGATTTTTTGGGTTGAATGTGACGGGGAAGCCAAATGAG GAAACTCTGGACATGATGAAAAAGCCTCGCTGTGGAGTGCCTGACAGTGGTGGTTTTATG TTAACCCCAGGAAACCCCAAGTGGGAACGCACTAACTTGACCTACAGGATTCGAAACTAT ACCCCACAGCTGTCAGAGGCTGAGGTAGAAAGAGCTATCAAGGATGCCTTTGAACTCTGG AGTGTTGCATCACCTCTCATCTTCACCAGGATCTCACAGGGAGAGGCAGATATCAACATT GCTTTTTACCAAAGAGATCACGGTGACAATTCTCCATTTGATGGACCCAATGGAATCCTT GCTCATGCCTTTCAGCCAGGCCAAGGTATTGGAGGAGATGCTCATTTTGATGCCGAAGAA ACATGGACCAACACCTCCGCAAATTACAACTTGTTTCTTGTTGCTGCTCATGAATTTGGC CATTCTTTGGGGCTCGCTCACTCCTCTGACCCTGGTGCCTTGATGTATCCCAACTATGCT TTCAGGGAAACCAGCAACTACTCACTCCCTCAAGATGACATCGATGGCATTCAGGCCATC TATGGACTTTCAAGCAACCCTATCCAACCTACTGGACCAAGCACACCCAAACCCTGTGAC CCCAGTTTGACATTTGATGCTATCACCACACTCCGTGGAGAAATACTTTTCTTTAAAGAC AGGTACTTCTGGAGAAGGCATCCTCAGCTACAAAGAGTCGAAATGAATTTTATTTCTCTA TTCTGGCCATCCCTTCCAACTGGTATACAGGCTGCTTATGAAGATTTTGACAGAGACCTC ATTTTCCTATTTAAAGGCAACCAATACTGGGCTCTGAGTGGCTATGATATTCTGCAAGGT TATCCCAAGGATATATCAAACTATGGCTTCCCCAGCAGCGTCCAAGCAATTGACGCAGCT GTTTTCTACAGAAGTAAAACATACTTCTTTGTAAATGACCAATTCTGGAGATATGATAAC CAAAGACAATTCATGGAGCCAGGTTATCCCAAAAGCATATCAGGTGCCTTTCCAGGAATA GAGAGTAAAGTTGATGCAGTTTTCCAGCAAGAACATTTCTTCCATGTCTTCAGTGGACCA AGATATTACGCATTTGATCTTATTGCTCAGAGAGTTACCAGAGTTGCAAGAGGCAATAAA TGGCTTAACTGTAGATATGGCTGA PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix component extracellular matrix (sensu Metazoa) function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding function catalytic activity function hydrolase activity process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism "
drug:(1S)-1-{[(4'-METHOXY-1,1'-BIPHENYL-4-YL)SULFONYL]AMINO}-2-METHYLPROPYLPHOSPHONIC ACIDrdfs:label"(1S)-1-{[(4'-METHOXY-1,1'-BIPHENYL-4-YL)SULFONYL]AMINO}-2-METHYLPROPYLPHOSPHONIC ACID"
drug:(1S)-1-{[(4'-METHOXY-1,1'-BIPHENYL-4-YL)SULFONYL]AMINO}-2-METHYLPROPYLPHOSPHONIC ACIDrdf:typedrugbank:drugs
drug:(1S)-2-(1H-INDOL-3-YL)-1-[({5-[(E)-2-PYRIDIN-4-YLVINYL]PYRIDIN-3-YL}OXY)METHYL]ETHYLAMINEdrugbank:description" experimental This compound belongs to the tryptamines and derivatives. These are compounds containing the tryptamine backbone, which is structurally characterized by an indole ring subsituted at the thrid position by an ethanamine. Tryptamines and Derivatives Organic Compounds Heterocyclic Compounds Indoles and Derivatives Tryptamines and Derivatives Indoles Alkyl Aryl Ethers Substituted Pyrroles Pyridines and Derivatives Benzene and Substituted Derivatives Polyamines Monoalkylamines indole alkyl aryl ether substituted pyrrole pyridine benzene pyrrole ether polyamine amine primary aliphatic amine primary amine organonitrogen compound logP 3.12 ALOGPS logS -5.7 ALOGPS Water Solubility 7.53e-04 g/l ALOGPS logP 3.09 ChemAxon IUPAC Name 3-[(2S)-2-amino-3-({5-[(E)-2-(pyridin-4-yl)ethenyl]pyridin-3-yl}oxy)propyl]-1H-indole ChemAxon Traditional IUPAC Name 3-[(2S)-2-amino-3-({5-[(E)-2-(pyridin-4-yl)ethenyl]pyridin-3-yl}oxy)propyl]-1H-indole ChemAxon Molecular Weight 370.447 ChemAxon Monoisotopic Weight 370.179361346 ChemAxon SMILES [H][C@@](N)(COC1=CN=CC(\C=C\C2=CC=NC=C2)=C1)CC1=CNC2=C1C=CC=C2 ChemAxon Molecular Formula C23H22N4O ChemAxon InChI InChI=1S/C23H22N4O/c24-20(12-19-14-27-23-4-2-1-3-22(19)23)16-28-21-11-18(13-26-15-21)6-5-17-7-9-25-10-8-17/h1-11,13-15,20,27H,12,16,24H2/b6-5+/t20-/m0/s1 ChemAxon InChIKey InChIKey=SGHXFHRRWFLILP-XJDXJNMNSA-N ChemAxon Polar Surface Area (PSA) 76.82 ChemAxon Refractivity 111.74 ChemAxon Polarizability 41.93 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 17.11 ChemAxon pKa (strongest basic) 9.24 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 6914613 PubChem Substance 99443578 ChemSpider 5290493 PDB 4EA BE0003761 cAMP-dependent protein kinase catalytic subunit alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown cAMP-dependent protein kinase catalytic subunit alpha Involved in ATP binding Phosphorylates a large number of substrates in the cytoplasm and the nucleus PRKACA 19p13.1 Cytoplasm (By similarity). Nucleus (By similarity) None 9.22 40589.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9380 GeneCards PRKACA GenBank Gene Database X07767 GenBank Protein Database 35479 UniProtKB P17612 UniProt Accession KAPCA_HUMAN PKA C-alpha >cAMP-dependent protein kinase catalytic subunit alpha MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVML VKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF >1056 bp ATGGGCAACGCCGCCGCCGCCAAGAAGGGCAGCGAGCAGGAGAGCGTGAAAGAATTCTTA GCCAAAGCCAAAGAAGATTTTCTTAAAAAATGGGAAAGTCCCGCTCAGAACACAGCCCAC TTGGATCAGTTTGAACGAATCAAGACCCTCGGCACGGGCTCCTTCGGGCGGGTGATGCTG GTGAAACACAAGGAGACCGGGAACCACTATGCCATGAAGATCCTCGACAAACAGAAGGTG GTGAAACTGAAACAGATCGAACACACCCTGAATGAAAAGCGCATCCTGCAAGCTGTCAAC TTTCCGTTCCTCGTCAAACTCGAGTTCTCCTTCAAGGACAACTCAAACTTATACATGGTC ATGGAGTACGTGCCCGGCGGGGAGATGTTCTCACACCTACGGCGGATCGGAAGGTTCAGT GAGCCCCATGCCCGTTTCTACGCGGCCCAGATCGTCCTGACCTTTGAGTATCTGCACTCG CTGGATCTCATCTACAGGGACCTGAAGCCGGAGAATCTGCTCATTGACCAGCAGGGCTAC ATTCAGGTGACAGACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGC GGCACCCCTGAGTACCTGGCCCCTGAGATTATCCTGAGCAAAGGCTACAACAAGGCCGTG GACTGGTGGGCCCTGGGGGTTCTTATCTATGAAATGGCCGCTGGCTACCCGCCCTTCTTC GCAGACCAGCCCATCCAGATCTATGAGAAGATCGTCTCTGGGAAGGTGCGCTTCCCTTCC CACTTCAGCTCTGACTTGAAGGACCTGCTGCGGAACCTCCTGCAGGTAGATCTCACCAAG CGCTTTGGGAACCTCAAGAATGGGGTCAACGATATCAAGAACCACAAGTGGTTTGCCACA ACTGACTGGATTGCCATCTACCAGAGGAAGGTGGAAGCTCCCTTCATACCAAAGTTTAAA GGCCCTGGGGATACGAGTAACTTTGACGACTATGAGGAAGAAGAAATCCGGGTCTCCATC AATGAGAAGTGTGGCAAGGAGTTTTCTGAGTTTTAG PF00069 Pkinase function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process BE0003762 cAMP-dependent protein kinase inhibitor alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown cAMP-dependent protein kinase inhibitor alpha Involved in cAMP-dependent protein kinase inhibitor act Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains PKIA 8q21.12 None 4.18 7988.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9017 GeneCards PKIA GenBank Gene Database S76965 GenBank Protein Database 243494 UniProtKB P61925 UniProt Accession IPKA_HUMAN cAMP-dependent protein kinase inhibitor, muscle/brain isoform PKI-alpha >cAMP-dependent protein kinase inhibitor alpha MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSS TEQSGEAQGEAAKSES >231 bp ATGACTGATGTGGAAACTACATATGCAGATTTTATTGCTTCAGGAAGAACAGGTAGAAGA AATGCAATACATGATATCCTGGTTTCCTCTGCAAGTGGCAACAGCAATGAATTAGCCTTG AAATTAGCAGGTCTTGATATCAACAAGACAGAAGGTGAAGAAGATGCACAACGAAGTTCT ACAGAACAAAGTGGGGAAGCCCAGGGAGAAGCAGCAAAATCTGAAAGCTAA PF02827 PKI function enzyme inhibitor activity function kinase inhibitor activity function protein kinase inhibitor activity function cAMP-dependent protein kinase inhibitor activity function enzyme regulator activity process regulation of enzyme activity process regulation of transferase activity process regulation of kinase activity process regulation of protein kinase activity process negative regulation of protein kinase activity process regulation of biological process "
drug:(1S)-2-(1H-INDOL-3-YL)-1-[({5-[(E)-2-PYRIDIN-4-YLVINYL]PYRIDIN-3-YL}OXY)METHYL]ETHYLAMINErdfs:label"(1S)-2-(1H-INDOL-3-YL)-1-[({5-[(E)-2-PYRIDIN-4-YLVINYL]PYRIDIN-3-YL}OXY)METHYL]ETHYLAMINE"
drug:(1S)-2-(1H-INDOL-3-YL)-1-[({5-[(E)-2-PYRIDIN-4-YLVINYL]PYRIDIN-3-YL}OXY)METHYL]ETHYLAMINErdf:typedrugbank:drugs
drug:(1S)-2-(1H-INDOL-3-YL)-1-{[(5-ISOQUINOLIN-6-YLPYRIDIN-3-YL)OXY]METHYL}ETHYLAMINEdrugbank:description" experimental This compound belongs to the isoquinolines and derivatives. These are aromatic polycyclic compounds containing an isoquinoline moiety, which consists of a benzene ring fused to a pyridine ring and forming benzo[c]pyridine. Isoquinolines and Derivatives Organic Compounds Heterocyclic Compounds Isoquinolines and Derivatives Indoles Alkyl Aryl Ethers Pyridines and Derivatives Benzene and Substituted Derivatives Polyamines Monoalkylamines alkyl aryl ether benzene pyridine ether polyamine primary amine primary aliphatic amine amine organonitrogen compound logP 3.33 ALOGPS logS -6.1 ALOGPS Water Solubility 3.20e-04 g/l ALOGPS logP 2.99 ChemAxon IUPAC Name 6-{5-[(2S)-2-amino-3-[(3R)-3H-indol-3-yl]propoxy]pyridin-3-yl}isoquinoline ChemAxon Traditional IUPAC Name 6-{5-[(2S)-2-amino-3-[(3R)-3H-indol-3-yl]propoxy]pyridin-3-yl}isoquinoline ChemAxon Molecular Weight 394.4684 ChemAxon Monoisotopic Weight 394.179361346 ChemAxon SMILES [H][C@@](N)(COC1=CN=CC(=C1)C1=CC2=C(C=C1)C=NC=C2)C[C@@]1([H])C=NC2=C1C=CC=C2 ChemAxon Molecular Formula C25H22N4O ChemAxon InChI InChI=1S/C25H22N4O/c26-22(10-21-14-29-25-4-2-1-3-24(21)25)16-30-23-11-20(13-28-15-23)17-5-6-19-12-27-8-7-18(19)9-17/h1-9,11-15,21-22H,10,16,26H2/t21-,22-/m0/s1 ChemAxon InChIKey InChIKey=BUCZDJYEOAQTHL-VXKWHMMOSA-N ChemAxon Polar Surface Area (PSA) 73.39 ChemAxon Refractivity 119.38 ChemAxon Polarizability 44.08 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 13.74 ChemAxon pKa (strongest basic) 9.53 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 5 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 46937039 PubChem Substance 99443430 PDB 2EA BE0003761 cAMP-dependent protein kinase catalytic subunit alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown cAMP-dependent protein kinase catalytic subunit alpha Involved in ATP binding Phosphorylates a large number of substrates in the cytoplasm and the nucleus PRKACA 19p13.1 Cytoplasm (By similarity). Nucleus (By similarity) None 9.22 40589.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9380 GeneCards PRKACA GenBank Gene Database X07767 GenBank Protein Database 35479 UniProtKB P17612 UniProt Accession KAPCA_HUMAN PKA C-alpha >cAMP-dependent protein kinase catalytic subunit alpha MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVML VKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF >1056 bp ATGGGCAACGCCGCCGCCGCCAAGAAGGGCAGCGAGCAGGAGAGCGTGAAAGAATTCTTA GCCAAAGCCAAAGAAGATTTTCTTAAAAAATGGGAAAGTCCCGCTCAGAACACAGCCCAC TTGGATCAGTTTGAACGAATCAAGACCCTCGGCACGGGCTCCTTCGGGCGGGTGATGCTG GTGAAACACAAGGAGACCGGGAACCACTATGCCATGAAGATCCTCGACAAACAGAAGGTG GTGAAACTGAAACAGATCGAACACACCCTGAATGAAAAGCGCATCCTGCAAGCTGTCAAC TTTCCGTTCCTCGTCAAACTCGAGTTCTCCTTCAAGGACAACTCAAACTTATACATGGTC ATGGAGTACGTGCCCGGCGGGGAGATGTTCTCACACCTACGGCGGATCGGAAGGTTCAGT GAGCCCCATGCCCGTTTCTACGCGGCCCAGATCGTCCTGACCTTTGAGTATCTGCACTCG CTGGATCTCATCTACAGGGACCTGAAGCCGGAGAATCTGCTCATTGACCAGCAGGGCTAC ATTCAGGTGACAGACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGC GGCACCCCTGAGTACCTGGCCCCTGAGATTATCCTGAGCAAAGGCTACAACAAGGCCGTG GACTGGTGGGCCCTGGGGGTTCTTATCTATGAAATGGCCGCTGGCTACCCGCCCTTCTTC GCAGACCAGCCCATCCAGATCTATGAGAAGATCGTCTCTGGGAAGGTGCGCTTCCCTTCC CACTTCAGCTCTGACTTGAAGGACCTGCTGCGGAACCTCCTGCAGGTAGATCTCACCAAG CGCTTTGGGAACCTCAAGAATGGGGTCAACGATATCAAGAACCACAAGTGGTTTGCCACA ACTGACTGGATTGCCATCTACCAGAGGAAGGTGGAAGCTCCCTTCATACCAAAGTTTAAA GGCCCTGGGGATACGAGTAACTTTGACGACTATGAGGAAGAAGAAATCCGGGTCTCCATC AATGAGAAGTGTGGCAAGGAGTTTTCTGAGTTTTAG PF00069 Pkinase function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process BE0003762 cAMP-dependent protein kinase inhibitor alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown cAMP-dependent protein kinase inhibitor alpha Involved in cAMP-dependent protein kinase inhibitor act Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains PKIA 8q21.12 None 4.18 7988.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9017 GeneCards PKIA GenBank Gene Database S76965 GenBank Protein Database 243494 UniProtKB P61925 UniProt Accession IPKA_HUMAN cAMP-dependent protein kinase inhibitor, muscle/brain isoform PKI-alpha >cAMP-dependent protein kinase inhibitor alpha MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSS TEQSGEAQGEAAKSES >231 bp ATGACTGATGTGGAAACTACATATGCAGATTTTATTGCTTCAGGAAGAACAGGTAGAAGA AATGCAATACATGATATCCTGGTTTCCTCTGCAAGTGGCAACAGCAATGAATTAGCCTTG AAATTAGCAGGTCTTGATATCAACAAGACAGAAGGTGAAGAAGATGCACAACGAAGTTCT ACAGAACAAAGTGGGGAAGCCCAGGGAGAAGCAGCAAAATCTGAAAGCTAA PF02827 PKI function enzyme inhibitor activity function kinase inhibitor activity function protein kinase inhibitor activity function cAMP-dependent protein kinase inhibitor activity function enzyme regulator activity process regulation of enzyme activity process regulation of transferase activity process regulation of kinase activity process regulation of protein kinase activity process negative regulation of protein kinase activity process regulation of biological process "
drug:(1S)-2-(1H-INDOL-3-YL)-1-{[(5-ISOQUINOLIN-6-YLPYRIDIN-3-YL)OXY]METHYL}ETHYLAMINErdfs:label"(1S)-2-(1H-INDOL-3-YL)-1-{[(5-ISOQUINOLIN-6-YLPYRIDIN-3-YL)OXY]METHYL}ETHYLAMINE"
drug:(1S)-2-(1H-INDOL-3-YL)-1-{[(5-ISOQUINOLIN-6-YLPYRIDIN-3-YL)OXY]METHYL}ETHYLAMINErdf:typedrugbank:drugs
drug:(1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-ETHYNYLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINEdrugbank:description" experimental This compound belongs to the alpha amino acid amides. These are amide derivatives of alpha amino acids. Alpha Amino Acid Amides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Tertiary Carboxylic Acid Amides Pyrrolidines Tertiary Amines Polyamines Carboxylic Acids Enolates Monoalkylamines pyrrolidine tertiary carboxylic acid amide carboxamide group tertiary amine polyamine enolate carboxylic acid amine primary amine primary aliphatic amine organonitrogen compound logP 0.46 ALOGPS logS -3.2 ALOGPS Water Solubility 1.66e-01 g/l ALOGPS logP 0.33 ChemAxon IUPAC Name (2S)-2-amino-1-[(2S,5R)-2-(aminomethyl)-5-ethynylpyrrolidin-1-yl]-2-cyclopentylethan-1-one ChemAxon Traditional IUPAC Name (2S)-2-amino-1-[(2S,5R)-2-(aminomethyl)-5-ethynylpyrrolidin-1-yl]-2-cyclopentylethanone ChemAxon Molecular Weight 249.3519 ChemAxon Monoisotopic Weight 249.184112373 ChemAxon SMILES [H][C@](N)(C1CCCC1)C(=O)N1[C@]([H])(CN)CC[C@]1([H])C#C ChemAxon Molecular Formula C14H23N3O ChemAxon InChI InChI=1S/C14H23N3O/c1-2-11-7-8-12(9-15)17(11)14(18)13(16)10-5-3-4-6-10/h1,10-13H,3-9,15-16H2/t11-,12-,13-/m0/s1 ChemAxon InChIKey InChIKey=XYVMJMYCUZCIPB-AVGNSLFASA-N ChemAxon Polar Surface Area (PSA) 72.35 ChemAxon Refractivity 70.92 ChemAxon Polarizability 28.34 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest basic) 9.26 ChemAxon Physiological Charge 2 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon ChEBI 40697 PubChem Compound 11840917 PubChem Substance 99443827 ChemSpider 10015422 PDB AIA BE0000854 Dipeptidyl peptidase 4 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dipeptidyl peptidase 4 Amino acid transport and metabolism Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Plays a role in T-cell activation DPP4 2q24.3 Cell membrane; single-pass type II membrane protein. Processed form:Secreted protein. Note=Also exis 7-28 5.92 88279.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3009 GenAtlas DPP4 GeneCards DPP4 GenBank Gene Database U13735 GenBank Protein Database 535388 UniProtKB P27487 UniProt Accession DPP4_HUMAN ADABP Adenosine deaminase complexing protein 2 Dipeptidyl peptidase IV DPP IV EC 3.4.14.5 T-cell activation antigen CD26 TP103 >Dipeptidyl peptidase 4 MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSL RWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNY VKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNL PSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYL CDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPS EPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISN EYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKY PLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGT FEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWE YYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP >2301 bp ATGAAGACACCGTGGAAGGTTCTTCTGGGACTGCTGGGTGCTGCTGCGCTTGTCACCATC ATCACCGTGCCCGTGGTTCTGCTGAACAAAGGCACAGATGATGCTACAGCTGACAGTCGC AAAACTTACACTCTAACTGATTACTTAAAAAATACTTATAGACTGAAGTTATACTCCTTA AGATGGATTTCAGATCATGAATATCTCTACAAACAAGAAAATAATATCTTGGTATTCAAT GCTGAATATGGAAACAGCTCAGTTTTCTTGGAGAACAGTACATTTGATGAGTTTGGACAT TCTATCAATGATTATTCAATATCTCCTGATGGGCAGTTTATTCTCTTAGAATACAACTAC GTGAAGCAATGGAGGCATTCCTACACAGCTTCATATGACATTTATGATTTAAATAAAAGG CAGCTGATTACAGAAGAGAGGATTCCAAACAACACACAGTGGGTCACATGGTCACCAGTG GGTCATAAATTGGCATATGTTTGGAACAATGACATTTATGTTAAAATTGAACCAAATTTA CCAAGTTACAGAATCACATGGACGGGGAAAGAAGATATAATATATAATGGAATAACTGAC TGGGTTTATGAAGAGGAAGTCTTCAGTGCCTACTCTGCTCTGTGGTGGTCTCCAAACGGC ACTTTTTTAGCATATGCCCAATTTAACGACACAGAAGTCCCACTTATTGAATACTCCTTC TACTCTGATGAGTCACTGCAGTACCCAAAGACTGTACGGGTTCCATATCCAAAGGCAGGA GCTGTGAATCCAACTGTAAAGTTCTTTGTTGTAAATACAGACTCTCTCAGCTCAGTCACC AATGCAACTTCCATACAAATCACTGCTCCTGCTTCTATGTTGATAGGGGATCACTACTTG TGTGATGTGACATGGGCAACACAAGAAAGAATTTCTTTGCAGTGGCTCAGGAGGATTCAG AACTATTCGGTCATGGATATTTGTGACTATGATGAATCCAGTGGAAGATGGAACTGCTTA GTGGCACGGCAACACATTGAAATGAGTACTACTGGCTGGGTTGGAAGATTTAGGCCTTCA GAACCTCATTTTACCCTTGATGGTAATAGCTTCTACAAGATCATCAGCAATGAAGAAGGT TACAGACACATTTGCTATTTCCAAATAGATAAAAAAGACTGCACATTTATTACAAAAGGC ACCTGGGAAGTCATCGGGATAGAAGCTCTAACCAGTGATTATCTATACTACATTAGTAAT GAATATAAAGGAATGCCAGGAGGAAGGAATCTTTATAAAATCCAACTTAGTGACTATACA AAAGTGACATGCCTCAGTTGTGAGCTGAATCCGGAAAGGTGTCAGTACTATTCTGTGTCA TTCAGTAAAGAGGCGAAGTATTATCAGCTGAGATGTTCCGGTCCTGGTCTGCCCCTCTAT ACTCTACACAGCAGCGTGAATGATAAAGGGCTGAGAGTCCTGGAAGACAATTCAGCTTTG GATAAAATGCTGCAGAATGTCCAGATGCCCTCCAAAAAACTGGACTTCATTATTTTGAAT GAAACAAAATTTTGGTATCAGATGATCTTGCCTCCTCATTTTGATAAATCCAAGAAATAT CCTCTACTATTAGATGTGTATGCAGGCCCATGTAGTCAAAAAGCAGACACTGTCTTCAGA CTGAACTGGGCCACTTACCTTGCAAGCACAGAAAACATTATAGTAGCTAGCTTTGATGGC AGAGGAAGTGGTTACCAAGGAGATAAGATCATGCATGCAATCAACAGAAGACTGGGAACA TTTGAAGTTGAAGATCAAATTGAAGCAGCCAGACAATTTTCAAAAATGGGATTTGTGGAC AACAAACGAATTGCAATTTGGGGCTGGTCATATGGAGGGTACGTAACCTCAATGGTCCTG GGATCGGGAAGTGGCGTGTTCAAGTGTGGAATAGCCGTGGCGCCTGTATCCCGGTGGGAG TACTATGACTCAGTGTACACAGAACGTTACATGGGTCTCCCAACTCCAGAAGACAACCTT GACCATTACAGAAATTCAACAGTCATGAGCAGAGCTGAAAATTTTAAACAAGTTGAGTAC CTCCTTATTCATGGAACAGCAGATGATAACGTTCACTTTCAGCAGTCAGCTCAGATCTCC AAAGCCCTGGTCGATGTTGGAGTGGATTTCCAGGCAATGTGGTATACTGATGAAGACCAT GGAATAGCTAGCAGCACAGCACACCAACATATATATACCCACATGAGCCACTTCATAAAA CAATGTTTCTCTTTACCTTAG PF00930 DPPIV_N PF00326 Peptidase_S9 component cell component membrane function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function serine-type peptidase activity function hydrolase activity function dipeptidyl-peptidase IV activity function prolyl oligopeptidase activity process protein metabolism process cellular protein metabolism process physiological process process proteolysis process metabolism process macromolecule metabolism "
drug:(1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-ETHYNYLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINErdfs:label"(1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-ETHYNYLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINE"
drug:(1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-ETHYNYLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINErdf:typedrugbank:drugs
drug:(1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-PROP-1-YN-1-YLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINEdrugbank:description" experimental This compound belongs to the alpha amino acid amides. These are amide derivatives of alpha amino acids. Alpha Amino Acid Amides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Tertiary Carboxylic Acid Amides Pyrrolidines Tertiary Amines Polyamines Carboxylic Acids Enolates Monoalkylamines pyrrolidine tertiary carboxylic acid amide carboxamide group tertiary amine polyamine enolate carboxylic acid amine primary amine primary aliphatic amine organonitrogen compound logP 1.05 ALOGPS logS -3.1 ALOGPS Water Solubility 1.93e-01 g/l ALOGPS logP 1.17 ChemAxon IUPAC Name (2S)-2-amino-1-[(2S,5R)-2-(aminomethyl)-5-(prop-1-yn-1-yl)pyrrolidin-1-yl]-2-cyclopentylethan-1-one ChemAxon Traditional IUPAC Name (2S)-2-amino-1-[(2S,5R)-2-(aminomethyl)-5-(prop-1-yn-1-yl)pyrrolidin-1-yl]-2-cyclopentylethanone ChemAxon Molecular Weight 263.3785 ChemAxon Monoisotopic Weight 263.199762437 ChemAxon SMILES [H][C@](N)(C1CCCC1)C(=O)N1[C@]([H])(CN)CC[C@]1([H])C#CC ChemAxon Molecular Formula C15H25N3O ChemAxon InChI InChI=1S/C15H25N3O/c1-2-5-12-8-9-13(10-16)18(12)15(19)14(17)11-6-3-4-7-11/h11-14H,3-4,6-10,16-17H2,1H3/t12-,13-,14-/m0/s1 ChemAxon InChIKey InChIKey=RIKCMKYTGBHVSX-IHRRRGAJSA-N ChemAxon Polar Surface Area (PSA) 72.35 ChemAxon Refractivity 76.42 ChemAxon Polarizability 30.6 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest basic) 9.26 ChemAxon Physiological Charge 2 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon ChEBI 39637 PubChem Compound 11840904 PubChem Substance 99443351 ChemSpider 10015409 PDB 1AD BE0000854 Dipeptidyl peptidase 4 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dipeptidyl peptidase 4 Amino acid transport and metabolism Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Plays a role in T-cell activation DPP4 2q24.3 Cell membrane; single-pass type II membrane protein. Processed form:Secreted protein. Note=Also exis 7-28 5.92 88279.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3009 GenAtlas DPP4 GeneCards DPP4 GenBank Gene Database U13735 GenBank Protein Database 535388 UniProtKB P27487 UniProt Accession DPP4_HUMAN ADABP Adenosine deaminase complexing protein 2 Dipeptidyl peptidase IV DPP IV EC 3.4.14.5 T-cell activation antigen CD26 TP103 >Dipeptidyl peptidase 4 MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSL RWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNY VKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNL PSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYL CDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPS EPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISN EYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKY PLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGT FEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWE YYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP >2301 bp ATGAAGACACCGTGGAAGGTTCTTCTGGGACTGCTGGGTGCTGCTGCGCTTGTCACCATC ATCACCGTGCCCGTGGTTCTGCTGAACAAAGGCACAGATGATGCTACAGCTGACAGTCGC AAAACTTACACTCTAACTGATTACTTAAAAAATACTTATAGACTGAAGTTATACTCCTTA AGATGGATTTCAGATCATGAATATCTCTACAAACAAGAAAATAATATCTTGGTATTCAAT GCTGAATATGGAAACAGCTCAGTTTTCTTGGAGAACAGTACATTTGATGAGTTTGGACAT TCTATCAATGATTATTCAATATCTCCTGATGGGCAGTTTATTCTCTTAGAATACAACTAC GTGAAGCAATGGAGGCATTCCTACACAGCTTCATATGACATTTATGATTTAAATAAAAGG CAGCTGATTACAGAAGAGAGGATTCCAAACAACACACAGTGGGTCACATGGTCACCAGTG GGTCATAAATTGGCATATGTTTGGAACAATGACATTTATGTTAAAATTGAACCAAATTTA CCAAGTTACAGAATCACATGGACGGGGAAAGAAGATATAATATATAATGGAATAACTGAC TGGGTTTATGAAGAGGAAGTCTTCAGTGCCTACTCTGCTCTGTGGTGGTCTCCAAACGGC ACTTTTTTAGCATATGCCCAATTTAACGACACAGAAGTCCCACTTATTGAATACTCCTTC TACTCTGATGAGTCACTGCAGTACCCAAAGACTGTACGGGTTCCATATCCAAAGGCAGGA GCTGTGAATCCAACTGTAAAGTTCTTTGTTGTAAATACAGACTCTCTCAGCTCAGTCACC AATGCAACTTCCATACAAATCACTGCTCCTGCTTCTATGTTGATAGGGGATCACTACTTG TGTGATGTGACATGGGCAACACAAGAAAGAATTTCTTTGCAGTGGCTCAGGAGGATTCAG AACTATTCGGTCATGGATATTTGTGACTATGATGAATCCAGTGGAAGATGGAACTGCTTA GTGGCACGGCAACACATTGAAATGAGTACTACTGGCTGGGTTGGAAGATTTAGGCCTTCA GAACCTCATTTTACCCTTGATGGTAATAGCTTCTACAAGATCATCAGCAATGAAGAAGGT TACAGACACATTTGCTATTTCCAAATAGATAAAAAAGACTGCACATTTATTACAAAAGGC ACCTGGGAAGTCATCGGGATAGAAGCTCTAACCAGTGATTATCTATACTACATTAGTAAT GAATATAAAGGAATGCCAGGAGGAAGGAATCTTTATAAAATCCAACTTAGTGACTATACA AAAGTGACATGCCTCAGTTGTGAGCTGAATCCGGAAAGGTGTCAGTACTATTCTGTGTCA TTCAGTAAAGAGGCGAAGTATTATCAGCTGAGATGTTCCGGTCCTGGTCTGCCCCTCTAT ACTCTACACAGCAGCGTGAATGATAAAGGGCTGAGAGTCCTGGAAGACAATTCAGCTTTG GATAAAATGCTGCAGAATGTCCAGATGCCCTCCAAAAAACTGGACTTCATTATTTTGAAT GAAACAAAATTTTGGTATCAGATGATCTTGCCTCCTCATTTTGATAAATCCAAGAAATAT CCTCTACTATTAGATGTGTATGCAGGCCCATGTAGTCAAAAAGCAGACACTGTCTTCAGA CTGAACTGGGCCACTTACCTTGCAAGCACAGAAAACATTATAGTAGCTAGCTTTGATGGC AGAGGAAGTGGTTACCAAGGAGATAAGATCATGCATGCAATCAACAGAAGACTGGGAACA TTTGAAGTTGAAGATCAAATTGAAGCAGCCAGACAATTTTCAAAAATGGGATTTGTGGAC AACAAACGAATTGCAATTTGGGGCTGGTCATATGGAGGGTACGTAACCTCAATGGTCCTG GGATCGGGAAGTGGCGTGTTCAAGTGTGGAATAGCCGTGGCGCCTGTATCCCGGTGGGAG TACTATGACTCAGTGTACACAGAACGTTACATGGGTCTCCCAACTCCAGAAGACAACCTT GACCATTACAGAAATTCAACAGTCATGAGCAGAGCTGAAAATTTTAAACAAGTTGAGTAC CTCCTTATTCATGGAACAGCAGATGATAACGTTCACTTTCAGCAGTCAGCTCAGATCTCC AAAGCCCTGGTCGATGTTGGAGTGGATTTCCAGGCAATGTGGTATACTGATGAAGACCAT GGAATAGCTAGCAGCACAGCACACCAACATATATATACCCACATGAGCCACTTCATAAAA CAATGTTTCTCTTTACCTTAG PF00930 DPPIV_N PF00326 Peptidase_S9 component cell component membrane function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function serine-type peptidase activity function hydrolase activity function dipeptidyl-peptidase IV activity function prolyl oligopeptidase activity process protein metabolism process cellular protein metabolism process physiological process process proteolysis process metabolism process macromolecule metabolism "
drug:(1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-PROP-1-YN-1-YLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINErdfs:label"(1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-PROP-1-YN-1-YLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINE"
drug:(1S)-2-[(2S,5R)-2-(AMINOMETHYL)-5-PROP-1-YN-1-YLPYRROLIDIN-1-YL]-1-CYCLOPENTYL-2-OXOETHANAMINErdf:typedrugbank:drugs
drug:(1S)-2-oxo-1-phenyl-2-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]ethyl acetatedrugbank:description" experimental This compound belongs to the isoquinolones and derivatives. These are aromatic polycyclic compounds containing a ketone bearing isoquinoline moiety. Isoquinolones and Derivatives Organic Compounds Heterocyclic Compounds Isoquinolines and Derivatives Isoquinolones and Derivatives Anilides Benzyloxycarbonyls Benzylethers N-unsubstituted Carboxylic Acid Imides Secondary Carboxylic Acid Amides Carboxylic Acid Esters Ketones Enolates Carboxylic Acids Polyamines Dialkyl Ethers benzylether benzene carboxylic acid imide, n-unsubstituted carboxylic acid imide ketone carboxamide group secondary carboxylic acid amide carboxylic acid ester carboxylic acid derivative polyamine ether dialkyl ether carboxylic acid enolate amine organonitrogen compound carbonyl group logP 1.91 ALOGPS logS -4.5 ALOGPS Water Solubility 1.26e-02 g/l ALOGPS logP 2 ChemAxon IUPAC Name (S)-phenyl[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)carbamoyl]methyl acetate ChemAxon Traditional IUPAC Name (S)-phenyl[(1,3,4-trioxo-2H-isoquinolin-5-yl)carbamoyl]methyl acetate ChemAxon Molecular Weight 366.3243 ChemAxon Monoisotopic Weight 366.08518619 ChemAxon SMILES [H][C@@](OC(C)=O)(C(=O)NC1=CC=CC2=C1C(=O)C(=O)NC2=O)C1=CC=CC=C1 ChemAxon Molecular Formula C19H14N2O6 ChemAxon InChI InChI=1S/C19H14N2O6/c1-10(22)27-16(11-6-3-2-4-7-11)19(26)20-13-9-5-8-12-14(13)15(23)18(25)21-17(12)24/h2-9,16H,1H3,(H,20,26)(H,21,24,25)/t16-/m0/s1 ChemAxon InChIKey InChIKey=NKBDSMREMMRFSI-INIZCTEOSA-N ChemAxon Polar Surface Area (PSA) 118.64 ChemAxon Refractivity 94.33 ChemAxon Polarizability 34.93 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 5.51 ChemAxon pKa (strongest basic) -7 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 24883486 PubChem Substance 99444968 PDB RXB BE0001162 Caspase-3 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Caspase-3 Involved in caspase activity Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin CASP3 4q34 Cytoplasm None 6.51 31608.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1504 GenAtlas CASP3 GeneCards CASP3 GenBank Gene Database U13737 GenBank Protein Database 561666 UniProtKB P42574 UniProt Accession CASP3_HUMAN Apopain CASP-3 Caspase-3 precursor CPP-32 Cysteine protease CPP32 EC 3.4.22.56 SCA-1 SREBP cleavage activity 1 Yama protein >Caspase-3 precursor MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTG MTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLS HGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDD DMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVN RKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH >834 bp ATGGAGAACACTGAAAACTCAGTGGATTCAAAATCCATTAAAAATTTGGAACCAAAGATC ATACATGGAAGCGAATCAATGGACTCTGGAATATCCCTGGACAACAGTTATAAAATGGAT TATCCTGAGATGGGTTTATGTATAATAATTAATAATAAGAATTTTCATAAAAGCACTGGA ATGACATCTCGGTCTGGTACAGATGTCGATGCAGCAAACCTCAGGGAAACATTCAGAAAC TTGAAATATGAAGTCAGGAATAAAAATGATCTTACACGTGAAGAAATTGTGGAATTGATG CGTGATGTTTCTAAAGAAGATCACAGCAAAAGGAGCAGTTTTGTTTGTGTGCTTCTGAGC CATGGTGAAGAAGGAATAATTTTTGGAACAAATGGACCTGTTGACCTGAAAAAAATAACA AACTTTTTCAGAGGGGATCGTTGTAGAAGTCTAACTGGAAAACCCAAACTTTTCATTATT CAGGCCTGCCGTGGTACAGAACTGGACTGTGGCATTGAGACAGACAGTGGTGTTGATGAT GACATGGCGTGTCATAAAATACCAGTGGATGCCGACTTCTTGTATGCATACTCCACAGCA CCTGGTTATTATTCTTGGCGAAATTCAAAGGATGGCTCCTGGTTCATCCAGTCGCTTTGT GCCATGCTGAAACAGTATGCCGACAAGCTTGAATTTATGCACATTCTTACCCGGGTTAAC CGAAAGGTGGCAACAGAATTTGAGTCCTTTTCCTTTGACGCTACTTTTCATGCAAAGAAA CAGATTCCATGTATTGTTTCCATGCTCACAAAAGAACTCTATTTTTATCACTAA PF00656 Peptidase_C14 function peptidase activity function endopeptidase activity function cysteine-type endopeptidase activity function caspase activity function catalytic activity function hydrolase activity process protein metabolism process cellular protein metabolism process proteolysis process physiological process process metabolism process macromolecule metabolism "
drug:(1S)-2-oxo-1-phenyl-2-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]ethyl acetaterdfs:label"(1S)-2-oxo-1-phenyl-2-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]ethyl acetate"
drug:(1S)-2-oxo-1-phenyl-2-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]ethyl acetaterdf:typedrugbank:drugs
drug:(1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATEdrugbank:description" experimental This compound belongs to the phosphatidylglycerols. These are glycerophosphoglycerols in which two fatty acids are bonded to the 1-glycerol moiety through ester linkages. Phosphatidylglycerols Organic Compounds Lipids Glycerophospholipids Glycerophosphoglycerols Monosaccharide Phosphates Fatty Acid Esters Trioses Dicarboxylic Acids and Derivatives Organophosphate Esters Organic Phosphoric Acids Carboxylic Acid Esters 1,2-Diols Secondary Alcohols Enolates Ethers Primary Alcohols Polyamines monosaccharide phosphate fatty acid ester monosaccharide dicarboxylic acid derivative triose monosaccharide saccharide organic phosphate phosphoric acid ester 1,2-diol carboxylic acid ester secondary alcohol ether enolate polyamine carboxylic acid derivative primary alcohol alcohol logP 1.87 ALOGPS logS -2.5 ALOGPS Water Solubility 1.59e+00 g/l ALOGPS logP 2.49 ChemAxon IUPAC Name (2R)-1-{[(R)-((2S)-2,3-dihydroxypropyl phosphonato)]oxy}-3-(pentanoyloxy)propan-2-yl octanoate ChemAxon Traditional IUPAC Name (2R)-1-{[(R)-((2S)-2,3-dihydroxypropyl phosphonato)]oxy}-3-(pentanoyloxy)propan-2-yl octanoate ChemAxon Molecular Weight 455.4569 ChemAxon Monoisotopic Weight 455.204608884 ChemAxon SMILES [H][C@](O)(CO)CO[P@@]([O-])(=O)OC[C@@]([H])(COC(=O)CCCC)OC(=O)CCCCCCC ChemAxon Molecular Formula C19H36O10P ChemAxon InChI InChI=1S/C19H37O10P/c1-3-5-7-8-9-11-19(23)29-17(14-26-18(22)10-6-4-2)15-28-30(24,25)27-13-16(21)12-20/h16-17,20-21H,3-15H2,1-2H3,(H,24,25)/p-1/t16-,17+/m0/s1 ChemAxon InChIKey InChIKey=UQSXQYRZHMGKIE-DLBZAZTESA-M ChemAxon Polar Surface Area (PSA) 151.65 ChemAxon Refractivity 106.77 ChemAxon Polarizability 46.57 ChemAxon Rotatable Bond Count 21 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 1.89 ChemAxon pKa (strongest basic) -3 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5287637 PubChem Substance 99443820 ChemSpider 4449965 PDB AGA BE0003815 Respiratory nitrate reductase 1 alpha chain Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Respiratory nitrate reductase 1 alpha chain Energy production and conversion The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction narG Cell membrane None 6.47 140488.5 Escherichia coli (strain K12) GeneCards narG GenBank Gene Database X16181 GenBank Protein Database 42086 UniProtKB P09152 UniProt Accession NARG_ECOLI Nitrate reductase A subunit alpha Quinol-nitrate oxidoreductase subunit alpha >Respiratory nitrate reductase 1 alpha chain MSKFLDRFRYFKQKGETFADGHGQLLNTNRDWEDGYRQRWQHDKIVRSTHGVNCTGSCSW KIYVKNGLVTWETQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRLMK MWREAKALHSDPVEAWASIIEDADKAKSFKQARGRGGFVRSSWQEVNELIAASNVYTIKN YGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASPQTWGEQTDVPE SADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTVAVTPDYAEIAKLCDLWLAPKQ GTDAAMALAMGHVMLREFHLDNPSQYFTDYVRRYTDMPMLVMLEERDGYYAAGRMLRAAD LVDALGQENNPEWKTVAFNTNGEMVAPNGSIGFRWGEKGKWNLEQRDGKTGEETELQLSL LGSQDEIAEVGFPYFGGDGTEHFNKVELENVLLHKLPVKRLQLADGSTALVTTVYDLTLA NYGLERGLNDVNCATSYDDVKAYTPAWAEQITGVSRSQIIRIAREFADNADKTHGRSMII VGAGLNHWYHLDMNYRGLINMLIFCGCVGQSGGGWAHYVGQEKLRPQTGWQPLAFALDWQ RPARHMNSTSYFYNHSSQWRYETVTAEELLSPMADKSRYTGHLIDFNVRAERMGWLPSAP QLGTNPLTIAGEAEKAGMNPVDYTVKSLKEGSIRFAAEQPENGKNHPRNLFIWRSNLLGS SGKGHEFMLKYLLGTEHGIQGKDLGQQGGVKPEEVDWQDNGLEGKLDLVVTLDFRLSSTC LYSDIILPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWEAKSDWEIYKAIAKKFSEVCVG HLGKETDIVTLPIQHDSAAELAQPLDVKDWKKGECDLIPGKTAPHIMVVERDYPATYERF TSIGPLMEKIGNGGKGIAWNTQSEMDLLRKLNYTKAEGPAKGQPMLNTAIDAAEMILTLA PETNGQVAVKAWAALSEFTGRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEH VSYNAGYTNVHELIPWRTLSGRQQLYQDHQWMRDFGESLLVYRPPIDTRSVKEVIGQKSN GNQEKALNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVWLSEADAKDLGIADNDWIEVFN SNGALTARAVVSQRVPAGMTMMYHAQERIVNLPGSEITQQRGGIHNSVTRITPKPTHMIG GYAHLAYGFNYYGTVGSNRDEFVVVRKMKNIDWLDGEGNDQVQESVK >3744 bp ATGAGTAAATTCCTGGACCGGTTTCGCTACTTCAAACAGAAGGGTGAAACCTTTGCCGAT GGGCATGGCCAGCTTCTCAATACCAACCGTGACTGGGAGGATGGATATCGCCAGCGTTGG CAGCATGACAAAATCGTCCGCTCTACCCACGGGGTAAACTGCACCGGCTCCTGCAGCTGG AAAATCTACGTCAAAAACGGTCTGGTCACCTGGGAAACCCAGCAGACTGACTATCCGCGT ACCCGTCCGGATCTGCCAAACCATGAACCTCGCGGCTGCCCGCGCGGTGCCAGCTACTCC TGGTATCTTTACAGTGCCAACCGCCTGAAATACCCGATGATGCGCAAACGCCTGATGAAA ATGTGGCGTGAAGCGAAGGCGCTGCATAGCGATCCGGTTGAGGCATGGGCTTCTATCATT GAAGACGCCGATAAAGCGAAAAGCTTTAAGCAGGCGCGTGGACGCGGTGGATTTGTTCGT TCTTCCTGGCAGGAGGTGAACGAACTGATCGCCGCATCTAACGTTTACACCATCAAAAAC TACGGCCCGGACCGTGTTGCTGGTTTCTCGCCAATTCCGGCAATGTCGATGGTTTCTTAC GCATCGGGTGCACGCTATCTCTCGCTGATTGGCGGTACTTGCTTAAGCTTCTACGACTGG TACTGCGACTTGCCTCCTGCGTCTCCGCAAACCTGGGGCGAGCAAACTGACGTACCGGAA TCTGCTGACTGGTACAACTCCAGCTACATCATCGCCTGGGGGTCAAACGTGCCGCAGACG CGTACCCCGGATGCTCACTTCTTTACTGAAGTGCGTTACAAAGGGACCAAAACTGTTGCC GTCACACCAGACTACGCTGAAATCGCCAAACTGTGCGATCTGTGGCTGGCACCGAAACAG GGCACCGATGCGGCAATGGCGCTGGCGATGGGCCACGTAATGCTGCGTGAATTCCACCTC GACAACCCAAGCCAGTATTTCACCGACTATGTGCGTCGCTACACCGACATGCCGATGCTG GTGATGCTGGAAGAACGCGACGGTTACTACGCTGCAGGTCGTATGCTGCGCGCTGCTGAT CTGGTTGATGCGCTGGGCCAGGAAAACAATCCGGAATGGAAAACTGTCGCCTTTAATACC AATGGCGAAATGGTTGCGCCGAACGGTTCTATTGGCTTCCGCTGGGGCGAGAAGGGCAAA TGGAATCTTGAGCAGCGCGACGGCAAAACTGGCGAAGAAACCGAGCTGCAACTGAGCCTG CTGGGTAGCCAGGATGAGATCGCTGAGGTAGGCTTCCCGTACTTTGGTGGCGACGGCACG GAACACTTCAACAAAGTGGAACTGGAAAACGTGCTGCTGCACAAACTGCCGGTGAAACGC CTGCAACTGGCTGATGGCAGCACCGCCCTGGTGACCACCGTTTATGATCTGACGCTGGCA AACTACGGTCTGGAACGTGGCCTGAACGACGTTAACTGTGCAACCAGCTATGACGATGTG AAAGCTTATACCCCGGCCTGGGCCGAGCAGATTACCGGCGTTTCTCGCAGCCAGATTATT CGCATCGCCCGTGAATTTGCCGATAACGCTGATAAAACGCACGGTCGTTCGATGATTATC GTCGGTGCGGGGCTGAACCACTGGTATCACCTCGATATGAACTATCGTGGTCTGATCAAC ATGCTGATTTTCTGCGGCTGTGTCGGTCAGAGCGGGGGCGGCTGGGCGCACTATGTAGGT CAGGAAAAACTGCGTCCGCAAACCGGCTGGCAGCCGCTGGCGTTTGCCCTTGACTGGCAG CGTCCGGCGCGTCACATGAACAGCACTTCTTATTTCTATAACCACTCCAGCCAGTGGCGT TATGAAACCGTCACGGCGGAAGAGTTGCTGTCACCGATGGCGGACAAATCCCGCTATACC GGACACTTGATCGACTTTAACGTCCGTGCGGAACGCATGGGCTGGCTGCCGTCTGCACCG CAGTTAGGCACTAACCCGCTGACTATCGCTGGCGAAGCGGAAAAAGCCGGGATGAATCCG GTGGACTATACGGTGAAATCCCTGAAAGAGGGTTCCATCCGTTTTGCGGCAGAACAACCA GAAAACGGTAAAAACCACCCGCGCAACCTGTTCATCTGGCGTTCTAACCTGCTCGGTTCT TCCGGTAAAGGTCATGAGTTTATGCTCAAGTACCTGCTGGGGACGGAGCACGGTATCCAG GGTAAAGATCTGGGGCAACAGGGCGGCGTGAAGCCGGAAGAAGTGGACTGGCAGGACAAT GGTCTGGAAGGCAAGCTGGATCTGGTGGTTACGCTGGACTTCCGTCTGTCGAGCACCTGT CTCTATTCCGACATCATTTTGCCGACGGCGACCTGGTACGAAAAAGACGACATGAATACT TCGGATATGCATCCGTTTATTCACCCGCTGTCTGCGGCGGTCGATCCGGCCTGGGAAGCG AAAAGCGACTGGGAAATCTACAAAGCCATCGCGAAGAAATTCTCCGAAGTGTGCGTCGGC CATCTGGGTAAAGAAACCGACATCGTCACGCTGCCTATCCAGCATGACTCTGCCGCTGAA CTGGCGCAGCCGCTGGATGTGAAAGACTGGAAAAAAGGCGAGTGCGACCTGATCCCAGGT AAAACCGCGCCACACATTATGGTCGTAGAGCGCGATTATCCGGCGACTTACGAACGCTTT ACCTCTATCGGCCCGCTGATGGAGAAAATCGGTAATGGCGGTAAAGGGATTGCCTGGAAC ACCCAGAGCGAGATGGATCTGCTGCGTAAGCTCAACTACACCAAAGCGGAAGGTCCGGCG AAAGGCCAGCCGATGCTGAACACCGCAATTGATGCGGCAGAGATGATCCTGACACTGGCA CCGGAAACCAACGGTCAGGTAGCCGTGAAAGCCTGGGCTGCCCTGAGCGAATTTACCGGT CGTGACCATACGCATCTGGCGCTGAATAAAGAAGACGAGAAGATCCGCTTCCGCGATATT CAGGCACAGCCGCGCAAAATTATCTCCAGCCCGACCTGGTCTGGTCTGGAAGATGAACAC GTTTCTTACAACGCCGGTTACACCAACGTTCACGAGCTGATCCCATGGCGTACGCTCTCT GGTCGTCAGCAACTGTATCAGGATCACCAGTGGATGCGTGATTTCGGTGAAAGCCTGCTG GTTTATCGTCCGCCGATCGACACCCGTTCGGTGAAAGAAGTGATAGGCCAGAAATCCAAC GGCAACCAGGAAAAAGCGCTCAACTTCCTGACGCCGCACCAGAAGTGGGGTATCCACTCC ACCTACAGCGACAACCTGCTGATGCTGACTTTAGGTCGCGGTGGTCCGGTGGTCTGGTTG AGTGAAGCCGATGCCAAAGATCTGGGTATCGCCGATAACGACTGGATTGAAGTCTTCAAC AGCAACGGTGCTCTGACTGCCCGTGCGGTTGTCAGCCAGCGTGTTCCGGCAGGGATGACC ATGATGTACCACGCGCAGGAACGTATCGTTAACCTGCCTGGTTCGGAAATTACCCAACAG CGTGGTGGTATCCATAACTCGGTCACCCGTATCACGCCGAAACCGACGCATATGATCGGC GGCTATGCCCATCTGGCATACGGCTTTAACTACTATGGCACCGTAGGTTCTAACCGCGAT GAGTTTGTTGTAGTGCGTAAGATGAAGAACATTGACTGGTTAGATGGCGAAGGCAATGAC CAGGTACAGGAGAGCGTAAAATGA PF00384 Molybdopterin PF01568 Molydop_binding component unlocalized protein complex component nitrate reductase complex component protein complex function catalytic activity function oxidoreductase activity, acting on other nitrogenous compounds as donors function molybdenum ion binding function oxidoreductase activity function ion binding function nitrate reductase activity function cation binding function transition metal ion binding function binding process physiological process process nitrogen compound metabolism process metabolism process cellular metabolism process nitrate metabolism process generation of precursor metabolites and energy process electron transport BE0003816 Respiratory nitrate reductase 1 beta chain Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Respiratory nitrate reductase 1 beta chain Energy production and conversion The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit narH Cell membrane None 6.76 58065.9 Escherichia coli (strain K12) GeneCards narH GenBank Gene Database M20147 GenBank Protein Database 146919 UniProtKB P11349 UniProt Accession NARH_ECOLI Nitrate reductase A subunit beta Quinol-nitrate oxidoreductase subunit beta >Respiratory nitrate reductase 1 beta chain MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENQE KYKGGWIRKINGKLQPRMGNRAMLLGKIFANPHLPGIDDYYEPFDFDYQNLHTAPEGSKS QPIARPRSLITGERMAKIEKGPNWEDDLGGEFDKLAKDKNFDNIQKAMYSQFENTFMMYL PRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGK SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADAIERAASTENEKDLYQRQLDVF LDPNDPKVIEQAIKDGIPLSVIEAAQQSPVYKMAMEWKLALPLHPEYRTLPMVWYVPPLS PIQSAADAGELGSNGILPDVESLRIPVQYLANLLTAGDTKPVLRALKRMLAMRHYKRAET VDGKVDTRALEEVGLTEAQAQEMYRYLAIANYEDRFVVPSSHRELAREAFPEKNGCGFTF GDGCHGSDTKFNLFNSRRIDAIDVTSKTEPHP >711 bp GACCAGCAAAACGGAGCCGCATCCATGATCGAACTCGTGATTGTATCGCGTCTCCTTGAA TATCCGGATGCTGCCTTATGGCAGCATCAACAAGAGATGTTTGAGGCGATTGCCGCGTCG AAAAATCTGCCAAAAGAGGATGCCCATGCGCTGGGCATTTTCCTGCGCGATTTAACGACG ATGGATCCGCTCGATGCCCAGGCGCAGTACAGCGAACTGTTCGACCGTGGCCGCGCCACG TCACTGTTGCTGTTTGAACATGTGCACGGCGAATCCCGCGACCGCGGCCAGGCGATGGTG GACCTGCTGGCGCAGTACGAGCAGCACGGCTTGCAGTTAAACAGCCGCGAATTGCCGGAC CATCTGCCGCTGTATCTGGAGTACCTGGCGCAGCTGCCGCAAAGCGAAGCCGTGGAAGGT TTGAAAGATATCGCGCCGATTCTGGCATTGCTGAGCGCGCGTCTGCAACAGCGTGAAAGC CGTTATGCCGTGCTGTTTGATCTGCTGCTGAAACTGGCGAATACCGCTATCGACAGCGAC AAAGTGGCGGAAAAAATTGCCGACGAAGCGCGCGATGATACGCCGCAGGCGCTGGATGCT GTCTGGGAAGAAGAGCAGGTTAAATTCTTTGCTGACAAAGGCTGCGGTGATTCAGCAATC ACTGCGCATCAGCGTCGCTTTGCCGGTGCCGTCGCGCCGCAATATCTGAAT component protein complex component unlocalized protein complex component nitrate reductase complex function oxidoreductase activity function oxidoreductase activity, acting on other nitrogenous compounds as donors function nitrate reductase activity function catalytic activity process metabolism process nitrogen compound metabolism process nitrate metabolism process physiological process BE0003817 Respiratory nitrate reductase 1 gamma chain Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Respiratory nitrate reductase 1 gamma chain Energy production and conversion The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit narI Cell inner membrane 4-29 48-70 83-112 125-148 183-198 10.11 25497.2 Escherichia coli (strain K12) GeneCards narI GenBank Gene Database M20147 GenBank Protein Database 146919 UniProtKB P11350 UniProt Accession NARI_ECOLI Cytochrome B-NR Nitrate reductase A subunit gamma Quinol-nitrate oxidoreductase subunit gamma >Respiratory nitrate reductase 1 gamma chain MQFLNMFFFDIYPYIAGAVFLIGSWLRYDYGQYTWRAASSQMLDRKGMNLASNLFHIGIL GIFVGHFFGMLTPHWMYEAWLPIEVKQKMAMFAGGASGVLCLIGGVLLLKRRLFSPRVRA TTTGADILILSLLVIQCALGLLTIPFSAQHMDGSEMMKLVGWAQSVVTFHGGASQHLDGV AFIFRLHLVLGMTLFLLFPFSRLIHIWSVPVEYLTRKYQLVRARH >711 bp GACCAGCAAAACGGAGCCGCATCCATGATCGAACTCGTGATTGTATCGCGTCTCCTTGAA TATCCGGATGCTGCCTTATGGCAGCATCAACAAGAGATGTTTGAGGCGATTGCCGCGTCG AAAAATCTGCCAAAAGAGGATGCCCATGCGCTGGGCATTTTCCTGCGCGATTTAACGACG ATGGATCCGCTCGATGCCCAGGCGCAGTACAGCGAACTGTTCGACCGTGGCCGCGCCACG TCACTGTTGCTGTTTGAACATGTGCACGGCGAATCCCGCGACCGCGGCCAGGCGATGGTG GACCTGCTGGCGCAGTACGAGCAGCACGGCTTGCAGTTAAACAGCCGCGAATTGCCGGAC CATCTGCCGCTGTATCTGGAGTACCTGGCGCAGCTGCCGCAAAGCGAAGCCGTGGAAGGT TTGAAAGATATCGCGCCGATTCTGGCATTGCTGAGCGCGCGTCTGCAACAGCGTGAAAGC CGTTATGCCGTGCTGTTTGATCTGCTGCTGAAACTGGCGAATACCGCTATCGACAGCGAC AAAGTGGCGGAAAAAATTGCCGACGAAGCGCGCGATGATACGCCGCAGGCGCTGGATGCT GTCTGGGAAGAAGAGCAGGTTAAATTCTTTGCTGACAAAGGCTGCGGTGATTCAGCAATC ACTGCGCATCAGCGTCGCTTTGCCGGTGCCGTCGCGCCGCAATATCTGAAT PF02665 Nitrate_red_gam component protein complex component unlocalized protein complex component nitrate reductase complex function oxidoreductase activity, acting on other nitrogenous compounds as donors function nitrate reductase activity function catalytic activity function oxidoreductase activity process generation of precursor metabolites and energy process electron transport process physiological process process metabolism process cellular metabolism BE0003818 Aquaporin Z Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aquaporin Z Carbohydrate transport and metabolism Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity aqpZ Cell inner membrane 9-29 34-54 82-102 131-151 156-176 202-222 7.63 23702.6 Escherichia coli (strain K12) GeneCards aqpZ GenBank Gene Database U38664 GenBank Protein Database 1051283 UniProtKB P60844 UniProt Accession AQPZ_ECOLI Bacterial nodulin-like intrinsic protein >Aquaporin Z MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGG HFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNG YGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPV TNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRD PF00230 MIP component cell component intrinsic to membrane component integral to membrane component membrane function transporter activity process cellular physiological process process transport process physiological process "
drug:(1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATErdfs:label"(1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE"
drug:(1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATErdf:typedrugbank:drugs
drug:(1S)-MENTHYL HEXYL PHOSPHONATE GROUPdrugbank:description" experimental This compound belongs to the monocyclic monoterpenes. These are monoterpenes containing 1 ring in the isoprene chain. Monocyclic Monoterpenes Organic Compounds Lipids Prenol Lipids Monoterpenes Phosphonic Acid Esters Organic Phosphonic Acids Polyamines phosphonic acid ester phosphonic acid derivative phosphonic acid polyamine logP 4.34 ALOGPS logS -3.9 ALOGPS Water Solubility 3.84e-02 g/l ALOGPS logP 4.58 ChemAxon IUPAC Name hexyl({[(1S,2R,5S)-5-methyl-2-(propan-2-yl)cyclohexyl]oxy})phosphinic acid ChemAxon Traditional IUPAC Name hexyl[(1S,2R,5S)-2-isopropyl-5-methylcyclohexyl]oxyphosphinic acid ChemAxon Molecular Weight 304.4052 ChemAxon Monoisotopic Weight 304.216731434 ChemAxon SMILES [H][C@]1(C)CC[C@]([H])(C(C)C)[C@]([H])(C1)O[P@](O)(=O)CCCCCC ChemAxon Molecular Formula C16H33O3P ChemAxon InChI InChI=1S/C16H33O3P/c1-5-6-7-8-11-20(17,18)19-16-12-14(4)9-10-15(16)13(2)3/h13-16H,5-12H2,1-4H3,(H,17,18)/t14-,15+,16-/m0/s1 ChemAxon InChIKey InChIKey=WAVIZOVSJOXCKT-XHSDSOJGSA-N ChemAxon Polar Surface Area (PSA) 46.53 ChemAxon Refractivity 84.04 ChemAxon Polarizability 35.22 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 1.93 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 446981 PubChem Substance 99444672 ChemSpider 394198 PDB MPC BE0002180 Cholinesterase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cholinesterase Lipid transport and metabolism An acylcholine + H(2)O = choline + a carboxylate BCHE 3q26.1-q26.2 Cytoplasmic None 7.47 68419.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:983 GenAtlas BCHE GeneCards BCHE GenBank Gene Database M32391 GenBank Protein Database 1311630 UniProtKB P06276 UniProt Accession CHLE_HUMAN Acylcholine acylhydrolase Butyrylcholine esterase Choline esterase II Cholinesterase precursor EC 3.1.1.8 Pseudocholinesterase >Cholinesterase MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV GL >1809 bp ATGCATAGCAAAGTCACAATCATATGCATCAGATTTCTCTTTTGGTTTCTTTTGCTCTGC ATGCTTATTGGGAAGTCACATACTGAAGATGACATCATAATTGCAACAAAGAATGGAAAA GTCAGAGGGATGAACTTGACAGTTTTTGGTGGCACGGTAACAGCCTTTCTTGGAATTCCC TATGCACAGCCACCTCTTGGTAGACTTCGATTCAAAAAGCCACAGTCTCTGACCAAGTGG TCTGATATTTGGAATGCCACAAAATATGCAAATTCTTGCTGTCAGAACATAGATCAAAGT TTTCCAGGCTTCCATGGATCAGAGATGTGGAACCCAAACACTGACCTCAGTGAAGACTGT TTATATCTAAATGTATGGATTCCAGCACCTAAACCAAAAAATGCCACTGTATTGATATGG ATTTATGGTGGTGGTTTTCAAACTGGAACATCATCTTTACATGTTTATGATGGCAAGTTT CTGGCTCGGGTTGAAAGAGTTATTGTAGTGTCAATGAACTATAGGGTGGGTGCCCTAGGA TTCTTAGCTTTGCCAGGAAATCCTGAGGCTCCAGGGAACATGGGTTTATTTGATCAACAG TTGGCTCTTCAGTGGGTTCAAAAAAATATAGCAGCCTTTGGTGGAAATCCTAAAAGTGTA ACTCTCTTTGGAGAAAGTGCAGGAGCAGCTTCAGTTAGCCTGCATTTGCTTTCTCCTGGA AGCCATTCATTGTTCACCAGAGCCATTCTGCAAAGTGGATCCTTTAATGCTCCTTGGGCG GTAACATCTCTTTATGAAGCTAGGAACAGAACGTTGAACTTAGCTAAATTGACTGGTTGC TCTAGAGAGAATGAGACTGAAATAATCAAGTGTCTTAGAAATAAAGATCCCCAAGAAATT CTTCTGAATGAAGCATTTGTTGTCCCCTATGGGACTCCTTTGTCAGTAAACTTTGGTCCG ACCGTGGATGGTGATTTTCTCACTGACATGCCAGACATATTACTTGAACTTGGACAATTT AAAAAAACCCAGATTTTGGTGGGTGTTAATAAAGATGAAGGGACAGCTTTTTTAGTCTAT GGTGCTCCTGGCTTCAGCAAAGATAACAATAGTATCATAACTAGAAAAGAATTTCAGGAA GGTTTAAAAATATTTTTTCCAGGAGTGAGTGAGTTTGGAAAGGAATCCATCCTTTTTCAT TACACAGACTGGGTAGATGATCAGAGACCTGAAAACTACCGTGAGGCCTTGGGTGATGTT GTTGGGGATTATAATTTCATATGCCCTGCCTTGGAGTTCACCAAGAAGTTCTCAGAATGG GGAAATAATGCCTTTTTCTACTATTTTGAACACCGATCCTCCAAACTTCCGTGGCCAGAA TGGATGGGAGTGATGCATGGCTATGAAATTGAATTTGTCTTTGGTTTACCTCTGGAAAGA AGAGATAATTACACAAAAGCCGAGGAAATTTTGAGTAGATCCATAGTGAAACGTTGGGCA AATTTTGCAAAATATGGGAATCCAAATGAGACTCAGAACAATAGCACAAGCTGGCCTGTC TTCAAAAGCACTGAACAAAAATATCTAACCTTGAATACAGAGTCAACAAGAATAATGACG AAACTACGTGCTCAACAATGTCGATTCTGGACATCATTTTTTCCAAAAGTCTTGGAAATG ACAGGAAATATTGATGAAGCAGAATGGGAGTGGAAAGCAGGATTCCATCGCTGGAACAAT TACATGATGGACTGGAAAAATCAATTTAACGATTACACTAGCAAGAAAGAAAGTTGTGTG GGTCTCTAA PF00135 COesterase PF08674 AChE_tetra function hydrolase activity function hydrolase activity, acting on ester bonds function carboxylic ester hydrolase activity function cholinesterase activity function catalytic activity "
drug:(1S)-MENTHYL HEXYL PHOSPHONATE GROUPrdfs:label"(1S)-MENTHYL HEXYL PHOSPHONATE GROUP"
drug:(1S)-MENTHYL HEXYL PHOSPHONATE GROUPrdf:typedrugbank:drugs
drug:(1S,2R)-2-[(2,5-difluorophenyl)carbamoyl]cyclopropanecarboxylic aciddrugbank:description" experimental This compound belongs to the anilides. These are organic heterocyclic compounds derived from oxoacids RkE(=O)l(OH)m (l not 0) by replacing an OH group by the NHPh group or derivative formed by ring substitution. Anilides Organic Compounds Benzenoids Benzene and Substituted Derivatives Anilides Fluorobenzenes Aryl Fluorides Cyclopropanecarboxylic Acids Secondary Carboxylic Acid Amides Enolates Polyamines Carboxylic Acids Organofluorides fluorobenzene cyclopropanecarboxylic acid or derivative aryl halide cyclopropanecarboxylic acid aryl fluoride carboxamide group secondary carboxylic acid amide carboxylic acid derivative carboxylic acid enolate polyamine organofluoride amine organonitrogen compound organohalogen logP 1.22 ALOGPS logS -2.5 ALOGPS Water Solubility 7.28e-01 g/l ALOGPS logP 1.5 ChemAxon IUPAC Name (1S,2R)-2-[(2,5-difluorophenyl)carbamoyl]cyclopropane-1-carboxylic acid ChemAxon Traditional IUPAC Name (1S,2R)-2-[(2,5-difluorophenyl)carbamoyl]cyclopropane-1-carboxylic acid ChemAxon Molecular Weight 241.1909 ChemAxon Monoisotopic Weight 241.055049569 ChemAxon SMILES [H][C@@]1(C[C@@]1([H])C(=O)NC1=CC(F)=CC=C1F)C(O)=O ChemAxon Molecular Formula C11H9F2NO3 ChemAxon InChI InChI=1S/C11H9F2NO3/c12-5-1-2-8(13)9(3-5)14-10(15)6-4-7(6)11(16)17/h1-3,6-7H,4H2,(H,14,15)(H,16,17)/t6-,7+/m1/s1 ChemAxon InChIKey InChIKey=QTWGHTBKFVANGX-RQJHMYQMSA-N ChemAxon Polar Surface Area (PSA) 66.4 ChemAxon Refractivity 54.99 ChemAxon Polarizability 20.46 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 3.52 ChemAxon pKa (strongest basic) -4.5 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 7100107 PubChem Substance 99444279 ChemSpider 5448167 PDB G30 BE0002718 Beta-lactamase Escherichia coli # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-lactamase Involved in beta-lactamase activity blaCTX-M-9a Cytoplasmic None 9.38 30952.0 Escherichia coli GenBank Gene Database AF252621 UniProtKB Q9L5C8 UniProt Accession Q9L5C8_ECOLX Beta-lactamase Betalactamase CTX-M-9 CTX-M-9 beta-lactamase >Beta-lactamase CTX-M-9a MVTKRVQRMMFAAAACIPLLLGSAPLYAQTSAVQQKLAALEKSSGGRLGVALIDTADNTQ VLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTM TLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDP RDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTAGDKTGS GDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVLASAARIIAEGL >876 bp ATGGTGACAAAGAGAGTGCAACGGATGATGTTCGCGGCGGCGGCGTGCATTCCGCTGCTG CTGGGCAGCGCGCCGCTTTATGCGCAGACGAGTGCGGTGCAGCAAAAGCTGGCGGCGCTG GAGAAAAGCAGCGGAGGGCGGCTGGGCGTCGCGCTCATCGATACCGCAGATAATACGCAG GTGCTTTATCGCGGTGATGAACGCTTTCCAATGTGCAGTACCAGTAAAGTTATGGCGGCC GCGGCGGTGCTTAAGCAGAGTGAAACGCAAAAGCAGCTGCTTAATCAGCCTGTCGAGATC AAGCCTGCCGATCTGGTTAACTACAATCCGATTGCCGAAAAACACGTCAACGGCACAATG ACGCTGGCAGAGCTGAGCGCGGCCGCGTTGCAGTACAGCGACAATACCGCCATGAACAAA TTGATTGCCCAGCTCGGTGGCCCGGGAGGCGTGACGGCTTTTGCCCGCGCGATCGGCGAT GAGACGTTTCGTCTGGATCGCACTGAACCTACGCTGAATACCGCCATTCCCGGCGACCCG AGAGACACCACCACGCCGCGGGCGATGGCACAGACGTTGCGTCAGCTTACGCTGGGTCAT GCGCTGGGCGAAACCCAGCGGGCGCAGTTGGTGACGTGGCTCAAAGGCAATACGACCGGC GCAGCCAGCATTCGGGCCGGCTTACCGACGTCGTGGACTGCAGGTGATAAGACCGGCAGC GGCGACTACGGCACCACCAATGATATTGCGGTGATCTGGCCGCAGGGTCGTGCGCCGCTG GTTCTGGTGACCTATTTTACCCAGCCGCAACAGAACGCAGAGAGCCGCCGCGATGTGCTG GCTTCAGCGGCGAGAATCATCGCCGAAGGGCTGTAA PF00144 Beta-lactamase function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides function catalytic activity function beta-lactamase activity process metabolism process drug metabolism process cellular metabolism process antibiotic metabolism process antibiotic catabolism process beta-lactam antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process response to antibiotic process physiological process "
drug:(1S,2R)-2-[(2,5-difluorophenyl)carbamoyl]cyclopropanecarboxylic acidrdfs:label"(1S,2R)-2-[(2,5-difluorophenyl)carbamoyl]cyclopropanecarboxylic acid"
drug:(1S,2R)-2-[(2,5-difluorophenyl)carbamoyl]cyclopropanecarboxylic acidrdf:typedrugbank:drugs
drug:(1S,2R,3S,4R,5R)-2,3,4-trihydroxy-N-octyl-6-oxa-8-azabicyclo[3.2.1]octane-8-carbothioamidedrugbank:description" experimental This compound belongs to the oxepanes. These are compounds containing an oxepane ring, which is a a seven-member saturated aliphatic heterocycle with one oxygen and six carbon atoms. Oxepanes Organic Compounds Heterocyclic Compounds Oxepanes Piperidines Tertiary Amines 1,2-Diols Secondary Alcohols Organic Thiocarbonic Acid Derivatives Ethers Polyamines piperidine thiocarbonic acid derivative 1,2-diol tertiary amine polyol secondary alcohol ether polyamine amine alcohol organonitrogen compound logP 1.31 ALOGPS logS -2.6 ALOGPS Water Solubility 8.05e-01 g/l ALOGPS logP 1.4 ChemAxon IUPAC Name (1S,2R,3S,4R,5R)-2,3,4-trihydroxy-N-octyl-6-oxa-8-azabicyclo[3.2.1]octane-8-carbothioamide ChemAxon Traditional IUPAC Name (1S,2R,3S,4R,5R)-2,3,4-trihydroxy-N-octyl-6-oxa-8-azabicyclo[3.2.1]octane-8-carbothioamide ChemAxon Molecular Weight 332.459 ChemAxon Monoisotopic Weight 332.176978084 ChemAxon SMILES [H][C@@]12CO[C@@]([H])(N1C(=S)NCCCCCCCC)[C@]([H])(O)[C@@]([H])(O)[C@]2([H])O ChemAxon Molecular Formula C15H28N2O4S ChemAxon InChI InChI=1S/C15H28N2O4S/c1-2-3-4-5-6-7-8-16-15(22)17-10-9-21-14(17)13(20)12(19)11(10)18/h10-14,18-20H,2-9H2,1H3,(H,16,22)/t10-,11+,12-,13+,14+/m0/s1 ChemAxon InChIKey InChIKey=LFSNQOFOMJLHIW-MEBFFEOJSA-N ChemAxon Polar Surface Area (PSA) 85.19 ChemAxon Refractivity 87.5 ChemAxon Polarizability 36.35 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 12.49 ChemAxon pKa (strongest basic) -3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 24963032 PubChem Substance 99444731 PDB NCW BE0001810 Beta-glucosidase A Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-glucosidase A Carbohydrate transport and metabolism Hydrolysis of terminal, non-reducing beta-D- glucose residues with release of beta-D-glucose bglA Cytoplasmic None 5.64 51549.0 Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) GenBank Gene Database X74163 GenBank Protein Database 395291 UniProtKB Q08638 UniProt Accession BGLA_THEMA Beta-D- glucoside glucohydrolase Cellobiase EC 3.2.1.21 Gentiobiase >Beta-glucosidase A MNVKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGDVACDHYNR WKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYNRIIDTLLEKGITPFVTIY HWDLPFALQLKGGWANREIADWFAEYSRVLFENFGDRVKNWITLNEPWVVAIVGHLYGVH APGMRDIYVAFRAVHNLLRAHARAVKVFRETVKDGKIGIVFNNGYFEPASEKEEDIRAVR FMHQFNNYPLFLNPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLV KFDPDAPAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITENGAAFDDVV SEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDNFEWAEGYSKRFGIVYVD YSTQKRIVKDSGYWYSNVVKNNGLED >1341 bp ATGAACGTGAAAAAGTTCCCTGAAGGATTCCTCTGGGGTGTTGCAACAGCTTCCTACCAG ATCGAGGGTTCTCCCCTCGCAGACGGAGCTGGTATGTCTATCTGGCACACCTTCTCCCAT ACTCCTGGAAATGTAAAGAACGGTGACACGGGAGATGTGGCCTGCGACCACTACAACAGA TGGAAAGAGGACATTGAAATCATAGAGAAACTCGGAGTAAAGGCTTACAGATTTTCAATC AGCTGGCCAAGAATACTTCCGGAAGGAACAGGAAGGGTGAATCAGAAAGGACTGGATTTT TACAACAGGATCATAGACACCCTGCTGGAAAAAGGTATCACACCCTTTGTGACCATCTAT CACTGGGATCTTCCCTTCGCTCTTCAGCTGAAAGGAGGATGGGCGAACAGAGAAATAGCG GATTGGTTCGCAGAATACTCAAGGGTTCTCTTTGAAAATTTCGGTGATCGTGTGAAGAAC TGGATCACCTTGAACGAACCGTGGGTTGTTGCCATAGTGGGGCATCTGTACGGAGTCCAC GCTCCTGGAATGAGAGATATTTACGTGGCTTTCCGAGCTGTTCACAATCTCTTGAGGGCA CACGCCAGAGCGGTGAAAGTGTTCAGGGAAACCGTGAAAGATGGAAAGATCGGAATAGTT TTCAACAATGGATATTTCGAACCTGCGAGTGAAAAAGAAGAAGACATCAGAGCGGTGAGA TTCATGCATCAGTTCAACAACTATCCTCTCTTTCTCAATCCGATCTACAGAGGAGATTAC CCGGAGCTCGTTCTGGAATTTGCCAGAGAGTATCTACCGGAGAATTACAAAGATGACATG TCCGAGATACAGGAAAAGATCGACTTTGTTGGATTGAACTATTACTCCGGTCATTTGGTG AAGTTCGATCCAGATGCACCAGCTAAGGTCTCTTTCGTTGAAAGGGATCTTCCAAAAACA GCCATGGGATGGGAGATCGTTCCAGAAGGAATCTACTGGATCCTGAAGAAGGTGAAAGAA GAATACAACCCACCAGAGGTTTACATCACAGAGAATGGGGCTGCTTTTGACGACGTAGTT AGTGAAGATGGAAGAGTTCACGATCAAAACAGAATCGATTATTTGAAGGCCCACATTGGT CAGGCATGGAAGGCCATACAGGAGGGAGTGCCGCTTAAAGGTTACTTCGTCTGGTCGCTC CTCGACAATTTCGAATGGGCAGAGGGATATTCCAAGAGATTTGGTATTGTGTATGTAGAC TACAGCACTCAAAAACGCATCGTAAAAGACAGTGGGTACTGGTACTCGAATGTGGTTAAA AACAACGGTCTGGAAGACTGA PF00232 Glyco_hydro_1 function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity function hydrolase activity process carbohydrate metabolism process physiological process process metabolism process macromolecule metabolism "
drug:(1S,2R,3S,4R,5R)-2,3,4-trihydroxy-N-octyl-6-oxa-8-azabicyclo[3.2.1]octane-8-carbothioamiderdfs:label"(1S,2R,3S,4R,5R)-2,3,4-trihydroxy-N-octyl-6-oxa-8-azabicyclo[3.2.1]octane-8-carbothioamide"
drug:(1S,2R,3S,4R,5R)-2,3,4-trihydroxy-N-octyl-6-oxa-8-azabicyclo[3.2.1]octane-8-carbothioamiderdf:typedrugbank:drugs
drug:(1S,2R,3S,4R,5S)-8-AZABICYCLO[3.2.1]OCTANE-1,2,3,4-TETROLdrugbank:description" experimental This compound belongs to the cyclitols and derivatives. These are compounds containing a cycloalkane moiety with one hydroxyl group on each of three or more ring atoms. Cyclitols and Derivatives Organic Compounds Organooxygen Compounds Alcohols and Polyols Cyclic Alcohols and Derivatives Piperidines Pyrrolidines Secondary Alcohols 1,2-Aminoalcohols Hemiaminals 1,2-Diols Dialkylamines Polyamines piperidine pyrrolidine hemiaminal 1,2-diol 1,2-aminoalcohol secondary alcohol polyol secondary amine polyamine secondary aliphatic amine amine organonitrogen compound logP -1.8 ALOGPS logS 0.62 ALOGPS Water Solubility 7.33e+02 g/l ALOGPS logP -2.1 ChemAxon IUPAC Name (1R,2S,3R,4S,5R)-8-azabicyclo[3.2.1]octane-1,2,3,4-tetrol ChemAxon Traditional IUPAC Name (1R,2S,3R,4S,5R)-8-azabicyclo[3.2.1]octane-1,2,3,4-tetrol ChemAxon Molecular Weight 175.1824 ChemAxon Monoisotopic Weight 175.084457909 ChemAxon SMILES O[C@H]1[C@H]2CC[C@](O)(N2)[C@@H](O)[C@@H]1O ChemAxon Molecular Formula C7H13NO4 ChemAxon InChI InChI=1S/C7H13NO4/c9-4-3-1-2-7(12,8-3)6(11)5(4)10/h3-6,8-12H,1-2H2/t3-,4+,5-,6+,7-/m1/s1 ChemAxon InChIKey InChIKey=FXFBVZOJVHCEDO-IBISWUOJSA-N ChemAxon Polar Surface Area (PSA) 92.95 ChemAxon Refractivity 39.07 ChemAxon Polarizability 16.66 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 12.13 ChemAxon pKa (strongest basic) 8.57 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 124434 PubChem Substance 46505662 PDB CGB BE0001810 Beta-glucosidase A Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) unknown Beta-glucosidase A Carbohydrate transport and metabolism Hydrolysis of terminal, non-reducing beta-D- glucose residues with release of beta-D-glucose bglA Cytoplasmic None 5.64 51549.0 Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) GenBank Gene Database X74163 GenBank Protein Database 395291 UniProtKB Q08638 UniProt Accession BGLA_THEMA Beta-D- glucoside glucohydrolase Cellobiase EC 3.2.1.21 Gentiobiase >Beta-glucosidase A MNVKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGDVACDHYNR WKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYNRIIDTLLEKGITPFVTIY HWDLPFALQLKGGWANREIADWFAEYSRVLFENFGDRVKNWITLNEPWVVAIVGHLYGVH APGMRDIYVAFRAVHNLLRAHARAVKVFRETVKDGKIGIVFNNGYFEPASEKEEDIRAVR FMHQFNNYPLFLNPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLV KFDPDAPAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITENGAAFDDVV SEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDNFEWAEGYSKRFGIVYVD YSTQKRIVKDSGYWYSNVVKNNGLED >1341 bp ATGAACGTGAAAAAGTTCCCTGAAGGATTCCTCTGGGGTGTTGCAACAGCTTCCTACCAG ATCGAGGGTTCTCCCCTCGCAGACGGAGCTGGTATGTCTATCTGGCACACCTTCTCCCAT ACTCCTGGAAATGTAAAGAACGGTGACACGGGAGATGTGGCCTGCGACCACTACAACAGA TGGAAAGAGGACATTGAAATCATAGAGAAACTCGGAGTAAAGGCTTACAGATTTTCAATC AGCTGGCCAAGAATACTTCCGGAAGGAACAGGAAGGGTGAATCAGAAAGGACTGGATTTT TACAACAGGATCATAGACACCCTGCTGGAAAAAGGTATCACACCCTTTGTGACCATCTAT CACTGGGATCTTCCCTTCGCTCTTCAGCTGAAAGGAGGATGGGCGAACAGAGAAATAGCG GATTGGTTCGCAGAATACTCAAGGGTTCTCTTTGAAAATTTCGGTGATCGTGTGAAGAAC TGGATCACCTTGAACGAACCGTGGGTTGTTGCCATAGTGGGGCATCTGTACGGAGTCCAC GCTCCTGGAATGAGAGATATTTACGTGGCTTTCCGAGCTGTTCACAATCTCTTGAGGGCA CACGCCAGAGCGGTGAAAGTGTTCAGGGAAACCGTGAAAGATGGAAAGATCGGAATAGTT TTCAACAATGGATATTTCGAACCTGCGAGTGAAAAAGAAGAAGACATCAGAGCGGTGAGA TTCATGCATCAGTTCAACAACTATCCTCTCTTTCTCAATCCGATCTACAGAGGAGATTAC CCGGAGCTCGTTCTGGAATTTGCCAGAGAGTATCTACCGGAGAATTACAAAGATGACATG TCCGAGATACAGGAAAAGATCGACTTTGTTGGATTGAACTATTACTCCGGTCATTTGGTG AAGTTCGATCCAGATGCACCAGCTAAGGTCTCTTTCGTTGAAAGGGATCTTCCAAAAACA GCCATGGGATGGGAGATCGTTCCAGAAGGAATCTACTGGATCCTGAAGAAGGTGAAAGAA GAATACAACCCACCAGAGGTTTACATCACAGAGAATGGGGCTGCTTTTGACGACGTAGTT AGTGAAGATGGAAGAGTTCACGATCAAAACAGAATCGATTATTTGAAGGCCCACATTGGT CAGGCATGGAAGGCCATACAGGAGGGAGTGCCGCTTAAAGGTTACTTCGTCTGGTCGCTC CTCGACAATTTCGAATGGGCAGAGGGATATTCCAAGAGATTTGGTATTGTGTATGTAGAC TACAGCACTCAAAAACGCATCGTAAAAGACAGTGGGTACTGGTACTCGAATGTGGTTAAA AACAACGGTCTGGAAGACTGA PF00232 Glyco_hydro_1 function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process "
drug:(1S,2R,3S,4R,5S)-8-AZABICYCLO[3.2.1]OCTANE-1,2,3,4-TETROLrdfs:label"(1S,2R,3S,4R,5S)-8-AZABICYCLO[3.2.1]OCTANE-1,2,3,4-TETROL"
drug:(1S,2R,3S,4R,5S)-8-AZABICYCLO[3.2.1]OCTANE-1,2,3,4-TETROLrdf:typedrugbank:drugs
drug:(1S,2R,5S)-5-[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]-2-(2,4,5-TRIFLUOROPHENYL)CYCLOHEXANAMINEdrugbank:description" experimental This compound belongs to the triazolopyrazines. These are compounds containing a triazole ring fused to a pyrazine ring. Triazolopyrazines Organic Compounds Heterocyclic Compounds Triazolopyrazines Fluorobenzenes Pyrazines Aryl Fluorides Triazoles Tertiary Amines Polyamines Organofluorides Monoalkylamines Alkyl Fluorides fluorobenzene aryl halide aryl fluoride pyrazine benzene 1,2,4-triazole triazole azole tertiary amine polyamine organohalogen organofluoride primary amine amine primary aliphatic amine alkyl halide alkyl fluoride organonitrogen compound logP 2.91 ALOGPS logS -4.2 ALOGPS Water Solubility 2.74e-02 g/l ALOGPS logP 2.38 ChemAxon IUPAC Name (1S,2R,5S)-5-[3-(trifluoromethyl)-5H,6H,7H,8H-[1,2,4]triazolo[4,3-a]pyrazin-7-yl]-2-(2,4,5-trifluorophenyl)cyclohexan-1-amine ChemAxon Traditional IUPAC Name (1S,2R,5S)-5-[3-(trifluoromethyl)-5H,6H,8H-[1,2,4]triazolo[4,3-a]pyrazin-7-yl]-2-(2,4,5-trifluorophenyl)cyclohexan-1-amine ChemAxon Molecular Weight 419.3674 ChemAxon Monoisotopic Weight 419.154464863 ChemAxon SMILES [H][C@@]1(CC[C@]([H])(C2=C(F)C=C(F)C(F)=C2)[C@@]([H])(N)C1)N1CCN2C(C1)=NN=C2C(F)(F)F ChemAxon Molecular Formula C18H19F6N5 ChemAxon InChI InChI=1S/C18H19F6N5/c19-12-7-14(21)13(20)6-11(12)10-2-1-9(5-15(10)25)28-3-4-29-16(8-28)26-27-17(29)18(22,23)24/h6-7,9-10,15H,1-5,8,25H2/t9-,10+,15-/m0/s1 ChemAxon InChIKey InChIKey=CNKRZILQBKJWDS-WMFXKJRFSA-N ChemAxon Polar Surface Area (PSA) 59.97 ChemAxon Refractivity 94.99 ChemAxon Polarizability 37.24 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 9.87 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11538992 PubChem Substance 99443543 ChemSpider 9713772 PDB 417 BE0000854 Dipeptidyl peptidase 4 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dipeptidyl peptidase 4 Amino acid transport and metabolism Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Plays a role in T-cell activation DPP4 2q24.3 Cell membrane; single-pass type II membrane protein. Processed form:Secreted protein. Note=Also exis 7-28 5.92 88279.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3009 GenAtlas DPP4 GeneCards DPP4 GenBank Gene Database U13735 GenBank Protein Database 535388 UniProtKB P27487 UniProt Accession DPP4_HUMAN ADABP Adenosine deaminase complexing protein 2 Dipeptidyl peptidase IV DPP IV EC 3.4.14.5 T-cell activation antigen CD26 TP103 >Dipeptidyl peptidase 4 MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSL RWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNY VKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNL PSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYL CDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPS EPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISN EYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKY PLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGT FEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWE YYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP >2301 bp ATGAAGACACCGTGGAAGGTTCTTCTGGGACTGCTGGGTGCTGCTGCGCTTGTCACCATC ATCACCGTGCCCGTGGTTCTGCTGAACAAAGGCACAGATGATGCTACAGCTGACAGTCGC AAAACTTACACTCTAACTGATTACTTAAAAAATACTTATAGACTGAAGTTATACTCCTTA AGATGGATTTCAGATCATGAATATCTCTACAAACAAGAAAATAATATCTTGGTATTCAAT GCTGAATATGGAAACAGCTCAGTTTTCTTGGAGAACAGTACATTTGATGAGTTTGGACAT TCTATCAATGATTATTCAATATCTCCTGATGGGCAGTTTATTCTCTTAGAATACAACTAC GTGAAGCAATGGAGGCATTCCTACACAGCTTCATATGACATTTATGATTTAAATAAAAGG CAGCTGATTACAGAAGAGAGGATTCCAAACAACACACAGTGGGTCACATGGTCACCAGTG GGTCATAAATTGGCATATGTTTGGAACAATGACATTTATGTTAAAATTGAACCAAATTTA CCAAGTTACAGAATCACATGGACGGGGAAAGAAGATATAATATATAATGGAATAACTGAC TGGGTTTATGAAGAGGAAGTCTTCAGTGCCTACTCTGCTCTGTGGTGGTCTCCAAACGGC ACTTTTTTAGCATATGCCCAATTTAACGACACAGAAGTCCCACTTATTGAATACTCCTTC TACTCTGATGAGTCACTGCAGTACCCAAAGACTGTACGGGTTCCATATCCAAAGGCAGGA GCTGTGAATCCAACTGTAAAGTTCTTTGTTGTAAATACAGACTCTCTCAGCTCAGTCACC AATGCAACTTCCATACAAATCACTGCTCCTGCTTCTATGTTGATAGGGGATCACTACTTG TGTGATGTGACATGGGCAACACAAGAAAGAATTTCTTTGCAGTGGCTCAGGAGGATTCAG AACTATTCGGTCATGGATATTTGTGACTATGATGAATCCAGTGGAAGATGGAACTGCTTA GTGGCACGGCAACACATTGAAATGAGTACTACTGGCTGGGTTGGAAGATTTAGGCCTTCA GAACCTCATTTTACCCTTGATGGTAATAGCTTCTACAAGATCATCAGCAATGAAGAAGGT TACAGACACATTTGCTATTTCCAAATAGATAAAAAAGACTGCACATTTATTACAAAAGGC ACCTGGGAAGTCATCGGGATAGAAGCTCTAACCAGTGATTATCTATACTACATTAGTAAT GAATATAAAGGAATGCCAGGAGGAAGGAATCTTTATAAAATCCAACTTAGTGACTATACA AAAGTGACATGCCTCAGTTGTGAGCTGAATCCGGAAAGGTGTCAGTACTATTCTGTGTCA TTCAGTAAAGAGGCGAAGTATTATCAGCTGAGATGTTCCGGTCCTGGTCTGCCCCTCTAT ACTCTACACAGCAGCGTGAATGATAAAGGGCTGAGAGTCCTGGAAGACAATTCAGCTTTG GATAAAATGCTGCAGAATGTCCAGATGCCCTCCAAAAAACTGGACTTCATTATTTTGAAT GAAACAAAATTTTGGTATCAGATGATCTTGCCTCCTCATTTTGATAAATCCAAGAAATAT CCTCTACTATTAGATGTGTATGCAGGCCCATGTAGTCAAAAAGCAGACACTGTCTTCAGA CTGAACTGGGCCACTTACCTTGCAAGCACAGAAAACATTATAGTAGCTAGCTTTGATGGC AGAGGAAGTGGTTACCAAGGAGATAAGATCATGCATGCAATCAACAGAAGACTGGGAACA TTTGAAGTTGAAGATCAAATTGAAGCAGCCAGACAATTTTCAAAAATGGGATTTGTGGAC AACAAACGAATTGCAATTTGGGGCTGGTCATATGGAGGGTACGTAACCTCAATGGTCCTG GGATCGGGAAGTGGCGTGTTCAAGTGTGGAATAGCCGTGGCGCCTGTATCCCGGTGGGAG TACTATGACTCAGTGTACACAGAACGTTACATGGGTCTCCCAACTCCAGAAGACAACCTT GACCATTACAGAAATTCAACAGTCATGAGCAGAGCTGAAAATTTTAAACAAGTTGAGTAC CTCCTTATTCATGGAACAGCAGATGATAACGTTCACTTTCAGCAGTCAGCTCAGATCTCC AAAGCCCTGGTCGATGTTGGAGTGGATTTCCAGGCAATGTGGTATACTGATGAAGACCAT GGAATAGCTAGCAGCACAGCACACCAACATATATATACCCACATGAGCCACTTCATAAAA CAATGTTTCTCTTTACCTTAG PF00930 DPPIV_N PF00326 Peptidase_S9 component cell component membrane function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function serine-type peptidase activity function hydrolase activity function dipeptidyl-peptidase IV activity function prolyl oligopeptidase activity process protein metabolism process cellular protein metabolism process physiological process process proteolysis process metabolism process macromolecule metabolism "
drug:(1S,2R,5S)-5-[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]-2-(2,4,5-TRIFLUOROPHENYL)CYCLOHEXANAMINErdfs:label"(1S,2R,5S)-5-[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]-2-(2,4,5-TRIFLUOROPHENYL)CYCLOHEXANAMINE"
drug:(1S,2R,5S)-5-[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]-2-(2,4,5-TRIFLUOROPHENYL)CYCLOHEXANAMINErdf:typedrugbank:drugs
drug:(1S,2S,3R,4S,5S)-2,3,4-TRIHYDROXY-5-(HYDROXYMETHYL)CYCLOHEXYL (1E)-2-PHENYL-N-(SULFOOXY)ETHANIMIDOTHIOATEdrugbank:description" experimental This compound belongs to the cyclitols and derivatives. These are compounds containing a cycloalkane moiety with one hydroxyl group on each of three or more ring atoms. Cyclitols and Derivatives Organic Compounds Organooxygen Compounds Alcohols and Polyols Cyclic Alcohols and Derivatives Cyclohexanols Benzene and Substituted Derivatives Organic Sulfuric Acids and Derivatives 1,2-Diols Imidothioic Acids and Derivatives Polyamines Primary Alcohols cyclohexanol benzene sulfuric acid derivative polyol 1,2-diol secondary alcohol imidothioic acid or derivative polyamine primary alcohol organonitrogen compound logP -1 ALOGPS logS -2.3 ALOGPS Water Solubility 1.90e+00 g/l ALOGPS logP -2 ChemAxon IUPAC Name {[(Z)-(2-phenyl-1-{[(1R,2R,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]sulfanyl}ethylidene)amino]oxy}sulfonic acid ChemAxon Traditional IUPAC Name [(Z)-(2-phenyl-1-{[(1R,2R,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]sulfanyl}ethylidene)amino]oxysulfonic acid ChemAxon Molecular Weight 407.459 ChemAxon Monoisotopic Weight 407.070858033 ChemAxon SMILES OC[C@H]1C[C@@H](S\C(=N/OS(O)(=O)=O)CC2=CC=CC=C2)[C@H](O)[C@@H](O)[C@@H]1O ChemAxon Molecular Formula C15H21NO8S2 ChemAxon InChI InChI=1S/C15H21NO8S2/c17-8-10-7-11(14(19)15(20)13(10)18)25-12(16-24-26(21,22)23)6-9-4-2-1-3-5-9/h1-5,10-11,13-15,17-20H,6-8H2,(H,21,22,23)/b16-12-/t10-,11-,13-,14+,15+/m1/s1 ChemAxon InChIKey InChIKey=LZDZCEOFJWRJIA-GGASBGQWSA-N ChemAxon Polar Surface Area (PSA) 156.88 ChemAxon Refractivity 93.82 ChemAxon Polarizability 38.02 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 8 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) -3.4 ChemAxon pKa (strongest basic) 0.072 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 9600408 PubChem Substance 46507070 PDB CGT BE0004338 Lactase-phlorizin hydrolase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Lactase-phlorizin hydrolase Carbohydrate transport and metabolism LPH splits lactose in the small intestine LCT 2q21 Apical cell membrane 1883-1901 6.3 218570.8 Human HUGO Gene Nomenclature Committee (HGNC) GNC:6530 GeneCards LCT GenBank Gene Database X07994 GenBank Protein Database 34400 UniProtKB P09848 UniProt Accession LPH_HUMAN Lactase Lactase-glycosylceramidase Phlorizin hydrolase >Lactase-phlorizin hydrolase MELSWHVVFIALLSFSCWGSDWESDRNFISTAGPLTNDLLHNLSGLLGDQSSNFVAGDKD MYVCHQPLPTFLPEYFSSLHASQITHYKVFLSWAQLLPAGSTQNPDEKTVQCYRRLLKAL KTARLQPMVILHHQTLPASTLRRTEAFADLFADYATFAFHSFGDLVGIWFTFSDLEEVIK ELPHQESRASQLQTLSDAHRKAYEIYHESYAFQGGKLSVVLRAEDIPELLLEPPISALAQ DTVDFLSLDLSYECQNEASLRQKLSKLQTIEPKVKVFIFNLKLPDCPSTMKNPASLLFSL FEAINKDQVLTIGFDINEFLSCSSSSKKSMSCSLTGSLALQPDQQQDHETTDSSPASAYQ RVWEAFANQSRAERDAFLQDTFPEGFLWGASTGAFNVEGGWAEGGRGVSIWDPRRPLNTT EGQATLEVASDSYHKVASDVALLCGLRAQVYKFSISWSRIFPMGHGSSPSLPGVAYYNKL IDRLQDAGIEPMATLFHWDLPQALQDHGGWQNESVVDAFLDYAAFCFSTFGDRVKLWVTF HEPWVMSYAGYGTGQHPPGISDPGVASFKVAHLVLKAHARTWHHYNSHHRPQQQGHVGIV LNSDWAEPLSPERPEDLRASERFLHFMLGWFAHPVFVDGDYPATLRTQIQQMNRQCSHPV AQLPEFTEAEKQLLKGSADFLGLSHYTSRLISNAPQNTCIPSYDTIGGFSQHVNHVWPQT SSSWIRVVPWGIRRLLQFVSLEYTRGKVPIYLAGNGMPIGESENLFDDSLRVDYFNQYIN EVLKAIKEDSVDVRSYIARSLIDGFEGPSGYSQRFGLHHVNFSDSSKSRTPRKSAYFFTS IIEKNGFLTKGAKRLLPPNTVNLPSKVRAFTFPSEVPSKAKVVWEKFSSQPKFERDLFYH GTFRDDFLWGVSSSAYQIEGAWDADGKGPSIWDNFTHTPGSNVKDNATGDIACDSYHQLD ADLNMLRALKVKAYRFSISWSRIFPTGRNSSINSHGVDYYNRLINGLVASNIFPMVTLFH WDLPQALQDIGGWENPALIDLFDSYADFCFQTFGDRVKFWMTFNEPMYLAWLGYGSGEFP PGVKDPGWAPYRIAHAVIKAHARVYHTYDEKYRQEQKGVISLSLSTHWAEPKSPGVPRDV EAADRMLQFSLGWFAHPIFRNGDYPDTMKWKVGNRSELQHLATSRLPSFTEEEKRFIRAT ADVFCLNTYYSRIVQHKTPRLNPPSYEDDQEMAEEEDPSWPSTAMNRAAPWGTRRLLNWI KEEYGDIPIYITENGVGLTNPNTEDTDRIFYHKTYINEALKAYRLDGIDLRGYVAWSLMD NFEWLNGYTVKFGLYHVDFNNTNRPRTARASARYYTEVITNNGMPLAREDEFLYGRFPEG FIWSAASAAYQIEGAWRADGKGLSIWDTFSHTPLRVENDAIGDVACDSYHKIAEDLVTLQ NLGVSHYRFSISWSRILPDGTTRYINEAGLNYYVRLIDTLLAASIQPQVTIYHWDLPQTL QDVGGWENETIVQRFKEYADVLFQRLGDKVKFWITLNEPFVIAYQGYGYGTAAPGVSNRP GTAPYIVGHNLIKAHAEAWHLYNDVYRASQGGVISITISSDWAEPRDPSNQEDVEAARRY VQFMGGWFAHPIFKNGDYNEVMKTRIRDRSLAAGLNKSRLPEFTESEKRRINGTYDFFGF NHYTTVLAYNLNYATAISSFDADRGVASIADRSWPDSGSFWLKMTPFGFRRILNWLKEEY NDPPIYVTENGVSQREETDLNDTARIYYLRTYINEALKAVQDKVDLRGYTVWSAMDNFEW ATGFSERFGLHFVNYSDPSLPRIPKASAKFYASVVRCNGFPDPATGPHACLHQPDAGPTI SPVRQEEVQFLGLMLGTTEAQTALYVLFSLVLLGVCGLAFLSYKYCKRSKQGKTQRSQQE LSPVSSF >5784 bp ATGGAGCTGTCTTGGCATGTAGTCTTTATTGCCCTGCTAAGTTTTTCATGCTGGGGGTCA GACTGGGAGTCTGATAGAAATTTCATTTCCACCGCTGGTCCTCTAACCAATGACTTGCTG CACAACCTGAGTGGTCTCCTGGGAGACCAGAGTTCTAACTTTGTAGCAGGGGACAAAGAC ATGTATGTTTGTCACCAGCCACTGCCCACTTTCCTGCCAGAATACTTCAGCAGTCTCCAT GCCAGTCAGATCACCCATTATAAGGTATTTCTGTCATGGGCACAGCTCCTCCCAGCAGGA AGCACCCAGAATCCAGACGAGAAAACAGTGCAGTGCTACCGGCGACTCCTCAAGGCCCTC AAGACTGCACGGCTTCAGCCCATGGTCATCCTGCACCACCAGACCCTCCCTGCCAGCACC CTCCGGAGAACCGAAGCCTTTGCTGACCTCTTCGCCGACTATGCCACATTCGCCTTCCAC TCCTTCGGGGACCTAGTTGGGATCTGGTTCACCTTCAGTGACTTGGAGGAAGTGATCAAG GAGCTTCCCCACCAGGAATCAAGAGCGTCACAACTCCAGACCCTCAGTGATGCCCACAGA AAAGCCTATGAGATTTACCACGAAAGCTATGCTTTTCAGGGCGGAAAACTCTCTGTTGTC CTGCGAGCTGAAGATATCCCGGAGCTCCTGCTAGAACCACCCATATCTGCGCTTGCCCAG GACACGGTCGATTTCCTCTCTCTTGATTTGTCTTATGAATGCCAAAATGAGGCAAGTCTG CGGCAGAAGCTGAGTAAATTGCAGACCATTGAGCCAAAAGTGAAAGTTTTCATCTTCAAC CTAAAACTCCCAGACTGCCCCTCCACCATGAAGAACCCAGCCAGTCTGCTCTTCAGCCTT TTTGAAGCCATAAATAAAGACCAAGTGCTCACCATTGGGTTTGATATTAATGAGTTTCTG AGTTGTTCATCAAGTTCCAAGAAAAGCATGTCTTGTTCTCTGACTGGCAGCCTGGCCCTT CAGCCTGACCAGCAGCAGGACCACGAGACCACGGACTCCTCTCCTGCCTCTGCCTATCAG AGAGTCTGGGAAGCATTTGCCAATCAGTCCAGAGCGGAAAGGGATGCCTTCCTGCAGGAT ACTTTCCCTGAAGGCTTCCTCTGGGGTGCCTCCACAGGAGCCTTTAACGTGGAAGGAGGC TGGGCCGAGGGTGGGAGAGGGGTGAGCATCTGGGATCCACGCAGGCCCCTGAACACCACT GAGGGCCAAGCGACGCTGGAGGTGGCCAGCGACAGTTACCACAAGGTAGCCTCTGACGTC GCCCTGCTTTGCGGCCTCCGGGCTCAGGTGTACAAGTTCTCCATCTCCTGGTCCCGGATC TTCCCCATGGGGCACGGGAGCAGCCCCAGCCTCCCAGGCGTTGCCTACTACAACAAGCTG ATTGACAGGCTACAGGATGCGGGCATCGAGCCCATGGCCACGCTGTTCCACTGGGACCTG CCTCAGGCCCTGCAGGATCATGGTGGATGGCAGAATGAGAGCGTGGTGGATGCCTTCCTG GACTATGCGGCCTTCTGCTTCTCCACATTTGGGGACCGTGTGAAGCTGTGGGTGACCTTC CATGAGCCGTGGGTGATGAGCTACGCAGGCTATGGCACCGGCCAGCACCCTCCCGGCATC TCTGACCCAGGAGTGGCCTCTTTTAAGGTGGCTCACTTGGTCCTCAAGGCTCATGCCAGA ACTTGGCACCACTACAACAGCCATCATCGCCCACAGCAGCAGGGGCACGTGGGCATTGTG CTGAACTCAGACTGGGCAGAACCCCTGTCTCCAGAGAGGCCTGAGGACCTGAGAGCCTCT GAGCGCTTCTTGCACTTCATGCTGGGCTGGTTTGCACACCCCGTCTTTGTGGATGGAGAC TACCCAGCCACCCTGAGGACCCAGATCCAACAGATGAACAGACAGTGCTCCCATCCTGTG GCTCAACTCCCCGAGTTCACAGAGGCAGAGAAGCAGCTCCTGAAAGGCTCTGCTGATTTT CTGGGTCTGTCGCATTACACCTCCCGCCTCATCAGCAACGCCCCACAAAACACCTGCATC CCTAGCTATGATACCATTGGAGGCTTCTCCCAACACGTGAACCATGTGTGGCCCCAGACC TCATCCTCTTGGATTCGTGTGGTGCCCTGGGGGATAAGGAGGCTGTTGCAGTTTGTATCC CTGGAATACACAAGAGGAAAAGTTCCAATATACCTTGCCGGGAATGGCATGCCCATAGGG GAAAGTGAAAATCTCTTTGATGATTCCTTAAGAGTAGACTACTTCAATCAATATATCAAT GAGGTGCTCAAGGCTATCAAGGAAGACTCTGTGGATGTTCGTTCCTACATTGCTCGTTCC CTCATTGATGGCTTCGAAGGCCCTTCTGGTTACAGCCAGCGGTTTGGCCTGCACCACGTC AACTTCAGCGACAGCAGCAAGTCAAGGACTCCCAGGAAATCTGCCTACTTTTTCACTAGC ATCATAGAAAAGAACGGTTTCCTCACCAAGGGGGCAAAAAGACTGCTACCACCTAATACA GTAAACCTCCCCTCCAAAGTCAGAGCCTTCACTTTTCCATCTGAGGTGCCCTCCAAGGCT AAAGTCGTTTGGGAAAAGTTCTCCAGCCAACCCAAGTTCGAAAGAGATTTGTTCTACCAC GGGACGTTTCGGGATGACTTTCTGTGGGGCGTGTCCTCTTCCGCTTATCAGATTGAAGGC GCGTGGGATGCCGATGGCAAAGGCCCCAGCATCTGGGATAACTTTACCCACACACCAGGG AGCAATGTGAAAGACAATGCCACTGGAGACATCGCCTGTGACAGCTATCACCAGCTGGAT GCCGATCTGAATATGCTCCGAGCTTTGAAGGTGAAGGCCTACCGCTTCTCTATCTCCTGG TCTCGGATTTTCCCAACTGGGAGAAACAGCTCTATCAACAGTCATGGGGTTGATTATTAC AACAGGCTGATCAATGGCTTGGTGGCAAGCAACATCTTTCCCATGGTGACATTGTTCCAT TGGGACCTGCCCCAGGCCCTCCAGGATATCGGAGGCTGGGAGAATCCTGCCTTGATTGAC TTGTTTGACAGCTACGCAGACTTTTGTTTCCAGACCTTTGGTGATAGAGTCAAGTTTTGG ATGACTTTTAATGAGCCCATGTACCTGGCATGGCTAGGTTATGGCTCAGGGGAATTTCCC CCAGGGGTGAAGGACCCAGGCTGGGCACCATATAGGATAGCCCACACCGTCATCAAAGCC CATGCCAGAGTCTATCACACGTACGATGAGAAATACAGGCAGGAGCAGAAGGGGGTCATC TCGCTGAGCCTCAGTACACACTGGGCAGAGCCCAAGTCACCAGGGGTCCCCAGAGATGTG GAAGCCGCTGACCGAATGCTGCAGTTCTCCCTGGGCTGGTTTGCTCACCCCATTTTTAGA AACGGAGACTATCCTGACACCATGAAGTGGAAAGTGGGGAACAGGAGTGAACTGCAGCAC TTAGCCACCTCCCGCCTGCCAAGCTTCACTGAGGAAGAGAAGAGGTTCATCAGGGCGACG GCCGACGTCTTCTGCCTCAACACGTACTACTCCAGAATCGTGCAGCACAAAACACCCAGG CTAAACCCACCCTCCTACGAAGACGACCAGGAGATGGCTGAGGAGGAGGACCCTTCGTGG CCTTCCACGGCAATGAACAGAGCTGCGCCCTGGGGGACGCGAAGGCTGCTGAACTGGATC AAGGAAGAGTATGGTGACATCCCCATTTACATCACCGAAAACGGAGTGGGGCTGACCAAT CCGAACACGGAGGATACTGATAGGATATTTTACCACAAAACCTACATCAATGAGGCTTTG AAAGCCTACAGGCTCGATGGTATAGACCTTCGAGGGTATGTCGCCTGGTCTCTGATGGAC AACTTTGAGTGGCTAAATGGCTACACGGTCAAGTTTGGACTGTACCATGTTGATTTCAAC AACACGAACAGGCCTCGCACAGCAAGAGCCTCCGCCAGGTACTACACAGAGGTCATTACC AACAACGGCATGCCACTGGCCAGGGAGGATGAGTTTCTGTACGGACGGTTTCCTGAGGGC TTCATCTGGAGTGCAGCTTCTGCTGCATATCAGATTGAAGGTGCGTGGAGAGCAGATGGC AAAGGACTCAGCATTTGGGACACGTTTTCTCACACACCACTGAGGGTTGAGAACGATGCC ATTGGAGACGTGGCCTGTGACAGTTATCACAAGATTGCTGAGGATCTGGTCACCCTGCAG AACCTGGGTGTGTCCCACTACCGTTTTTCCATCTCCTGGTCTCGCATCCTCCCTGATGGA ACCACCAGGTACATCAATGAAGCGGGCCTGAACTACTACGTGAGGCTCATCGATACACTG CTGGCCGCCAGCATCCAGCCCCAGGTGACCATTTACCACTGGGACCTACCACAGACGCTC CAAGATGTAGGAGGCTGGGAGAATGAGACCATCGTGCAGCGGTTTAAGGAGTATGCAGAT GTGCTCTTCCAGAGGCTGGGAGACAAGGTGAAGTTTTGGATCACGTTGAATGAGCCCTTT GTCATTGCTTACCAGGGCTATGGCTACGGAACAGCAGCTCCAGGAGTCTCCAATAGGCCT GGCACTGCCCCCTACATTGTTGGCCACAATCTAATAAAGGCTCATGCTGAGGCCTGGCAT CTGTACAACGATGTGTACCGCGCCAGTCAAGGTGGCGTGATTTCCATCACCATCAGCAGT GACTGGGCTGAACCCAGAGATCCCTCTAACCAGGAGGATGTGGAGGCAGCCAGGAGATAT GTTCAGTTCATGGGAGGCTGGTTTGCACATCCTATTTTCAAGAATGGAGATTACAATGAG GTGATGAAGACGCGGATCCGTGACAGGAGCTTGGCTGCAGGCCTCAACAAGTCTCGGCTG CCAGAATTTACAGAGAGTGAGAAGAGGAGGATCAACGGCACCTATGACTTTTTTGGGTTC AATCACTACACCACTGTCCTCGCCTACAACCTCAACTATGCCACTGCCATCTCTTCTTTT GATGCAGACAGAGGAGTTGCTTCCATCGCAGATCGCTCGTGGCCAGACTCTGGCTCCTTC TGGCTGAAGATGACGCCTTTTGGCTTCAGGAGGATCCTGAACTGGTTAAAGGAGGAATAC AATGACCCTCCAATTTATGTCACAGAGAATGGAGTGTCCCAGCGGGAAGAAACAGACCTC AATGACACTGCAAGGATCTACTACCTTCGGACTTACATCAATGAGGCCCTCAAAGCTGTG CAGGACAAGGTGGACCTTCGAGGATACACAGTTTGGAGTGCGATGGACAATTTTGAGTGG GCCACAGGCTTTTCAGAGAGATTTGGTCTGCATTTTGTGAACTACAGTGACCCTTCTCTG CCAAGGATCCCCAAAGCATCAGCGAAGTTCTACGCCTCTGTGGTCCGATGCAATGGCTTC CCTGACCCCGCTACAGGGCCTCACGCTTGTCTCCACCAGCCAGATGCTGGACCCACCATC AGCCCCGTGAGACAGGAGGAGGTGCAGTTCCTGGGGCTAATGCTCGGCACCACAGAAGCA CAGACAGCTTTGTACGTTCTCTTTTCTCTTGTGCTTCTTGGAGTCTGTGGCTTGGCATTT CTGTCATACAAGTACTGCAAGCGCTCTAAGCAAGGGAAAACACAACGAAGCCAACAGGAA TTGAGCCCGGTGTCTTCATTCTGA PF00232 Glyco_hydro_1 function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process "
drug:(1S,2S,3R,4S,5S)-2,3,4-TRIHYDROXY-5-(HYDROXYMETHYL)CYCLOHEXYL (1E)-2-PHENYL-N-(SULFOOXY)ETHANIMIDOTHIOATErdfs:label"(1S,2S,3R,4S,5S)-2,3,4-TRIHYDROXY-5-(HYDROXYMETHYL)CYCLOHEXYL (1E)-2-PHENYL-N-(SULFOOXY)ETHANIMIDOTHIOATE"
drug:(1S,2S,3R,4S,5S)-2,3,4-TRIHYDROXY-5-(HYDROXYMETHYL)CYCLOHEXYL (1E)-2-PHENYL-N-(SULFOOXY)ETHANIMIDOTHIOATErdf:typedrugbank:drugs
drug:(1S,2S,3R,6R)-4-(hydroxymethyl)-6-(octylamino)cyclohex-4-ene-1,2,3-trioldrugbank:description" experimental This compound belongs to the aminocyclitols and derivatives. These are cyclitols with at least one hydroxyl group replace by an amino group. Aminocyclitols and Derivatives Organic Compounds Organooxygen Compounds Alcohols and Polyols Cyclic Alcohols and Derivatives Secondary Alcohols 1,2-Diols Primary Alcohols Dialkylamines Polyamines secondary alcohol 1,2-diol polyol secondary amine primary alcohol secondary aliphatic amine polyamine amine organonitrogen compound logP 0.95 ALOGPS logS -1.4 ALOGPS Water Solubility 1.13e+01 g/l ALOGPS logP 0.4 ChemAxon IUPAC Name (1S,2S,3R,6R)-4-(hydroxymethyl)-6-(octylamino)cyclohex-4-ene-1,2,3-triol ChemAxon Traditional IUPAC Name (1S,2S,3R,6R)-4-(hydroxymethyl)-6-(octylamino)cyclohex-4-ene-1,2,3-triol ChemAxon Molecular Weight 287.3951 ChemAxon Monoisotopic Weight 287.209658421 ChemAxon SMILES [H][C@@]1(O)C(CO)=C[C@@]([H])(NCCCCCCCC)[C@]([H])(O)[C@@]1([H])O ChemAxon Molecular Formula C15H29NO4 ChemAxon InChI InChI=1S/C15H29NO4/c1-2-3-4-5-6-7-8-16-12-9-11(10-17)13(18)15(20)14(12)19/h9,12-20H,2-8,10H2,1H3/t12-,13-,14+,15+/m1/s1 ChemAxon InChIKey InChIKey=UPZUHYMBTUUPML-KBXIAJHMSA-N ChemAxon Polar Surface Area (PSA) 92.95 ChemAxon Refractivity 78.94 ChemAxon Polarizability 33.42 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 12.83 ChemAxon pKa (strongest basic) 8.47 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 9817381 PubChem Substance 99444792 ChemSpider 7993131 PDB OEV BE0003505 Alpha-mannosidase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Alpha-mannosidase 2 Carbohydrate transport and metabolism Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway MAN2A1 Golgi apparatus membrane 6-26 7.61 131142.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6824 GenAtlas MAN2A1 GenBank Gene Database D63998 UniProtKB Q16706 UniProt Accession MA2A1_HUMAN Alpha-mannosidase II EC 3.2.1.114 Golgi alpha- mannosidase II MAN II Mannosidase alpha class 2A member 1 Mannosyl- oligosaccharide 1,3-1,6-alpha-mannosidase >Alpha-mannosidase 2 MKLSRQFTVFGSAIFCVVIFSLYLMLDRGHLDYPRNPRREGSFPQGQLSMLQEKIDHLER LLAENNEIISNIRDSVINLSESVEDGPKSSQSNFSQGAGSHLLPSQLSLSVDTADCLFAS QSGSHNSDVQMLDVYSLISFDNPDGGVWKQGFDITYESNEWDTEPLQVFVVPHSHNDPGW LKTFNDYFRDKTQYIFNNMVLKLKEDSRRKFIWSEISYLSKWWDIIDIQKKDAVKSLIEN GQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLENNIGVKPRSGWAIDPFGHSPTMAYL LNRAGLSHMLIQRVHYAVKKHFALHKTLEFFWRQNWDLGSVTDILCHMMPFYSYDIPHTC GPDPKICCQFDFKRLPGGRFGCPWGVPPETIHPGNVQSRARMLLDQYRKKSKLFRTKVLL APLGDDFRYCEYTEWDLQFKNYQQLFDYMNSQSKFKVKIQFGTLSDFFDALDKADETQRD KGQSMFPVLSGDFFTYADRDDHYWSGYFTSRPFYKRMDRIMESHLRAAEILYYFALRQAH KYKINKFLSSSLYTALTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFHSLMVLEKIIG NSAFLLILKDKLTYDSYSPDTFLEMDLKQKSQDSLPQKNIIRLSAEPRYLVVYNPLEQDR ISLVSVYVSSPTVQVFSASGKPVEVQVSAVWDTANTISETAYEISFRAHIPPLGLKVYKI LESASSNSHLADYVLYKNKVEDSGIFTIKNMINTEEGITLENSFVLLRFDQTGLMKQMMT KEDGKHHEVNVQFSWYGTTIKRDKSGAYLFLPDGNAKPYVYTTPPFVRVTHGRIYSEVTC FFDHVTHRVRLYHIQGIEGQSVEVSNIVDIRKVYNREIAMKISSDIKSQNRFYTDLNGYQ IQPRMTLSKLPLQANVYPMTTMAYIQDAKHRLTLLSAQSLGVSSLNSGQIEVIMDRRLMQ DDNRGLEQGIQDNKITANLFRILLEKRSAVNTEEEKKSVSYPSLLSHITSSLMNHPVIPM ANKFSSPTLELQGEFSPLQSSLPCDIHLVNLRTIQSKVGNGHSNEAALILHRKGFDCRFS SKGTGLFCSTTQGKILVQKLLNKFIVESLTPSSLSLMHSPPGTQNISEINLSPMEISTFR IQLR PF09261 Alpha-mann_mid PF01074 Glyco_hydro_38 PF07748 Glyco_hydro_38C function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity function mannosidase activity function alpha-mannosidase activity function hydrolase activity process macromolecule metabolism process carbohydrate metabolism process alcohol metabolism process monosaccharide metabolism process hexose metabolism process physiological process process mannose metabolism process metabolism process cellular metabolism "
drug:(1S,2S,3R,6R)-4-(hydroxymethyl)-6-(octylamino)cyclohex-4-ene-1,2,3-triolrdfs:label"(1S,2S,3R,6R)-4-(hydroxymethyl)-6-(octylamino)cyclohex-4-ene-1,2,3-triol"
drug:(1S,2S,3R,6R)-4-(hydroxymethyl)-6-(octylamino)cyclohex-4-ene-1,2,3-triolrdf:typedrugbank:drugs
drug:(1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOLdrugbank:description" experimental This compound belongs to the gamma amino acids and derivatives. These are amino acids having a (-NH2) group attached to the gamma carbon atom. Gamma Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Benzamides Benzoyl Derivatives Cyclohexanols Secondary Carboxylic Acid Amides Cyclic Alcohols and Derivatives Carboxylic Acids Polyamines Enolates benzamide benzoyl cyclohexanol benzene cyclic alcohol carboxamide group secondary carboxylic acid amide secondary alcohol enolate polyamine carboxylic acid amine organonitrogen compound alcohol logP 3.3 ALOGPS logS -5.1 ALOGPS Water Solubility 2.98e-03 g/l ALOGPS logP 3.28 ChemAxon IUPAC Name 4-({4-[(1R,2S,4S)-2-hydroxy-4-phenylcyclohexyl]phenyl}formamido)butanoic acid ChemAxon Traditional IUPAC Name 4-({4-[(1R,2S,4S)-2-hydroxy-4-phenylcyclohexyl]phenyl}formamido)butanoic acid ChemAxon Molecular Weight 381.4648 ChemAxon Monoisotopic Weight 381.194008357 ChemAxon SMILES [H][C@]1(O)C[C@]([H])(CC[C@]1([H])C1=CC=C(C=C1)C(=O)NCCCC(O)=O)C1=CC=CC=C1 ChemAxon Molecular Formula C23H27NO4 ChemAxon InChI InChI=1S/C23H27NO4/c25-21-15-19(16-5-2-1-3-6-16)12-13-20(21)17-8-10-18(11-9-17)23(28)24-14-4-7-22(26)27/h1-3,5-6,8-11,19-21,25H,4,7,12-15H2,(H,24,28)(H,26,27)/t19-,20+,21-/m0/s1 ChemAxon InChIKey InChIKey=OBWILOKKNDYPLX-HBMCJLEFSA-N ChemAxon Polar Surface Area (PSA) 86.63 ChemAxon Refractivity 108 ChemAxon Polarizability 43.82 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 4.14 ChemAxon pKa (strongest basic) -0.49 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon ChEBI 43278 PubChem Compound 444394 PubChem Substance 99444380 ChemSpider 392337 PDB HOP BE0004119 Uncharacterized protein Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Uncharacterized protein Involved in protein binding None 7.7 25701.7 Human HUGO Gene Nomenclature Committee (HGNC) GNC:5732 GenBank Gene Database BC005332 GenBank Protein Database 13529116 UniProtKB Q7Z3Y4 UniProt Accession Q7Z3Y4_HUMAN >Putative uncharacterized protein MDMRVLAQLLGLLLLCFPGARCDIQMTQSPSSLSASVGDTVTITCRASQDISNYLAWFQQ KPGKAPKSLIYGASSLQSGVQSKFSGSGSGTDFTLTISSLQPEDFATYYCQQYKSYPVTF GQGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGN SQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC >711 bp ATGGACATGAGAGTCCTCGCTCAGCTCCTGGGGCTCCTGCTGCTCTGTTTCCCAGGTGCC AGATGTGACATCCAGATGACCCAGTCTCCATCCTCACTGTCTGCATCTGTCGGAGACACA GTCACCATCACTTGTCGGGCGAGTCAGGACATTAGCAATTATTTAGCCTGGTTTCAGCAG AAACCAGGGAAAGCCCCTAAGTCCCTGATCTATGGTGCATCCAGTTTGCAAAGTGGGGTC CAATCAAAGTTCAGCGGCAGTGGATCTGGGACAGATTTCACTCTCACCATCAGCAGCCTG CAGCCTGAAGATTTTGCAACTTATTACTGCCAACAGTATAAAAGTTATCCTGTCACTTTT GGCCAGGGGACCAAGCTGGAGATCAAACGAACTGTGGCTGCACCATCTGTCTTCATCTTC CCGCCATCTGATGAGCAGTTGAAATCTGGAACTGCCTCTGTTGTGTGCCTGCTGAATAAC TTCTATCCCAGAGAGGCCAAAGTACAGTGGAAGGTGGATAACGCCCTCCAATCGGGTAAC TCCCAGGAGAGTGTCACAGAGCAGGACAGCAAGGACAGCACCTACAGCCTCAGCAGCACC CTGACGCTGAGCAAAGCAGACTACGAGAAACACAAAGTCTACGCCTGCGAAGTCACCCAT CAGGGCCTGAGCTCGCCCGTCACAAAGAGCTTCAACAGGGGAGAGTGTTAG PF07686 V-set PF07654 C1-set BE0002815 Ig gamma-1 chain C region Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Ig gamma-1 chain C region IGHG1 14q32.33 None 8.31 36106.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:5525 GenAtlas IGHG1 UniProtKB P01857 UniProt Accession IGHG1_HUMAN >Ig gamma-1 chain C region ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYN STYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDE LTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW QQGNVFSCSVMHEALHNHYTQKSLSLSPGK PF07654 C1-set BE0003836 Ig kappa chain C region Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Ig kappa chain C region Involved in antigen binding IGKC 2p12 None 5.68 11608.8 Human HUGO Gene Nomenclature Committee (HGNC) GNC:5716 GeneCards IGKC GenBank Gene Database J00241 GenBank Protein Database 185945 UniProtKB P01834 UniProt Accession IGKC_HUMAN >Ig kappa chain C region TVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDS KDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC PF07654 C1-set "
drug:(1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOLrdfs:label"(1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOL"
drug:(1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOLrdf:typedrugbank:drugs
drug:(1S,3R,4S,5S,7S)-4-{[2-(4-METHOXYPHENOXY)-2-METHYLPROPANOYL]AMINO}ADAMANTANE-1-CARBOXAMIDEdrugbank:description" experimental This compound belongs to the anisoles. These are organic compounds contaiing a methoxybenzene or a derivative thereof. Anisoles Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenol Ethers Alkyl Aryl Ethers Secondary Carboxylic Acid Amides Primary Carboxylic Acid Amides Enolates Carboxylic Acids Polyamines alkyl aryl ether primary carboxylic acid amide secondary carboxylic acid amide carboxamide group enolate polyamine carboxylic acid derivative ether carboxylic acid amine organonitrogen compound logP 2.84 ALOGPS logS -4.5 ALOGPS Water Solubility 1.17e-02 g/l ALOGPS logP 2.41 ChemAxon IUPAC Name (1s,3R,4s,5S,7s)-4-[2-(4-methoxyphenoxy)-2-methylpropanamido]adamantane-1-carboxamide ChemAxon Traditional IUPAC Name (1s,3R,4s,5S,7s)-4-[2-(4-methoxyphenoxy)-2-methylpropanamido]adamantane-1-carboxamide ChemAxon Molecular Weight 386.4846 ChemAxon Monoisotopic Weight 386.220557458 ChemAxon SMILES [H][C@@]12C[C@@]3([H])C[C@@](C1)(C[C@@]([H])(C2)[C@@]3([H])NC(=O)C(C)(C)OC1=CC=C(OC)C=C1)C(N)=O ChemAxon Molecular Formula C22H30N2O4 ChemAxon InChI InChI=1S/C22H30N2O4/c1-21(2,28-17-6-4-16(27-3)5-7-17)20(26)24-18-14-8-13-9-15(18)12-22(10-13,11-14)19(23)25/h4-7,13-15,18H,8-12H2,1-3H3,(H2,23,25)(H,24,26)/t13-,14-,15+,18-,22- ChemAxon InChIKey InChIKey=MNVKIDPRYUGTTG-YINOZDTMSA-N ChemAxon Polar Surface Area (PSA) 90.65 ChemAxon Refractivity 104.46 ChemAxon Polarizability 42.32 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 14.84 ChemAxon pKa (strongest basic) 0.8 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 15942677 PubChem Substance 99444751 PDB NN4 BE0000329 Corticosteroid 11-beta-dehydrogenase isozyme 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Corticosteroid 11-beta-dehydrogenase isozyme 1 Lipid transport and metabolism Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7- ketocholesterol to 7-beta-hydroxycholesterol HSD11B1 1q32-q41 Endoplasmic reticulum; endoplasmic reticulum membrane; single-pass type II membrane protein 7-23 8.77 32270.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:5208 GenAtlas HSD11B1 GeneCards HSD11B1 GenBank Gene Database M76665 GenBank Protein Database 179475 UniProtKB P28845 UniProt Accession DHI1_HUMAN 11-beta-HSD1 11-beta-hydroxysteroid dehydrogenase 1 11-DH EC 1.1.1.146 >Corticosteroid 11-beta-dehydrogenase isozyme 1 AFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHV VVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHI TNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVA AYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEEC ALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK >879 bp ATGGCTTTTATGAAAAAATATCTCCTCCCCATTCTGGGGCTCTTCATGGCCTACTACTAC TATTCTGCAAACGAGGAATTCAGACCAGAGATGCTCCAAGGAAAGAAAGTGATTGTCACA GGGGCCAGCAAAGGGATCGGAAGAGAGATGGCTTATCATCTGGCGAAGATGGGAGCCCAT GTGGTGGTGACAGCGAGGTCAAAAGAAACTCTACAGAAGGTGGTATCCCACTGCCTGGAG CTTGGAGCAGCCTCAGCACACTACATTGCTGGCACCATGGAAGACATGACCTTCGCAGAG CAATTTGTTGCCCAAGCAGGAAAGCTCATGGGAGGACTAGACATGCTCATTCTCAACCAC ATCACCAACACTTCTTTGAATCTTTTTCATGATGATATTCACCATGTGCGCAAAAGCATG GAAGTCAACTTCCTCAGTTACGTGGTCCTGACTGTAGCTGCCTTGCCCATGCTGAAGCAG AGCAATGGAAGCATTGTTGTCGTCTCCTCTCTGGCTGGGAAAGTGGCTTATCCAATGGTT GCTGCCTATTCTGCAAGCAAGTTTGCTTTGGATGGGTTCTTCTCCTCCATCAGAAAGGAA TATTCAGTGTCCAGGGTCAATGTATCAATCACTCTCTGTGTTCTTGGCCTCATAGACACA GAAACAGCCATGAAGGCAGTTTCTGGGATAGTCCATATGCAAGCAGCTCCAAAGGAGGAA TGTGCCCTGGAGATCATCAAAGGGGGAGCTCTGCGCCAAGAAGAAGTGTATTATGACAGC TCACTCTGGACCACTCTTCTGATCAGAAATCCATGCAGGAAGATCCTGGAATTTCTCTAC TCAACGAGCTATAATATGGACAGATTCATAAACAAGTAG PF00106 adh_short function catalytic activity function oxidoreductase activity process physiological process process metabolism "
drug:(1S,3R,4S,5S,7S)-4-{[2-(4-METHOXYPHENOXY)-2-METHYLPROPANOYL]AMINO}ADAMANTANE-1-CARBOXAMIDErdfs:label"(1S,3R,4S,5S,7S)-4-{[2-(4-METHOXYPHENOXY)-2-METHYLPROPANOYL]AMINO}ADAMANTANE-1-CARBOXAMIDE"
drug:(1S,3R,4S,5S,7S)-4-{[2-(4-METHOXYPHENOXY)-2-METHYLPROPANOYL]AMINO}ADAMANTANE-1-CARBOXAMIDErdf:typedrugbank:drugs
drug:(1S,3R,6S)-4-oxo-6-{4-[(2-phenylquinolin-4-yl)methoxy]phenyl}-5-azaspiro[2.4]heptane-1-carboxylic aciddrugbank:description" experimental This compound belongs to the phenylquinolines. These are heterocyclic compounds containing a quinoline moiety substituted with a phenyl group. Phenylquinolines Organic Compounds Heterocyclic Compounds Quinolines and Derivatives Phenylquinolines Phenylpyridines Phenylpyrrolidines Phenol Ethers Alkyl Aryl Ethers Pyrrolidones Cyclopropanecarboxylic Acids Pyrroles Lactams Secondary Carboxylic Acid Amides Polyamines Carboxylic Acids Enolates 2-phenylpyridine 2-phenylpyrrolidine phenol ether alkyl aryl ether cyclopropanecarboxylic acid pyrrolidone cyclopropanecarboxylic acid or derivative pyridine benzene pyrrolidine pyrrole secondary carboxylic acid amide lactam carboxamide group enolate polyamine ether carboxylic acid carboxylic acid derivative organonitrogen compound logP 4.59 ALOGPS logS -6 ALOGPS Water Solubility 5.13e-04 g/l ALOGPS logP 4.3 ChemAxon IUPAC Name (1S,3R,6S)-4-oxo-6-{4-[(2-phenylquinolin-4-yl)methoxy]phenyl}-5-azaspiro[2.4]heptane-1-carboxylic acid ChemAxon Traditional IUPAC Name (1S,3R,6S)-4-oxo-6-{4-[(2-phenylquinolin-4-yl)methoxy]phenyl}-5-azaspiro[2.4]heptane-1-carboxylic acid ChemAxon Molecular Weight 464.5119 ChemAxon Monoisotopic Weight 464.173607266 ChemAxon SMILES [H][C@@]1(C[C@@]11C[C@]([H])(NC1=O)C1=CC=C(OCC2=CC(=NC3=C2C=CC=C3)C2=CC=CC=C2)C=C1)C(O)=O ChemAxon Molecular Formula C29H24N2O4 ChemAxon InChI InChI=1S/C29H24N2O4/c32-27(33)23-15-29(23)16-26(31-28(29)34)19-10-12-21(13-11-19)35-17-20-14-25(18-6-2-1-3-7-18)30-24-9-5-4-8-22(20)24/h1-14,23,26H,15-17H2,(H,31,34)(H,32,33)/t23-,26+,29-/m1/s1 ChemAxon InChIKey InChIKey=BFZXMIUWGSTUAL-ZSOKXDGFSA-N ChemAxon Polar Surface Area (PSA) 88.52 ChemAxon Refractivity 129.82 ChemAxon Polarizability 50.58 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 4.09 ChemAxon pKa (strongest basic) 3.46 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 6 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 25049750 PubChem Substance 99443660 PDB 642 BE0003754 Disintegrin and metalloproteinase domain-containing protein 17 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Disintegrin and metalloproteinase domain-containing protein 17 Involved in integrin binding Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Also involved in the activation of Notch pathway (By similarity) ADAM17 2p25 Membrane 672-692 5.5 93020.2 Human HUGO Gene Nomenclature Committee (HGNC) GNC:195 GeneCards ADAM17 GenBank Gene Database U86755 GenBank Protein Database 1857673 UniProtKB P78536 UniProt Accession ADA17_HUMAN ADAM 17 CD156b antigen Snake venom-like protease TNF-alpha convertase TNF-alpha-converting enzyme >Disintegrin and metalloproteinase domain-containing protein 17 MRQSLLFLTSVVPFVLAPRPPDDPGFGPHQRLEKLDSLLSDYDILSLSNIQQHSVRKRDL QTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQDFFTGHVV GEPDSRVLAHIRDDDVIIRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKNVSRLQS PKVCGYLKVDNEELLPKGLVDREPPEELVHRVKRRADPDPMKNTCKLLVVADHRFYRYMG RGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNM AKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANS HGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGL AECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGN SRVDEGEECDPGIMYLNNDTCCNSDCTLKEGVQCSDRNSPCCKNCQFETAQKKCQEAINA TCKGVSYCTGNSSECPPPGNAEDDTVCLDLGKCKDGKCIPFCEREQQLESCACNETDNSC KVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWDFIDQLS INTFGKFLADNIVGSVLVFSLIFWIPFSILVHCVDKKLDKQYESLSLFHPSNVEMLSSMD SASVRIIKPFPAPQTPGRLQPAPVIPSAPAAPKLDHQRMDTIQEDPSTDSHMDEDGFEKD PFPNSSTAAKSFEDLTDHPVTRSEKAASFKLQRQNRVDSKETEC >2475 bp ATGAGGCAGTCTCTCCTATTCCTGACCAGCGTGGTTCCTTTCGTGCTGGCGCCGCGACCT CCGGATGACCCGGGCTTCGGCCCCCACCAGAGACTCGAGAAGCTTGATTCTTTGCTCTCA GACTACGATATTCTCTCTTTATCTAATATCCAGCAGCATTCGGTAAGAAAAAGAGATCTA CAGACTTCAACACATGTAGAAACACTACTAACTTTTTCAGCTTTGAAAAGGCATTTTAAA TTATACCTGACATCAAGTACTGAACGTTTTTCACAAAATTTCAAGGTCGTGGTGGTGGAT GGTAAAAACGAAAGCGAGTACACTGTAAAATGGCAGGACTTCTTCACTGGACACGTGGTT GGTGAGCCTGACTCTAGGGTTCTAGCCCACATAAGAGATGATGATGTTATAATCAGAATC AACACAGATGGGGCCGAATATAACATAGAGCCACTTTGGAGATTTGTTAATGATACCAAA GACAAAAGAATGTTAGTTTATAAATCTGAAGATATCAAGAATGTTTCACGTTTGCAGTCT CCAAAAGTGTGTGGTTATTTAAAAGTGGATAATGAAGAGTTGCTCCCAAAAGGGTTAGTA GACAGAGAACCACCTGAAGAGCTTGTTCATCGAGTGAAAAGAAGAGCTGACCCAGATCCC ATGAAGAACACGTGTAAATTATTGGTGGTAGCAGATCATCGCTTCTACAGATACATGGGC AGAGGGGAAGAGAGTACAACTACAAATTACTTAATAGAGCTAATTGACAGAGTTGATGAC ATCTATCGGAACACTTCATGGGATAATGCAGGTTTTAAAGGCTATGGAATACAGATAGAG CAGATTCGCATTCTCAAGTCTCCACAAGAGGTAAAACCTGGTGAAAAGCACTACAACATG GCAAAAAGTTACCCAAATGAAGAAAAGGATGCTTGGGATGTGAAGATGTTGCTAGAGCAA TTTAGCTTTGATATAGCTGAGGAAGCATCTAAAGTTTGCTTGGCACACCTTTTCACATAC CAAGATTTTGATATGGGAACTCTTGGATTAGCTTATGTTGGCTCTCCCAGAGCAAACAGC CATGGAGGTGTTTGTCCAAAGGCTTATTATAGCCCAGTTGGGAAGAAAAATATCTATTTG AATAGTGGTTTGACGAGCACAAAGAATTATGGTAAAACCATCCTTACAAAGGAAGCTGAC CTGGTTACAACTCATGAATTGGGACATAATTTTGGAGCAGAACATGATCCGGATGGTCTA GCAGAATGTGCCCCGAATGAGGACCAGGGAGGGAAATATGTCATGTATCCCATAGCTGTG AGTGGCGATCACGAGAACAATAAGATGTTTTCAAACTGCAGTAAACAATCAATCTATAAG ACCATTGAAAGTAAGGCCCAGGAGTGTTTTCAAGAACGCAGCAATAAAGTTTGTGGGAAC TCGAGGGTGGATGAAGGAGAAGAGTGTGATCCTGGCATCATGTATCTGAACAACGACACC TGCTGCAACAGCGACTGCACGTTGAAGGAAGGTGTCCAGTGCAGTGACAGGAACAGTCCT TGCTGTAAAAACTGTCAGTTTGAGACTGCCCAGAAGAAGTGCCAGGAGGCGATTAATGCT ACTTGCAAAGGCGTGTCCTACTGCACAGGTAATAGCAGTGAGTGCCCGCCTCCAGGAAAT GCTGAAGATGACACTGTTTGCTTGGATCTTGGCAAGTGTAAGGATGGGAAATGCATCCCT TTCTGCGAGAGGGAACAGCAGCTGGAGTCCTGTGCATGTAATGAAACTGACAACTCCTGC AAGGTGTGCTGCAGGGACCTTTCTGGCCGCTGTGTGCCCTATGTCGATGCTGAACAAAAG AACTTATTTTTGAGGAAAGGAAAGCCCTGTACAGTAGGATTTTGTGACATGAATGGCAAA TGTGAGAAACGAGTACAGGATGTAATTGAACGATTTTGGGATTTCATTGACCAGCTGAGC ATCAATACTTTTGGAAAGTTTTTAGCAGACAACATCGTTGGGTCTGTCCTGGTTTTCTCC TTGATATTTTGGATTCCTTTCAGCATTCTTGTCCATTGTGTGGATAAGAAATTGGATAAA CAGTATGAATCTCTGTCTCTGTTTCACCCCAGTAACGTCGAAATGCTGAGCAGCATGGAT TCTGCATCGGTTCGCATTATCAAACCCTTTCCTGCGCCCCAGACTCCAGGCCGCCTGCAG CCTGCCCCTGTGATCCCTTCGGCGCCAGCAGCTCCAAAACTGGACCACCAGAGAATGGAC ACCATCCAGGAAGACCCCAGCACAGACTCACATATGGACGAGGATGGGTTTGAGAAGGAC CCCTTCCCAAATAGCAGCACAGCTGCCAAGTCATTTGAGGATCTCACGGACCATCCGGTC ACCAGAAGTGAAAAGGCTGCCTCCTTTAAACTGCAGCGTCAGAATCGTGTTGACAGCAAA GAAACAGAGTGCTAA PF01421 Reprolysin PF00200 Disintegrin component extracellular matrix component extracellular matrix (sensu Metazoa) function catalytic activity function peptidase activity function hydrolase activity function endopeptidase activity function ion binding function metallopeptidase activity function cation binding function metalloendopeptidase activity function transition metal ion binding function zinc ion binding function binding process cellular protein metabolism process metabolism process macromolecule metabolism process proteolysis process physiological process process protein metabolism "
drug:(1S,3R,6S)-4-oxo-6-{4-[(2-phenylquinolin-4-yl)methoxy]phenyl}-5-azaspiro[2.4]heptane-1-carboxylic acidrdfs:label"(1S,3R,6S)-4-oxo-6-{4-[(2-phenylquinolin-4-yl)methoxy]phenyl}-5-azaspiro[2.4]heptane-1-carboxylic acid"
drug:(1S,3R,6S)-4-oxo-6-{4-[(2-phenylquinolin-4-yl)methoxy]phenyl}-5-azaspiro[2.4]heptane-1-carboxylic acidrdf:typedrugbank:drugs
drug:(1S,3S,5S)-2-{(2S)-2-amino-2-[(1R,3S,5R,7S)-3-hydroxytricyclo[3.3.1.1~3,7~]dec-1-yl]acetyl}-2-azabicyclo[3.1.0]hexane-3-carbonitriledrugbank:description" experimental This compound belongs to the alpha amino acid amides. These are amide derivatives of alpha amino acids. Alpha Amino Acid Amides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues N-Acylpiperidines Cyclohexanols Pyrrolidines Tertiary Alcohols Tertiary Carboxylic Acid Amides Tertiary Amines Cyclic Alcohols and Derivatives Nitriles Enolates Polyamines Carboxylic Acids Monoalkylamines n-acyl-piperidine cyclohexanol piperidine tertiary carboxylic acid amide pyrrolidine tertiary alcohol cyclic alcohol tertiary amine carboxamide group carboxylic acid carbonitrile enolate polyamine nitrile amine alcohol organonitrogen compound primary amine primary aliphatic amine logP 0.88 ALOGPS logS -2.1 ALOGPS Water Solubility 2.26e+00 g/l ALOGPS logP -0.08 ChemAxon IUPAC Name (1S,3S,5S)-2-[(2S)-2-amino-2-[(1r,3R,5R,7S)-3-hydroxyadamantan-1-yl]acetyl]-2-azabicyclo[3.1.0]hexane-3-carbonitrile ChemAxon Traditional IUPAC Name (1S,3S,5S)-2-[(2S)-2-amino-2-[(1r,3R,5R,7S)-3-hydroxyadamantan-1-yl]acetyl]-2-azabicyclo[3.1.0]hexane-3-carbonitrile ChemAxon Molecular Weight 315.41 ChemAxon Monoisotopic Weight 315.194677059 ChemAxon SMILES [H][C@@](N)(C(=O)N1[C@@]2([H])C[C@@]2([H])C[C@@]1([H])C#N)[C@]12C[C@@]3([H])C[C@]([H])(C[C@](O)(C3)C1)C2 ChemAxon Molecular Formula C18H25N3O2 ChemAxon InChI InChI=1S/C18H25N3O2/c19-8-13-2-12-3-14(12)21(13)16(22)15(20)17-4-10-1-11(5-17)7-18(23,6-10)9-17/h10-15,23H,1-7,9,20H2/t10-,11+,12-,13+,14+,15-,17+,18-/m1/s1 ChemAxon InChIKey InChIKey=QGJUIPDUBHWZPV-YQBUGCKMSA-N ChemAxon Polar Surface Area (PSA) 90.35 ChemAxon Refractivity 83.99 ChemAxon Polarizability 33.84 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 14.74 ChemAxon pKa (strongest basic) 7.9 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 5 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11235729 PubChem Substance 99443936 PDB BJM BE0000854 Dipeptidyl peptidase 4 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dipeptidyl peptidase 4 Amino acid transport and metabolism Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Plays a role in T-cell activation DPP4 2q24.3 Cell membrane; single-pass type II membrane protein. Processed form:Secreted protein. Note=Also exis 7-28 5.92 88279.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3009 GenAtlas DPP4 GeneCards DPP4 GenBank Gene Database U13735 GenBank Protein Database 535388 UniProtKB P27487 UniProt Accession DPP4_HUMAN ADABP Adenosine deaminase complexing protein 2 Dipeptidyl peptidase IV DPP IV EC 3.4.14.5 T-cell activation antigen CD26 TP103 >Dipeptidyl peptidase 4 MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSL RWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNY VKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNL PSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYL CDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPS EPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISN EYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKY PLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGT FEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWE YYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP >2301 bp ATGAAGACACCGTGGAAGGTTCTTCTGGGACTGCTGGGTGCTGCTGCGCTTGTCACCATC ATCACCGTGCCCGTGGTTCTGCTGAACAAAGGCACAGATGATGCTACAGCTGACAGTCGC AAAACTTACACTCTAACTGATTACTTAAAAAATACTTATAGACTGAAGTTATACTCCTTA AGATGGATTTCAGATCATGAATATCTCTACAAACAAGAAAATAATATCTTGGTATTCAAT GCTGAATATGGAAACAGCTCAGTTTTCTTGGAGAACAGTACATTTGATGAGTTTGGACAT TCTATCAATGATTATTCAATATCTCCTGATGGGCAGTTTATTCTCTTAGAATACAACTAC GTGAAGCAATGGAGGCATTCCTACACAGCTTCATATGACATTTATGATTTAAATAAAAGG CAGCTGATTACAGAAGAGAGGATTCCAAACAACACACAGTGGGTCACATGGTCACCAGTG GGTCATAAATTGGCATATGTTTGGAACAATGACATTTATGTTAAAATTGAACCAAATTTA CCAAGTTACAGAATCACATGGACGGGGAAAGAAGATATAATATATAATGGAATAACTGAC TGGGTTTATGAAGAGGAAGTCTTCAGTGCCTACTCTGCTCTGTGGTGGTCTCCAAACGGC ACTTTTTTAGCATATGCCCAATTTAACGACACAGAAGTCCCACTTATTGAATACTCCTTC TACTCTGATGAGTCACTGCAGTACCCAAAGACTGTACGGGTTCCATATCCAAAGGCAGGA GCTGTGAATCCAACTGTAAAGTTCTTTGTTGTAAATACAGACTCTCTCAGCTCAGTCACC AATGCAACTTCCATACAAATCACTGCTCCTGCTTCTATGTTGATAGGGGATCACTACTTG TGTGATGTGACATGGGCAACACAAGAAAGAATTTCTTTGCAGTGGCTCAGGAGGATTCAG AACTATTCGGTCATGGATATTTGTGACTATGATGAATCCAGTGGAAGATGGAACTGCTTA GTGGCACGGCAACACATTGAAATGAGTACTACTGGCTGGGTTGGAAGATTTAGGCCTTCA GAACCTCATTTTACCCTTGATGGTAATAGCTTCTACAAGATCATCAGCAATGAAGAAGGT TACAGACACATTTGCTATTTCCAAATAGATAAAAAAGACTGCACATTTATTACAAAAGGC ACCTGGGAAGTCATCGGGATAGAAGCTCTAACCAGTGATTATCTATACTACATTAGTAAT GAATATAAAGGAATGCCAGGAGGAAGGAATCTTTATAAAATCCAACTTAGTGACTATACA AAAGTGACATGCCTCAGTTGTGAGCTGAATCCGGAAAGGTGTCAGTACTATTCTGTGTCA TTCAGTAAAGAGGCGAAGTATTATCAGCTGAGATGTTCCGGTCCTGGTCTGCCCCTCTAT ACTCTACACAGCAGCGTGAATGATAAAGGGCTGAGAGTCCTGGAAGACAATTCAGCTTTG GATAAAATGCTGCAGAATGTCCAGATGCCCTCCAAAAAACTGGACTTCATTATTTTGAAT GAAACAAAATTTTGGTATCAGATGATCTTGCCTCCTCATTTTGATAAATCCAAGAAATAT CCTCTACTATTAGATGTGTATGCAGGCCCATGTAGTCAAAAAGCAGACACTGTCTTCAGA CTGAACTGGGCCACTTACCTTGCAAGCACAGAAAACATTATAGTAGCTAGCTTTGATGGC AGAGGAAGTGGTTACCAAGGAGATAAGATCATGCATGCAATCAACAGAAGACTGGGAACA TTTGAAGTTGAAGATCAAATTGAAGCAGCCAGACAATTTTCAAAAATGGGATTTGTGGAC AACAAACGAATTGCAATTTGGGGCTGGTCATATGGAGGGTACGTAACCTCAATGGTCCTG GGATCGGGAAGTGGCGTGTTCAAGTGTGGAATAGCCGTGGCGCCTGTATCCCGGTGGGAG TACTATGACTCAGTGTACACAGAACGTTACATGGGTCTCCCAACTCCAGAAGACAACCTT GACCATTACAGAAATTCAACAGTCATGAGCAGAGCTGAAAATTTTAAACAAGTTGAGTAC CTCCTTATTCATGGAACAGCAGATGATAACGTTCACTTTCAGCAGTCAGCTCAGATCTCC AAAGCCCTGGTCGATGTTGGAGTGGATTTCCAGGCAATGTGGTATACTGATGAAGACCAT GGAATAGCTAGCAGCACAGCACACCAACATATATATACCCACATGAGCCACTTCATAAAA CAATGTTTCTCTTTACCTTAG PF00930 DPPIV_N PF00326 Peptidase_S9 component cell component membrane function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function serine-type peptidase activity function hydrolase activity function dipeptidyl-peptidase IV activity function prolyl oligopeptidase activity process protein metabolism process cellular protein metabolism process physiological process process proteolysis process metabolism process macromolecule metabolism "
drug:(1S,3S,5S)-2-{(2S)-2-amino-2-[(1R,3S,5R,7S)-3-hydroxytricyclo[3.3.1.1~3,7~]dec-1-yl]acetyl}-2-azabicyclo[3.1.0]hexane-3-carbonitrilerdfs:label"(1S,3S,5S)-2-{(2S)-2-amino-2-[(1R,3S,5R,7S)-3-hydroxytricyclo[3.3.1.1~3,7~]dec-1-yl]acetyl}-2-azabicyclo[3.1.0]hexane-3-carbonitrile"
drug:(1S,3S,5S)-2-{(2S)-2-amino-2-[(1R,3S,5R,7S)-3-hydroxytricyclo[3.3.1.1~3,7~]dec-1-yl]acetyl}-2-azabicyclo[3.1.0]hexane-3-carbonitrilerdf:typedrugbank:drugs
drug:(1S,3aS,5aR,8aS)-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylic aciddrugbank:description" experimental This compound belongs to the triquinane sesquiterpenes. Triquinane Sesquiterpenes Organic Compounds Lipids Prenol Lipids Sesquiterpenes Polyamines Enolates Carboxylic Acids enolate polyamine carboxylic acid carboxylic acid derivative logP 3.59 ALOGPS logS -3.8 ALOGPS Water Solubility 4.15e-02 g/l ALOGPS logP 3.29 ChemAxon IUPAC Name (1S,2S,5S,8R)-2,10,10-trimethyltricyclo[6.3.0.0^{1,5}]undec-6-ene-6-carboxylic acid ChemAxon Traditional IUPAC Name (1S,2S,5S,8R)-2,10,10-trimethyltricyclo[6.3.0.0^{1,5}]undec-6-ene-6-carboxylic acid ChemAxon Molecular Weight 234.334 ChemAxon Monoisotopic Weight 234.161979948 ChemAxon SMILES [H][C@]1(C)CC[C@]2([H])C(=C[C@@]3([H])CC(C)(C)C[C@@]123)C(O)=O ChemAxon Molecular Formula C15H22O2 ChemAxon InChI InChI=1S/C15H22O2/c1-9-4-5-12-11(13(16)17)6-10-7-14(2,3)8-15(9,10)12/h6,9-10,12H,4-5,7-8H2,1-3H3,(H,16,17)/t9-,10-,12+,15-/m0/s1 ChemAxon InChIKey InChIKey=DCFDRCCHOOORSB-JOXOIDLHSA-N ChemAxon Polar Surface Area (PSA) 37.3 ChemAxon Refractivity 67.41 ChemAxon Polarizability 26.71 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 4.94 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937034 PubChem Substance 99443374 PDB 1PL BE0003748 1-deoxypentalenic acid 11-beta-hydroxylase Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown 1-deoxypentalenic acid 11-beta-hydroxylase ptlH None 5.68 32264.0 Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) GeneCards ptlH GenBank Gene Database BA000030 GenBank Protein Database 29603637 UniProtKB Q82IZ1 UniProt Accession PTLH_STRAW Fe(II)/alpha-ketoglutarate dependent hydroxylase >1-deoxypentalenic acid 11-beta hydroxylase MTNVTGDYTDCTPLLGDRAALDSFYEEHGYLFLRNVLDRDLVKTVAEQMREGLVALGAAD PHATLEELTIDSFESVDEVAMHDYVKYDAFWNNPSTIKVFEQVFGEPVFVFLSTTIRYYP SQAGSEEPSFHYLTPFHQDGFYIGPNQDFRTFWIPLIRTTRESGGVALADGSHRRGKRDH VLNESFRRFGHPVRGIPPTEVSEDEHLLHSPMEPGDILLFHAHMCHKSIPNLSKDPRLMR MSMDTRVQPAKSHRGFNAMTPWTESAKDASKGIMAKITGTPTDVE >234 bp GTGCCCCCTCAGGGAGCCCGTGGCACGATCGTGTCAGCTACCGGGTCCGGCAAAACGAGC ATGGCCGCCGCGAGCACGCTGAACTGCTTCCCCGAAGGCCGGATCCTCGTGACCGTGCCG ACCCTGGACCTGCTCGCACAGACCGCCCAGGCGTGGCGGGCAGTCGGCCACCACTCCCCC ATGATCGCGGTGTGCTCGCTGGAGAACGACCCAGTGCTGAACGAGCGGACCTGA PF05721 PhyH "
drug:(1S,3aS,5aR,8aS)-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylic acidrdfs:label"(1S,3aS,5aR,8aS)-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylic acid"
drug:(1S,3aS,5aR,8aS)-1,7,7-trimethyl-1,2,3,3a,5a,6,7,8-octahydrocyclopenta[c]pentalene-4-carboxylic acidrdf:typedrugbank:drugs
drug:(1S,4R,7AR)-4-BUTOXY-1-[(1R)-1-FORMYLPROPYL]-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACIDdrugbank:description" experimental This compound belongs to the isoindoles. These are heteropolycyclic compounds whose structure contain isoindole, a benzo-fused pyrrole. Isoindoles Organic Compounds Heterocyclic Compounds Isoindoles and Derivatives Isoindoles Pyrroline Carboxylic Acids Enolates Ethers Polyamines Enamines Carboxylic Acids Aldehydes pyrroline carboxylic acid or derivative pyrroline carboxylic acid pyrroline polyamine enolate carboxylic acid derivative ether enamine carboxylic acid organonitrogen compound aldehyde logP 2.45 ALOGPS logS -3.2 ALOGPS Water Solubility 2.06e-01 g/l ALOGPS logP 2.1 ChemAxon IUPAC Name (1S,4R,7aR)-4-butoxy-1-[(2R)-1-oxobutan-2-yl]-2,4,5,6,7,7a-hexahydro-1H-isoindole-3-carboxylic acid ChemAxon Traditional IUPAC Name (3S,3aR,7R)-7-butoxy-3-[(2R)-1-oxobutan-2-yl]-3,3a,4,5,6,7-hexahydro-2H-isoindole-1-carboxylic acid ChemAxon Molecular Weight 309.4006 ChemAxon Monoisotopic Weight 309.194008357 ChemAxon SMILES [H][C@](CC)(C=O)[C@@]1([H])NC(C(O)=O)=C2[C@@]1([H])CCC[C@@]2([H])OCCCC ChemAxon Molecular Formula C17H27NO4 ChemAxon InChI InChI=1S/C17H27NO4/c1-3-5-9-22-13-8-6-7-12-14(13)16(17(20)21)18-15(12)11(4-2)10-19/h10-13,15,18H,3-9H2,1-2H3,(H,20,21)/t11-,12+,13+,15+/m0/s1 ChemAxon InChIKey InChIKey=WRBRCIHZCYLBFW-KYEXWDHISA-N ChemAxon Polar Surface Area (PSA) 75.63 ChemAxon Refractivity 84.63 ChemAxon Polarizability 34.61 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 4.47 ChemAxon pKa (strongest basic) 1.8 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937124 PubChem Substance 99444580 PDB LK5 BE0001430 Beta-lactamase Enterobacter cloacae # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-lactamase Defense mechanisms and antibiotic degradation This protein is a serine beta-lactamase with a substrate specificity for cephalosporins ampC Periplasm None 8.67 41302.0 Enterobacter cloacae GenBank Gene Database X07274 GenBank Protein Database 42261 UniProtKB P05364 UniProt Accession AMPC_ENTCL Beta-lactamase precursor Cephalosporinase EC 3.5.2.6 >Beta-lactamase precursor MMRKSLCCALLLGISCSALATPVSEKQLAEVVANTITPLMKAQSVPGMAVAVIYQGKPHY YTFGKADIAANKPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDAVTRYWPQLTGKQ WQGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYANASIGLFGA LAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAWGYRDGKAVRVSPGMLDAQA YGVKTNVQDMANWVMANMAPENVADASLKQGIALAQSRYWRIGSMYQGLGWEMLNWPVEA NTVVEGSDSKVALAPLPVAEVNPPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLA NTSYPNPARVEAAYHILEALQ >1146 bp ATGATGAGAAAATCCCTTTGCTGCGCCCTGCTGCTCGGCATCTCTTGCTCTGCTCTCGCC ACGCCAGTGTCAGAAAAACAGCTGGCGGAGGTGGTCGCGAATACGATTACCCCGCTGATG AAAGCCCAGTCTGTTCCAGGCATGGCGGTGGCCGTTATTTATCAGGGAAAACCGCACTAT TACACATTTGGCAAGGCCGATATCGCGGCGAATAAACCCGTTACGCCTCAGACCCTGTTC GAGCTGGGTTCTATAAGTAAAACCTTCACCGGCGTTTTAGGTGGGGATGCCATTGCTCGC GGTGAAATTTCGCTGGACGATGCGGTGACCAGATACTGGCCACAGCTGACGGGCAAGCAG TGGCAGGGTATTCGTATGCTGGATCTCGCCACCTACACCGCTGGCGGCCTGCCGCTACAG GTACCGGATGAGGTCACGGATAACGCCTCCCTGCTGCGCTTTTATCAAAACTGGCAGCCG CAGTGGAAGCCTGGCACAACGCGTCTTTACGCCAACGCCAGCATCGGTCTTTTTGGTGCG CTGGCGGTCAAACCTTCTGGCATGCCCTATGAGCAGGCCATGACGACGCGGGTCCTTAAG CCGCTCAAGCTGGACCATACCTGGATTAACGTGCCGAAAGCGGAAGAGGCGCATTACGCC TGGGGCTATCGTGACGGTAAAGCGGTGCGCGTTTCGCCGGGTATGCTGGATGCACAAGCC TATGGCGTGAAAACCAACGTGCAGGATATGGCGAACTGGGTCATGGCAAACATGGCGCCG GAGAACGTTGCTGATGCCTCACTTAAGCAGGGCATCGCGCTGGCGCAGTCGCGCTACTGG CGTATCGGGTCAATGTATCAGGGTCTGGGCTGGGAGATGCTCAACTGGCCCGTGGAGGCC AACACGGTGGTCGAGGGCAGCGACAGTAAGGTAGCACTGGCGCCGTTGCCCGTGGCAGAA GTGAATCCACCGGCTCCCCCGGTCAAAGCGTCCTGGGTCCATAAAACGGGCTCTACTGGC GGGTTTGGCAGCTACGTGGCCTTTATTCCTGAAAAGCAGATCGGTATTGTGATGCTCGCG AATACAAGCTATCCGAACCCGGCACGCGTTGAGGCGGCATACCATATCCTCGAGGCGCTA CAGTAA PF00144 Beta-lactamase component cell component periplasmic space component periplasmic space (sensu Gram-negative Bacteria) function beta-lactamase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function catalytic activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides process metabolism process cellular metabolism process drug metabolism process antibiotic metabolism process antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process physiological process process response to antibiotic "
drug:(1S,4R,7AR)-4-BUTOXY-1-[(1R)-1-FORMYLPROPYL]-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACIDrdfs:label"(1S,4R,7AR)-4-BUTOXY-1-[(1R)-1-FORMYLPROPYL]-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACID"
drug:(1S,4R,7AR)-4-BUTOXY-1-[(1R)-1-FORMYLPROPYL]-2,4,5,6,7,7A-HEXAHYDRO-1H-ISOINDOLE-3-CARBOXYLIC ACIDrdf:typedrugbank:drugs
drug:(1S,4R,9S)-5-(trifluoromethyl)-1,2,3,4-tetrahydro-1,4-methanonaphthalen-9-aminedrugbank:description" experimental This compound belongs to the tetralins. These are polycyclic aromatic compounds containing a tetralin moiety, which consists of a benzene fused to a cyclohexane. Tetralins Organic Compounds Benzenoids Tetralins Indanes Benzene and Substituted Derivatives Polyamines Monoalkylamines Organofluorides Alkyl Fluorides benzene polyamine organonitrogen compound amine primary amine primary aliphatic amine organofluoride organohalogen alkyl halide alkyl fluoride logP 3.09 ALOGPS logS -2.7 ALOGPS Water Solubility 4.51e-01 g/l ALOGPS logP 2.63 ChemAxon IUPAC Name (1R,8S,11S)-3-(trifluoromethyl)tricyclo[6.2.1.0^{2,7}]undeca-2(7),3,5-trien-11-amine ChemAxon Traditional IUPAC Name (1R,8S,11S)-3-(trifluoromethyl)tricyclo[6.2.1.0^{2,7}]undeca-2(7),3,5-trien-11-amine ChemAxon Molecular Weight 227.2256 ChemAxon Monoisotopic Weight 227.092184004 ChemAxon SMILES [H][C@]12CC[C@]([H])(C3=C(C=CC=C13)C(F)(F)F)[C@@]2([H])N ChemAxon Molecular Formula C12H12F3N ChemAxon InChI InChI=1S/C12H12F3N/c13-12(14,15)9-3-1-2-6-7-4-5-8(10(6)9)11(7)16/h1-3,7-8,11H,4-5,16H2/t7-,8+,11-/m0/s1 ChemAxon InChIKey InChIKey=HHIJEPNAHYLKPE-RNSXUZJQSA-N ChemAxon Polar Surface Area (PSA) 26.02 ChemAxon Refractivity 55.38 ChemAxon Polarizability 20.87 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 9.94 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937127 PubChem Substance 99444599 PDB LT3 BE0000865 Phenylethanolamine N-methyltransferase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Phenylethanolamine N-methyltransferase Involved in methyltransferase activity Converts noradrenaline to adrenaline PNMT 17q21-q22 None 5.96 30855.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9160 GenAtlas PNMT GeneCards PNMT GenBank Gene Database J03727 GenBank Protein Database 190142 UniProtKB P11086 UniProt Accession PNMT_HUMAN EC 2.1.1.28 Noradrenaline N-methyltransferase PNMTase >Phenylethanolamine N-methyltransferase MSGADRSPNAGAAPDSAPGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRC LAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEEPGA FNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPLPADALVS AFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVR EALVRSGYKVRDLRTYIMPAHLQTGVDDVKGVFFAWAQKVGL >849 bp ATGAGCGGCGCAGACCGTAGCCCCAATGCGGGCGCAGCCCCTGACTCGGCCCCGGGCCAG GCGGCGGTGGCTTCGGCCTACCAGCGCTTCGAGCCGCGCGCCTACCTCCGCAACAACTAC GCGCCCCCTCGCGGGGACCTGTGCAACCCGAACGGCGTCGGGCCGTGGAAGCTGCGCTGC TTGGCGCAGACCTTCGCCACCGGTGAAGTGTCCGGACGCACCCTCATCGACATTGGTTCA GGCCCCACCGTGTACCAGCTGCTCAGTGCCTGCAGCCACTTTGAGGACATCACCATGACA GATTTCCTGGAGGTCAACCGCCAGGAGCTGGGGCGCTGGCTGCAGGAGGAGCCGGGGGCC TTCAACTGGAGCATGTACAGCCAACATGCCTGCCTCATTGAGGGCAAGGGGGAATGCTGG CAGGATAAGGAGCGCCAGCTGCGAGCCAGGGTGAAACGGGTCCTGCCCATCGACGTGCAC CAGCCCCAGCCCCTGGGTGCTGGGAGCCCAGCTCCCCTGCCTGCTGACGCCCTGGTCTCT GCCTTCTGCTTGGAGGCTGTGAGCCCAGATCTTGCCAGCTTTCAGCGGGCCCTGGACCAC ATCACCACGCTGCTGAGGCCTGGGGGGCACCTCCTCCTCATCGGGGCCCTGGAGGAGTCG TGGTACCTGGCTGGGGAGGCCAGGCTGACGGTGGTGCCAGTGTCTGAGGAGGAGGTGAGG GAGGCCCTGGTGCGTAGTGGCTACAAGGTCCGGGACCTCCGCACCTATATCATGCCTGCC CACCTTCAGACAGGCGTAGATGATGTCAAGGGCGTCTTCTTCGCCTGGGCTCAGAAGGTT GGGCTGTGA PF01234 NNMT_PNMT_TEMT function transferase activity, transferring one-carbon groups function methyltransferase activity function catalytic activity function transferase activity "
drug:(1S,4R,9S)-5-(trifluoromethyl)-1,2,3,4-tetrahydro-1,4-methanonaphthalen-9-aminerdfs:label"(1S,4R,9S)-5-(trifluoromethyl)-1,2,3,4-tetrahydro-1,4-methanonaphthalen-9-amine"
drug:(1S,4R,9S)-5-(trifluoromethyl)-1,2,3,4-tetrahydro-1,4-methanonaphthalen-9-aminerdf:typedrugbank:drugs
drug:(1S,4S)-4-(3,4-dichlorophenyl)-N-methyl-1,2,3,4-tetrahydronaphthalen-1-aminedrugbank:description" experimental This compound belongs to the tametralines. These are compounds containing a tametraline moiety, which consists of a tetrahydronaphthalene linked to a phenyl group to form N-methyl-4-phenyl-1,2,3,4-tetrahydronaphthalen-1-amine skeleton. Tametralines Organic Compounds Benzenoids Tetralins Tametralines Dichlorobenzenes Aryl Chlorides Polyamines Dialkylamines Organochlorides 1,2-dichlorobenzene chlorobenzene benzene aryl chloride aryl halide secondary amine polyamine secondary aliphatic amine organohalogen organonitrogen compound amine organochloride logP 5.06 ALOGPS logS -6.3 ALOGPS Water Solubility 1.45e-04 g/l ALOGPS logP 5.15 ChemAxon IUPAC Name (1S,4S)-4-(3,4-dichlorophenyl)-N-methyl-1,2,3,4-tetrahydronaphthalen-1-amine ChemAxon Traditional IUPAC Name sertraline ChemAxon Molecular Weight 306.23 ChemAxon Monoisotopic Weight 305.073804963 ChemAxon SMILES [H][C@@]1(CC[C@@]([H])(C2=CC(Cl)=C(Cl)C=C2)C2=CC=CC=C12)NC ChemAxon Molecular Formula C17H17Cl2N ChemAxon InChI InChI=1S/C17H17Cl2N/c1-20-17-9-7-12(13-4-2-3-5-14(13)17)11-6-8-15(18)16(19)10-11/h2-6,8,10,12,17,20H,7,9H2,1H3/t12-,17-/m0/s1 ChemAxon InChIKey InChIKey=VGKDLMBJGBXTGI-SJCJKPOMSA-N ChemAxon Polar Surface Area (PSA) 12.03 ChemAxon Refractivity 85.74 ChemAxon Polarizability 32.45 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 9.85 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Ghose Filter true ChemAxon PubChem Compound 68617 PubChem Substance 99445038 ChemSpider 61881 PDB SRE BE0003930 Transporter Aquifex aeolicus (strain VF5) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Transporter Involved in neurotransmitter:sodium symporter activity snf None 9.17 57407.5 Aquifex aeolicus (strain VF5) GeneCards snf GenBank Gene Database AE000657 GenBank Protein Database 2982776 UniProtKB O67854 UniProt Accession O67854_AQUAE >Transporter MEVKREHWATRLGLILAMAGNAVGLGNFLRFPVQAAENGGGAFMIPYIIAFLLVGIPLMW IEWAMGRYGGAQGHGTTPAIFYLLWRNRFAKILGVFGLWIPLVVAIYYVYIESWTLGFAI KFLVGLVPEPPPNATDPDSILRPFKEFLYSYIGVPKGDEPILKPSLFAYIVFLITMFINV SILIRGISKGIERFAKIAMPTLFILAVFLVIRVFLLETPNGTAADGLNFLWTPDFEKLKD PGVWIAAVGQIFFTLSLGFGAIITYASYVRKDQDIVLSGLTAATLNEKAEVILGGSISIP AAVAFFGVANAVAIAKAGAFNLGFITLPAIFSQTAGGTFLGFLWFFLLFFAGLTSSIAIM QPMIAFLEDELKLSRKHAVLWTAAIVFFSAHLVMFLNKSLDEMDFWAGTIGVVFFGLTEL IIFFWIFGADKAWEEINRGGIIKVPRIYYYVMRYITPAFLAVLLVVWAREYIPKIMEETH WTVWITRFYIIGLFLFLTFLVFLAERRRNHESA >2100 bp ATGGCGAGAGAGGTGCCTATAGAGAAATTGAGAAACATAGGTATAGTTGCTCACATTGAC GCGGGTAAAACTACGACTACCGAGAGAATTCTCTATTACACGGGTAAGACTTACAAGATA GGTGAAGTTCACGAAGGTGCTGCAACGATGGACTGGATGCCCCAGGAAAAGGAAAGAGGT ATAACCATAACCGTTGCAACGACCGCATGTTATTGGACGAGAAACGGGGAGAGGTATCAA ATAAACATAATTGACACACCCGGACACGTTGACTTCTCCGTTGAAGTTGTACGTTCCATG AAAGTTCTCGACGGAATAGTTTTCATATTCTCCGCGGTTGAAGGTGTGCAACCTCAGTCC GAAGCAAACTGGAGATGGGCGGACAGGTTCCAAGTTCCGAGGATAGCCTTCATAAACAAG ATGGACCGTCTGGGTGCGGATTTTTACAGAGTGTTTAAGGAAATAGAAGAAAAGCTAACC ATAAAGCCCGTTGCCATTCAAATACCCCTGGGAGCGGAGGACCAGTTTGAAGGTGTTATA GATCTAATGGAAATGAAGGCAATAAGGTGGCTCGAAGAAACCCTCGGAGCTAAATACGAA GTAGTAGACATTCCTCCAGAATACCAGGAAAAGGCTCAAGAATGGCGCGAAAAGATGATA GAAACCATCGTAGAAACCGACGACGAGTTAATGGAAAAGTACTTAGAAGGACAGGAAATA TCTATAGATGAACTAAGAAAAGCTTTAAGAAAGGCAACAATAGAGAGAAAGCTCGTTCCC GTTCTTTGCGGTTCTGCATTCAAGAACAAAGGTGTTCAACCCCTTCTTGACGCAGTTATA GATTACCTGCCTTCTCCTATAGACCTTCCTCCCGTTAAGGGGACAAATCCCAAGACCGGG GAAGAAGAGGTCAGACACCCCTCTGACGACGAACCCTTCTGCGCTTACGCCTTTAAGGTT ATGTCCGACCCGTATGCCGGACAACTTACCTACATCAGAGTGTTCTCAGGAACGCTAAAA GCGGGTTCTTACGTCTACAACGCAACCAAGGACGAAAAGCAAAGGGCTGGAAGACTTCTT CTCATGCACGCGAACTCCAGAGAGGAAATACAGCAGGTTTCCGCGGGTGAAATTTGTGCA GTTGTAGGACTAGACGCCGCAACGGGTGATACTCTCTGTGATGAAAAGCACCCCATAATC CTTGAAAAGCTTGAATTCCCTGACCCCGTTATATCTATGGCTATAGAGCCAAAGACCAAG AAGGACCAAGAAAAACTCTCACAAGTTCTCAACAAGTTCATGAAAGAGGATCCAACCTTC AGGGCAACAACCGATCCCGAAACTGGTCAGATACTCATACACGGAATGGGTGAGCTCCAC CTCGAAATAATGGTTGACAGAATGAAGAGGGAATACGGAATTGAAGTGAACGTCGGTAAA CCGCAGGTTGCTTACAAGGAAACCATCAGGAAAAAGGCAATTGGTGAGGGTAAGTTCATC AAGCAAACTGGTGGTAGAGGGCAGTACGGTCACGCGATAATCGAAATCGAACCCCTCCCC AGAGGTGCGGGATTTGAATTCATAGACGACATTCACGGAGGAGTTATCCCCAAAGAATTC ATACCCTCCGTTGAGAAGGGTGTAAAGGAAGCTATGCAAAACGGAATTCTCGCAGGATAC CCCGTTGTTGACGTTAGAGTTAGACTCTTTGACGGTTCTTACCACGAAGTTGACTCTTCG GACATAGCATTCCAGGTTGCGGGTTCCTTGGCATTCAAAGATGCAGCCAAAAAGGCAGAT CCCGTTCTTCTGGAACCCATAATGGAAGTTGAAGTGGAAACTCCCGAAAAGTACGTGGGT GACGTTATAGGTGACCTTAACTCCAGAAGAGGAAAGATTATGGGAATGGAAAACAAGGGA GTTATAACAGTCATAAAGGCTCACGTTCCCCTCGCAGAGATGTTCGGATACGCTACGACG CTCAGGAGCTTGACACAAGGTAGGGGAACCTTTATAATGAAATTTTCCCACTACGACGAA GTTCCGCAGCAAATTGCGGAAAAGATTATCGGCGAAAGAATGGCCGGTAAGAGCTCTTAA PF00209 SNF component cell component intrinsic to membrane component integral to membrane component membrane component integral to plasma membrane function transporter activity function neurotransmitter transporter activity function neurotransmitter:sodium symporter activity process transport process neurotransmitter transport process physiological process process cellular physiological process "
drug:(1S,4S)-4-(3,4-dichlorophenyl)-N-methyl-1,2,3,4-tetrahydronaphthalen-1-aminerdfs:label"(1S,4S)-4-(3,4-dichlorophenyl)-N-methyl-1,2,3,4-tetrahydronaphthalen-1-amine"
drug:(1S,4S)-4-(3,4-dichlorophenyl)-N-methyl-1,2,3,4-tetrahydronaphthalen-1-aminerdf:typedrugbank:drugs
drug:(1S,4S,5S)-1,4,5-TRIHYDROXY-3-[3-(PHENYLTHIO)PHENYL]CYCLOHEX-2-ENE-1-CARBOXYLIC ACIDdrugbank:description" experimental This compound belongs to the quinic acids and derivatives. These are compounds containing a quinic acid moiety (or a derivative thereof), whis is a cyclitol made up of a cyclohexane ring that bears four hydroxyl groups at positions 1,3.4, and 5, as well as a carboxylic acid at position 1. Quinic Acids and Derivatives Organic Compounds Organooxygen Compounds Alcohols and Polyols Cyclic Alcohols and Derivatives Benzene and Substituted Derivatives Alpha Hydroxy Acids and Derivatives Tertiary Alcohols Secondary Alcohols 1,2-Diols Enolates Carboxylic Acids Polyamines Thioethers hydroxy acid benzene alpha-hydroxy acid tertiary alcohol polyol 1,2-diol secondary alcohol enolate polyamine carboxylic acid carboxylic acid derivative thioether logP 1.8 ALOGPS logS -3.6 ALOGPS Water Solubility 8.93e-02 g/l ALOGPS logP 2.11 ChemAxon IUPAC Name (1R,4R,5R)-1,4,5-trihydroxy-3-[3-(phenylsulfanyl)phenyl]cyclohex-2-ene-1-carboxylic acid ChemAxon Traditional IUPAC Name (1R,4R,5R)-1,4,5-trihydroxy-3-[3-(phenylsulfanyl)phenyl]cyclohex-2-ene-1-carboxylic acid ChemAxon Molecular Weight 358.408 ChemAxon Monoisotopic Weight 358.087494376 ChemAxon SMILES [H][C@@]1(O)C[C@@](O)(C=C(C2=CC=CC(SC3=CC=CC=C3)=C2)[C@@]1([H])O)C(O)=O ChemAxon Molecular Formula C19H18O5S ChemAxon InChI InChI=1S/C19H18O5S/c20-16-11-19(24,18(22)23)10-15(17(16)21)12-5-4-8-14(9-12)25-13-6-2-1-3-7-13/h1-10,16-17,20-21,24H,11H2,(H,22,23)/t16-,17-,19+/m1/s1 ChemAxon InChIKey InChIKey=QMNMNSINKIFYBV-LMMKCTJWSA-N ChemAxon Polar Surface Area (PSA) 97.99 ChemAxon Refractivity 96.26 ChemAxon Polarizability 36.7 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 3.29 ChemAxon pKa (strongest basic) -3.2 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 16058682 PubChem Substance 99444956 ChemSpider 17218400 PDB RP4 BE0001769 3-dehydroquinate dehydratase Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown 3-dehydroquinate dehydratase Amino acid transport and metabolism Catalyzes a trans-dehydration via an enolate intermediate aroQ None 6.41 16682.0 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) GenBank Gene Database AJ001493 GenBank Protein Database 2558614 UniProtKB P15474 UniProt Accession AROQ_STRCO 3-dehydroquinase EC 4.2.1.10 Type II DHQase >3-dehydroquinate dehydratase MPRSLANAPIMILNGPNLNLLGQRQPEIYGSDTLADVEALCVKAAAAHGGTVDFRQSNHE GELVDWIHEARLNHCGIVINPAAYSHTSVAILDALNTCDGLPVVEVHISNIHQREPFRHH SYVSQRADGVVAGCGVQGYVFGVERIAALAGAGSARA >474 bp GTGCCCCGCAGCCTGGCCAACGCCCCGATCATGATCCTCAACGGCCCCAACCTGAACCTG CTCGGCCAGCGCCAGCCGGAGATCTACGGCTCCGACACCCTCGCCGACGTCGAGGCGCTG TGCGTGAAGGCGGCGGCCGCGCACGGCGGCACGGTGGACTTCCGGCAGTCCAACCACGAG GGCGAACTGGTCGACTGGATCCACGAGGCCCGGCTGAACCACTGCGGGATCGTGATCAAC CCCGCCGCCTACTCGCACACGTCCGTCGCCATCCTGGATGCGCTCAACACCTGCGACGGG CTGCCGGTGGTGGAGGTCCACATCTCCAACATCCACCAGCGTGAGCCGTTCCGGCACCAC TCCTACGTCTCGCAGCGCGCCGACGGCGTCGTCGCGGGGTGCGGTGTGCAGGGGTACGTC TTCGGTGTGGAGCGGATCGCCGCCCTGGCCGGGGCGGGCTCGGCCAGGGCCTGA PF01220 DHquinase_II function carbon-oxygen lyase activity function hydro-lyase activity function 3-dehydroquinate dehydratase activity function catalytic activity function lyase activity process amino acid and derivative metabolism process amino acid biosynthesis process aromatic amino acid family biosynthesis process physiological process process metabolism process cellular metabolism process amino acid metabolism "
drug:(1S,4S,5S)-1,4,5-TRIHYDROXY-3-[3-(PHENYLTHIO)PHENYL]CYCLOHEX-2-ENE-1-CARBOXYLIC ACIDrdfs:label"(1S,4S,5S)-1,4,5-TRIHYDROXY-3-[3-(PHENYLTHIO)PHENYL]CYCLOHEX-2-ENE-1-CARBOXYLIC ACID"
drug:(1S,4S,5S)-1,4,5-TRIHYDROXY-3-[3-(PHENYLTHIO)PHENYL]CYCLOHEX-2-ENE-1-CARBOXYLIC ACIDrdf:typedrugbank:drugs
drug:(1S,5S,7R)-N~7~-(BIPHENYL-4-YLMETHYL)-N~3~-HYDROXY-6,8-DIOXA-3-AZABICYCLO[3.2.1]OCTANE-3,7-DICARBOXAMIDEdrugbank:description" experimental This compound belongs to the biphenyls and derivatives. These are organic compounds containing to benzene rings linked together by a C-C bond. Biphenyls and Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Biphenyls and Derivatives Morpholine Carboxylic Acids and Derivatives 1,3-Dioxolanes Tertiary Amines Secondary Carboxylic Acid Amides Enolates Carboxylic Acids Acetals Polyamines morpholine-4-carboxylic acid or derivative morpholine oxazinane meta-dioxolane tertiary amine carboxamide group secondary carboxylic acid amide polyamine carboxylic acid enolate ether acetal carboxylic acid derivative amine organonitrogen compound logP 1.34 ALOGPS logS -2.9 ALOGPS Water Solubility 4.58e-01 g/l ALOGPS logP 1.51 ChemAxon IUPAC Name (1S,5S,7R)-3-N-hydroxy-7-N-[(4-phenylphenyl)methyl]-6,8-dioxa-3-azabicyclo[3.2.1]octane-3,7-dicarboxamide ChemAxon Traditional IUPAC Name (1S,5S,7R)-3-N-hydroxy-7-N-[(4-phenylphenyl)methyl]-6,8-dioxa-3-azabicyclo[3.2.1]octane-3,7-dicarboxamide ChemAxon Molecular Weight 383.3978 ChemAxon Monoisotopic Weight 383.148120797 ChemAxon SMILES [H][C@]12CN(C[C@]([H])(O1)[C@@]([H])(O2)C(=O)NCC1=CC=C(C=C1)C1=CC=CC=C1)C(=O)NO ChemAxon Molecular Formula C20H21N3O5 ChemAxon InChI InChI=1S/C20H21N3O5/c24-19(18-16-11-23(20(25)22-26)12-17(27-16)28-18)21-10-13-6-8-15(9-7-13)14-4-2-1-3-5-14/h1-9,16-18,26H,10-12H2,(H,21,24)(H,22,25)/t16-,17-,18+/m0/s1 ChemAxon InChIKey InChIKey=PPLDARNGJSQINK-OKZBNKHCSA-N ChemAxon Polar Surface Area (PSA) 100.13 ChemAxon Refractivity 99.56 ChemAxon Polarizability 39.77 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 10.04 ChemAxon pKa (strongest basic) -4.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11987860 PubChem Substance 99443497 ChemSpider 10160333 PDB 37A BE0001198 Macrophage metalloelastase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Macrophage metalloelastase Involved in protease activity May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3 MMP12 11q22.3 Cytoplasmic None 8.98 54002.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7158 GenAtlas MMP12 GeneCards MMP12 GenBank Gene Database L23808 GenBank Protein Database 435970 UniProtKB P39900 UniProt Accession MMP12_HUMAN EC 3.4.24.65 HME Macrophage elastase Macrophage metalloelastase precursor Matrix metalloproteinase-12 ME MMP-12 >Macrophage metalloelastase precursor MKFLLILLLQATASGALPLNSSTSLEKNNVLFGERYLEKFYGLEINKLPVTKMKYSGNLM KEKIQEMQHFLGLKVTGQLDTSTLEMMHAPRCGVPDVHHFREMPGGPVWRKHYITYRINN YTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGI LAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTY KYVDINTFRLSADDIRGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFF FKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNLRP EPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITK NFQGIGPKIDAVFYSKNKYYYFFQGSNQFEYDFLLQRITKTLKSNSWFGC >1413 bp ATGAAGTTTCTTCTAATACTGCTCCTGCAGGCCACTGCTTCTGGAGCTCTTCCCCTGAAC AGCTCTACAAGCCTGGAAAAAAATAATGTGCTATTTGGTGAGAGATACTTAGAAAAATTT TATGGCCTTGAGATAAACAAACTTCCAGTGACAAAAATGAAATATAGTGGAAACTTAATG AAGGAAAAAATCCAAGAAATGCAGCACTTCTTGGGTCTGAAAGTGACCGGGCAACTGGAC ACATCTACCCTGGAGATGATGCACGCACCTCGATGTGGAGTCCCCGATCTCCATCATTTC AGGGAAATGCCAGGGGGGCCCGTATGGAGGAAACATTATATCACCTACAGAATCAATAAT TACACACCTGACATGAACCGTGAGGATGTTGACTACGCAATCCGGAAAGCTTTCCAAGTA TGGAGTAATGTTACCCCCTTGAAATTCAGCAAGATTAACACAGGCATGGCTGACATTTTG GTGGTTTTTGCCCGTGGAGCTCATGGAGACTTCCATGCTTTTGATGGCAAAGGTGGAATC CTAGCCCATGCTTTTGGACCTGGATCTGGCATTGGAGGGGATGCACATTTCGATGAGGAC GAATTCTGGACTACACATTCAGGAGGCACAAACTTGTTCCTCACTGCTGTTCACGAGATT GGCCATTCCTTAGGTCTTGGCCATTCTAGTGATCCAAAGGCTGTAATGTTCCCCACCTAC AAATATGTCGACATCAACACATTTCGCCTCTCTGCTGATGACATACGTGGCATTCAGTCC CTGTATGGAGACCCAAAAGAGAACCAACGCTTGCCAAATCCTGACAATTCAGAACCAGCT CTCTGTGACCCCAATTTGAGTTTTGATGCTGTCACTACCGTGGGAAATAAGATCTTTTTC TTCAAAGACAGGTTCTTCTGGCTGAAGGTTTCTGAGAGACCAAAGACCAGTGTTAATTTA ATTTCTTCCTTATGGCCAACCTTGCCATCTGGCATTGAAGCTGCTTATGAAATTGAAGCC AGAAATCAAGTTTTTCTTTTTAAAGATGACAAATACTGGTTAATTAGCAATTTAAGACCA GAGCCAAATTATCCCAAGAGCATACATTCTTTTGGTTTTCCTAACTTTGTGAAAAAAATT GATGCAGCTGTTTTTAACCCACGTTTTTATAGGACCTACTTCTTTGTAGATAACCAGTAT TGGAGGTATGATGAAAGGAGACAGATGATGGACCCTGGTTATCCCAAACTGATTACCAAG AACTTCCAAGGAATCGGGCCTAAAATTGATGCAGTCTTCTATTCTAAAAACAAATACTAC TATTTCTTCCAAGGATCTAACCAATTTGAATATGACTTCCTACTCCAACGTATCACCAAA ACACTGAAAAGCAATAGCTGGTTTGGTTGTTAG PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix component extracellular matrix (sensu Metazoa) function catalytic activity function hydrolase activity function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process "
drug:(1S,5S,7R)-N~7~-(BIPHENYL-4-YLMETHYL)-N~3~-HYDROXY-6,8-DIOXA-3-AZABICYCLO[3.2.1]OCTANE-3,7-DICARBOXAMIDErdfs:label"(1S,5S,7R)-N~7~-(BIPHENYL-4-YLMETHYL)-N~3~-HYDROXY-6,8-DIOXA-3-AZABICYCLO[3.2.1]OCTANE-3,7-DICARBOXAMIDE"
drug:(1S,5S,7R)-N~7~-(BIPHENYL-4-YLMETHYL)-N~3~-HYDROXY-6,8-DIOXA-3-AZABICYCLO[3.2.1]OCTANE-3,7-DICARBOXAMIDErdf:typedrugbank:drugs
drug:(1S,6BR,9AS,11R,11BR)-9A,11B-DIMETHYL-1-[(METHYLOXY)METHYL]-3,6,9-TRIOXO-1,6,6B,7,8,9,9A,10,11,11B-DECAHYDRO-3H-FURO[4,3,2-DE]INDENO[4,5-H][2]BENZOPYRAN-11-YL ACETATEdrugbank:description" experimental This compound belongs to the other steroids and derivatives. Other Steroids and Derivatives Organic Compounds Lipids Steroids and Steroid Derivatives Other Steroids and Derivatives Oxasteroids and Derivatives Naphthopyrans Naphthalenes Furopyrans Pyrans Furans Ketones Carboxylic Acid Esters Enolates Dialkyl Ethers Polyamines naphthopyran naphthalene acene furopyran pyran furan carboxylic acid ester ketone ether dialkyl ether polyamine enolate carboxylic acid derivative carbonyl group logP 2.31 ALOGPS logS -3.5 ALOGPS Water Solubility 1.21e-01 g/l ALOGPS logP 1.44 ChemAxon IUPAC Name (1R,3R,5S,9R,18S)-18-(methoxymethyl)-1,5-dimethyl-6,11,16-trioxo-13,17-dioxapentacyclo[10.6.1.0^{2,10}.0^{5,9}.0^{15,19}]nonadeca-2(10),12(19),14-trien-3-yl acetate ChemAxon Traditional IUPAC Name wortmannin ChemAxon Molecular Weight 428.4319 ChemAxon Monoisotopic Weight 428.147117744 ChemAxon SMILES [H][C@@]12CCC(=O)[C@@]1(C)C[C@@]([H])(OC(C)=O)C1=C2C(=O)C2=C3C(=CO2)C(=O)O[C@]([H])(COC)[C@]13C ChemAxon Molecular Formula C23H24O8 ChemAxon InChI InChI=1S/C23H24O8/c1-10(24)30-13-7-22(2)12(5-6-14(22)25)16-18(13)23(3)15(9-28-4)31-21(27)11-8-29-20(17(11)23)19(16)26/h8,12-13,15H,5-7,9H2,1-4H3/t12-,13+,15+,22-,23-/m0/s1 ChemAxon InChIKey InChIKey=QDLHCMPXEPAAMD-QAIWCSMKSA-N ChemAxon Polar Surface Area (PSA) 109.11 ChemAxon Refractivity 106.86 ChemAxon Polarizability 42.99 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest acidic) 19.67 ChemAxon pKa (strongest basic) -4.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 5 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 312145 PubChem Substance 99444530 ChemSpider 276037 PDB KWT BE0001315 Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform Involved in phosphotransferase activity, alcohol group as acceptor 3-phosphorylates the cellular phosphoinositide PtdIns- 4,5-biphosphate (PtdIns(4,5)P2) to produce PtdIns-3, 4,5- triiphosphate (PtdIns(3,4,5)P3). Links G-protein coupled receptor activation to the secondary messenger PtdIns(3,4,5)P3 production PIK3CG 7q22.3 None 7.53 126455.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:8978 GenAtlas PIK3CG GeneCards PIK3CG GenBank Gene Database X83368 GenBank Protein Database 1507822 UniProtKB P48736 UniProt Accession PK3CG_HUMAN EC 2.7.1.153 p120-PI3K PI3-kinase p110 subunit gamma PI3K PI3Kgamma PtdIns-3- kinase subunit p110 >Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform MELENYKQPVVLREDNCRRRRRMKPRSAAASLSSMELIPIEFVLPTSQRKCKSPETALLH VAGHGNVEQMKAQVWLRALETSVAADFYHRLGPHHFLLLYQKKGQWYEIYDKYQVVQTLD CLRYWKATHRSPGQIHLVQRHPPSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGL VTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDT PGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNG EEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRK FRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKI KDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEY VLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEG DRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQ QEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYL LQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAY LRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLP ESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQ DMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTG AFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNL FHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLAL RHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGW TVQFNWFLHLVLGIKQGEKHSA >3306 bp ATGGAGCTGGAGAACTATAAACAGCCCGTGGTGCTGAGAGAGGACAACTGCCGAAGGCGC CGGAGGATGAAGCCGCGCAGTGCTGCCAGCCTGTCCTCCATGGAGCTCATCCCCATCGAG TTCGTGCTGCCCACCAGCCAGCGCAAATGCAAGAGCCCCGAAACGGCGCTGCTGCACGTG GCCGGCCACGGCAACGTGGAGCAGATGAAGGCCCAGGTGTGGCTGCGAGCGCTGGAGACC AGCGTGGCGGCGGACTTCTACCACCGGCTGGGACCGCATCACTTCCTCCTGCTCTATCAG AAGAAGGGGCAGTGGTACGAGATCTACGACAAGTACCAGGTGGTGCAGACTCTGGACTGC CTGCGCTACTGGAAGGCCACGCACCGGAGCCCGGGCCAGATCCACCTGGTGCAGCGGCAC CCGCCCTCCGAGGAGTCCCAAGCCTTCCAGCGGCAGCTCACGGCGCTGATTGGCTATGAC GTCACTGACGTCAGCAACGTGCACGACGATGAGCTGGAGTTCACGCGCCGTGGCTTGGTG ACCCCGCGCATGGCGGAGGTGGCCAGCCGCGACCCCAAGCTCTACGCCATGCACCCGTGG GTGACGTCCAAGCCCCTCCCGGAGTACCTGTGGAAGAAGATTGCCAACAACTGCATCTTC ATCGTCATTCACCGCAGCACCACCAGCCAGACCATTAAGGTCTCACCCGACGACACCCCC GGCGCCATCCTGCAGAGCTTCTTCACCAAGATGGCCAAGAAGAAATCTCTGATGGATATT CCCGAAAGCCAAAGCGAACAGGATTTTGTGCTGCGCGTCTGTGGCCGGGATGAGTACCTG GTGGGCGAAACGCCCATCAAAAACTTCCAGTGGGTGAGGCACTGCCTCAAGAACGGAGAA GAGATTCACGTGGTACTGGACACGCCTCCAGACCCGGCCCTAGACGAGGTGAGGAAGGAA GAGTGGCCGCTGGTGGACGACTGCACGGGAGTCACCGGCTACCATGAGCAGCTTACCATC CACGGCAAGGACCACGAGAGTGTGTTCACCGTGTCCCTGTGGGACTGCGACCGCAAGTTC AGGGTCAAGATCAGAGGCATTGATATCCCCGTCCTGCCTCGGAACACCGACCTCACAGTT TTTGTAGAGGCAAACATCCAGCATGGGCAACAAGTCCTTTGCCAAAGGAGAACCAGCCCC AAACCCTTCACAGAGGAGGTGCTGTGGAATGTGTGGCTTGAGTTCAGTATCAAAATCAAA GACTTGCCCAAAGGGGCTCTACTGAACCTCCAGATCTACTGCGGTAAAGCTCCAGCACTG TCCAGCAAGGCCTCTGCAGAGTCCCCCAGTTCTGAGTCCAAGGGCAAAGTTCGGCTTCTC TATTATGTGAACCTGCTGCTGATAGACCACCGTTTCCTCCTGCGCCGTGGAGAATACGTC CTCCACATGTGGCAGATATCTGGGAAGGGAGAAGACCAAGGAAGCTTCAATGCTGACAAA CTCACGTCTGCAACTAACCCAGACAAGGAGAACTCAATGTCCATCTCCATTCTTCTGGAC AATTACTGCCACCCGATAGCCCTGCCTAAGCATCAGCCCACCCCTGACCCGGAAGGGGAC CGGGTTCGAGCAGAAATGCCCAACCAGCTTCGCAAGCAATTGGAGGCGATCATAGCCACT GATCCACTTAACCCTCTCACAGCAGAGGACAAAGAATTGCTCTGGCATTTTAGATACGAA AGCCTTAAGCACCCAAAAGCATATCCTAAGCTATTTAGTTCAGTGAAATGGGGACAGCAA GAAATTGTGGCCAAAACATACCAATTGTTGGCCAGAAGGGAAGTCTGGGATCAAAGTGCT TTGGATGTTGGGTTAACAATGCAGCTCCTGGACTGCAACTTCTCAGATGAAAATGTAAGA GCCATTGCAGTTCAGAAACTGGAGAGCTTGGAGGACGATGATGTTCTGCATTACCTTCTA CAATTGGTCCAGGCTGTGAAATTTGAACCATACCATGATAGCGCCCTTGCCAGATTTCTG CTGAAGCGTGGTTTAAGAAACAAAAGAATTGGTCACTTTTTGTTTTGGTTCTTGAGAAGT GAGATAGCCCAGTCCAGACACTATCAGCAGAGGTTCGCTGTGATTCTGGAAGCCTATCTG AGGGGCTGTGGCACAGCCATGCTGCACGACTTTACCCAACAAGTCCAAGTAATCGAGATG TTACAAAAAGTCACCCTTGATATTAAATCGCTCTCTGCTGAAAAGTATGACGTCAGTTCC CAAGTTATTTCACAACTTAAACAAAAGCTTGAAAACCTGCAGAATTCTCAACTCCCCGAA AGCTTTAGAGTTCCATATGATCCTGGACTGAAAGCAGGAGCGCTGGCAATTGAAAAATGT AAAGTAATGGCCTCCAAGAAAAAACCACTATGGCTTGAGTTTAAATGTGCCGATCCTACA GCCCTATCAAATGAAACAATTGGAATTATCTTTAAACATGGTGATGATCTGCGCCAAGAC ATGCTTATTTTACAGATTCTACGAATCATGGAGTCTATTTGGGAGACTGAATCTTTGGAT CTATGCCTCCTGCCATATGGTTGCATTTCAACTGGTGACAAAATAGGAATGATCGAGATT GTGAAAGACGCCACGACAATTGCCAAAATTCAGCAAAGCACAGTGGGCAACACGGGAGCA TTTAAAGATGAAGTCCTGAATCACTGGCTCAAAGAAAAATCCCCTACTGAAGAAAAGTTT CAGGCAGCAGTGGAGAGATTTGTTTATTCCTGTGCAGGCTACTGTGTGGCAACCTTTGTT CTTGGAATAGGCGACAGACACAATGACAATATTATGATCACCGAGACAGGAAACCTATTT CATATTGACTTCGGGCACATTCTTGGGAATTACAAAAGTTTCCTGGGCATTAATAAAGAG AGAGTGCCATTTGTGCTAACCCCTGACTTCCTCTTTGTGATGGGAACTTCTGGAAAGAAG ACAAGCCCACACTTCCAGAAATTTCAGGACATCTGTGTTAAGGCTTATCTAGCCCTTCGT CATCACACAAACCTACTGATCATCCTGTTCTCCATGATGCTGATGACAGGAATGCCCCAG TTAACAAGCAAAGAAGACATTGAATATATCCGGGATGCCCTCACAGTGGGGAAAAATGAG GAGGATGCTAAAAAGTATTTTCTTGATCAGATCGAAGTTTGCAGAGACAAAGGATGGACT GTGCAGTTTAATTGGTTTCTACATCTTGTTCTTGGCATCAAACAAGGAGAGAAACATTCA GCCTAA PF00454 PI3_PI4_kinase PF00792 PI3K_C2 PF00794 PI3K_rbd PF00613 PI3Ka component protein complex component phosphoinositide 3-kinase complex function transferase activity function transferase activity, transferring phosphorus-containing groups function kinase activity function phosphotransferase activity, alcohol group as acceptor function lipid kinase activity function phosphoinositide 3-kinase activity function phosphatidylinositol 3-kinase activity function inositol or phosphatidylinositol kinase activity function catalytic activity BE0003745 Serine/threonine-protein kinase PLK1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Serine/threonine-protein kinase PLK1 Involved in ATP binding Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of APC/C inhibitors, and the regulation of mitotic exit and cytokinesis PLK1 16p12.2 Nucleus None 9.19 68254.0 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9077 GeneCards PLK1 GenBank Gene Database U01038 GenBank Protein Database 393017 UniProtKB P53350 UniProt Accession PLK1_HUMAN PLK-1 Polo-like kinase 1 Serine/threonine-protein kinase 13 STPK13 >Serine/threonine-protein kinase PLK1 MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLG KGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFF EDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLG NLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCI MYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELL NDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERPREKEE PVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDK YGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLK YFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTK LILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRL KAS >1812 bp ATGACTGCAGCGGTGACTGCGGGGAAGCTGCCACGGGCACCGGCCGACCCTGGGAAAGCC GGGGTCCCCGGAGTTGCAGCTCCCGGAGCTCCGGCGGCGGCTCCACCGGCGAAAGAGATC CCGGAGGTCCTAGTGGACCCACGCAGCCGGCGGCGCTATGTGCGGGGCCGCCTTTTGAGC AAGGGCGGCTTTGCCAAGTGCTTCGAGATCTCGGACGCGGACACCAAGGAGGTGTTCGCG GGCAAGATTGTGCCTAAGTCTCTGCTGCTCAAGCCGCACCAGAGGGAGAAGATGTCCATG GAAATATCCATTCACCGCAGCCTCGCCCACCAGCACGTCGTAGGATTCCACGGCTTTTTC GAGGACAACGACTTCGTGTTCGTGGTGTTGGAGCTCTGCCGCCGGAGGTCTCTCCTGGAG CTGCACAAGAGGAGGAAAGCCCTGACTGAGCCTGAGGCCCGATACTACCTACGGCAAATT GTGCTTGGCTGCCAGTACCTGCACCGAAACCGAGTTATTCATCGAGACCTCAAGCTGGGC AACCTTTTCCTGAATGAAGATCTGGAGGTGAAAATAGGGGATTTTGGACTGGCAACCAAA GTCGAATATGACGGGGAGAGGAAGAAGACCCTGTGTGGGACTCCTAATTACATAGCTCCC GAGGTGCTGAGCAAGAAAGGGCACAGTTTCGAGGTGGATGTGTGGTCCATTGGGTGTATC ATGTATACCTTGTTAGTGGGCAAACCACCTTTTGAGACTTCTTGCCTAAAAGAGACCTAC CTCCGGATCAAGAAGAATGAATACAGTATTCCCAAGCACATCAACCCCGTGGCCGCCTCC CTCATCCAGAAGATGCTTCAGACAGATCCCACTGCCCGCCCAACCATTAACGAGCTGCTT AATGACGAGTTCTTTACTTCTGGCTATATCCCTGCCCGTCTCCCCATCACCTGCCTGACC ATTCCACCAAGGTTTTCGATTGCTCCCAGCAGCCTGGACCCCAGCAACCGGAAGCCCCTC ACAGTCCTCAATAAAGGCTTGGAGAACCCCCTGCCTGAGCGTCCCCGGGAAAAAGAAGAA CCAGTGGTTCGAGAGACAGGTGAGGTGGTCGACTGCCACCTCAGTGACATGCTGCAGCAA CTGCACAGTGTCAATGCCTCCAAGCCCTCGGAGCGTGGGCTGGTCAGGCAAGAGGAGGCT GAGGATCCTGCCTGCATCCCCATCTTCTGGGTCAGCAAGTGGGTGGACTATTCGGACAAG TACGGCCTTGGGTATCAGCTCTGTGATAACAGCGTGGGGGTGCTCTTCAATGACTCAACA CGCCTCATCCTCTACAATGATGGTGACAGCCTGCAGTACATAGAGCGTGACGGCACTGAG TCCTACCTCACCGTGAGTTCCCATCCCAACTCCTTGATGAAGAAGATCACCCTCCTTAAA TATTTCCGCAATTACATGAGCGAGCACTTGCTGAAGGCAGGTGCCAACATCACGCCGCGC GAAGGTGATGAGCTCGCCCGGCTGCCCTACCTACGGACCTGGTTCCGCACCCGCAGCGCC ATCATCCTGCACCTCAGCAACGGCAGCGTGCAGATCAACTTCTTCCAGGATCACACCAAG CTCATCTTGTGCCCACTGATGGCAGCCGTGACCTACATCGACGAGAAGCGGGACTTCCGC ACATACCGCCTGAGTCTCCTGGAGGAGTACGGCTGCTGCAAGGAGCTGGCCAGCCGGCTC CGCTACGCCCGCACTATGGTGGACAAGCTGCTGAGCTCACGCTCGGCCAGCAACCGTCTC AAGGCCTCCTAA PF00069 Pkinase PF00659 POLO_box function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function protein binding function transferase activity function catalytic activity function ATP binding function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process physiological process process metabolism process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein amino acid phosphorylation process protein modification BE0000955 Phosphatidylinositol 3-kinase regulatory subunit alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Phosphatidylinositol 3-kinase regulatory subunit alpha Replication, recombination and repair Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues PIK3R1 5q13.1 Cytoplasmic None 6.06 83599.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:8979 GenAtlas PIK3R1 GeneCards PIK3R1 GenBank Gene Database M61906 UniProtKB P27986 UniProt Accession P85A_HUMAN PI3-kinase p85-subunit alpha PI3K PtdIns-3-kinase p85-alpha >Phosphatidylinositol 3-kinase regulatory subunit alpha MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEEIGWLNGYN ETTGERGDFPGTYVEYIGRKKISPPTPKPRPPRPLPVAPGSSKTEADVEQQALTLPDLAE QFAPPDIAPPLLIKLVEAIEKKGLECSTLYRTQSSSNLAELRQLLDCDTPSVDLEMIDVH VLADAFKRYLLDLPNPVIPAAVYSEMISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTL QYLLKHFFKLSQTSSKNLLNARVLSEIFSPMLFRFSAASSDNTENLIKVIEILISTEWNE RQPAPALPPKPPKPTTVANNGMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDA STKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFSSVVELINHYRNESLAQYNPKL DVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMK RTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEIQRIMHNYDKLKSRISEIID SRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGN ENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACS VVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYA QQRR PF00017 SH2 PF00018 SH3_1 PF00620 RhoGAP component phosphoinositide 3-kinase complex component protein complex function phosphatidylinositol 3-kinase activity function transferase activity function hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides function pyrophosphatase activity function nucleoside-triphosphatase activity function GTPase activity function transferase activity, transferring phosphorus-containing groups function binding function kinase activity function catalytic activity function hydrolase activity function guanyl nucleotide binding function lipid kinase activity function nucleotide binding function GTP binding function phosphoinositide 3-kinase activity function purine nucleotide binding function hydrolase activity, acting on acid anhydrides process cellular process process cell communication process signal transduction process response to stimulus process response to biotic stimulus process defense response process intracellular signaling cascade process immune response BE0002379 Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform Involved in phosphotransferase activity, alcohol group as acceptor Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2 PIK3CA 3q26.3 None 7.23 124286.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:8975 GenAtlas PIK3CA GeneCards PIK3CA GenBank Gene Database Z29090 UniProtKB P42336 UniProt Accession PK3CA_HUMAN EC 2.7.1.153 PI3-kinase p110 subunit alpha PI3K PtdIns-3- kinase p110 >Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLITIKHELFKEARKYPLHQ LLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFA IGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKH IYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLK LCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMD CFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGI YHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHC PLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWF SSVVKFPDMSVIEEHANWSVSREAGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPL SEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAME LLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTN QRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILK QEKKDETQKVQMKFLVEQMRRPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLW LNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLS IGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRS CAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDF LIVISKGAQECTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIA YIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDWIFHTIKQHALN >3207 bp ATGCCTCCAAGACCATCATCAGGTGAACTGTGGGGCATCCACTTGATGCCCCCAAGAATC CTAGTGGAATGTTTACTACCAAATGGAATGATAGTGACTTTAGAATGCCTCCGTGAGGCT ACATTAGTAACTATAAAGCATGAACTATTTAAAGAAGCAAGAAAATACCCTCTCCATCAA CTTCTTCAAGATGAATCTTCTTACATTTTCGTAAGTGTTACCCAAGAAGCAGAAAGGGAA GAATTTTTTGATGAAACAAGACGACTTTGTGATCTTCGGCTTTTTCAACCATTTTTAAAA GTAATTGAACCAGTAGGCAACCGTGAAGAAAAGATCCTCAATCGAGAAATTGGTTTTGCT ATCGGCATGCCAGTGTGCGAATTTGATATGGTTAAAGATCCTGAAGTACAGGACTTCCGA AGAAATATTCTTAATGTTTGTAAAGAAGCTGTGGATCTTAGGGATCTTAATTCACCTCAT AGTAGAGCAATGTATGTCTATCCGCCACATGTAGAATCTTCACCAGAGCTGCCAAAGCAC ATATATAATAAATTGGATAGAGGCCAAATAATAGTGGTGATTTGGGTAATAGTTTCTCCA AATAATGACAAGCAGAAGTATACTCTGAAAATCAACCATGACTGTGTGCCAGAACAAGTA ATTGCTGAAGCAATCAGGAAAAAAACTAGAAGTATGTTGCTATCATCTGAACAATTAAAA CTCTGTGTTTTAGAATATCAGGGCAAGTACATTTTAAAAGTGTGTGGATGTGATGAATAC TTCCTAGAAAAATATCCTCTGAGTCAGTATAAGTATATAAGAAGCTGTATAATGCTTGGG AGGATGCCCAATTTGAAGATGATGGCTAAAGAAAGCCTTTATTCTCAACTGCCAATGGAC TGTTTTACAATGCCATCTTATTCCAGACGCATTTCCACAGCTACACCATATATGAATGGA GAAACATCTACAAAATCCCTTTGGGTTATAAATAGAGCACTCAGAATAAAAATTCTTTGT GCAACCTACGTGAATCTAAATATTCGAGACATTGACAAGATTTATGTTCGAACAGGTATC TACCATGGAGGAGAACCCTTATGTGACAATGTGAACACTCAAAGAGTACCTTGTTCCAAT CCCAGGTGGAATGAATGGCTGAATTATGATATATACATTCCTGATCTTCCTCGTGCTGCT CGACTTTGCCTTTCCATTTGCTCTGTTAAAGGCCGAAAGGGTGCTAAAGAGGAACACTGT CCATTGGCATGGGGAAATATAAACTTGTTTGATTACACAGACACTCTAGTATCTGGAAAA ATGGCTTTGAATCTTTGGCCAGTACCTCATGGATTAGAAGATTTGCTGAACCCTATTGGT GTTACTGGATCAAATCCAAATAAAGAAACTCCATGCTTAGAGTTGGAGTTTGACTGGTTC AGCAGTGTGGTAAAGTTCCCAGATATGTCAGTGATTGAAGAGCATGCCAATTGGTCTGTA TCCCGAGAAGCAGGATTTAGCTATTCCCACGCAGGACTGAGTAACAGACTAGCTAGAGAC AATGAATTAAGGGAAAATGACAAAGAACAGCTCAAAGCAATTTCTACACGAGATCCTCTC TCTGAAATCACTGAGCAGGAGAAAGATTTTCTATGGAGTCACAGACACTATTGTGTAACT ATCCCCGAAATTCTACCCAAATTGCTTCTGTCTGTTAAATGGAATTCTAGAGATGAAGTA GCCCAGATGTATTGCTTGGTAAAAGATTGGCCTCCAATCAAACCTGAACAGGCTATGGAA CTTCTGGACTGTAATTACCCAGATCCTATGGTTCGAGGTTTTGCTGTTCGGTGCTTGGAA AAATATTTAACAGATGACAAACTTTCTCAGTATTTAATTCAGCTAGTACAGGTCCTAAAA TATGAACAATATTTGGATAACTTGCTTGTGAGATTTTTACTGAAGAAAGCATTGACTAAT CAAAGGATTGGGCACTTTTTCTTTTGGCATTTAAAATCTGAGATGCACAATAAAACAGTT AGCCAGAGGTTTGGCCTGCTTTTGGAGTCCTATTGTCGTGCATGTGGGATGTATTTGAAG CACCTGAATAGGCAAGTCGAGGCAATGGAAAAGCTCATTAACTTAACTGACATTCTCAAA CAGGAGAGGAAGGATGAAACACAAAAGGTACAGATGAAGTTTTTAGTTGAGCAAATGAGG CGACCAGATTTCATGGATGCCCTACAGGGCTTGCTGTCTCCTCTAAACCCTGCTCATCAA CTAGGAAACCTCAGGCTTAAAGAGTGTCGAATTATGTCTTCTGCAAAAAGGCCACTGTGG TTGAATTGGGAGAACCCAGACATCATGTCAGAGTTACTGTTTCAGAACAATGAGATCATC TTTAAAAATGGGGATGATTTACGGCAAGATATGCTAACACTTCAAATTATTCGTATTATG GAAAATATCTGGCAAAATCAAGGTCTTGATCTTCGAATGTTACCTTATGGTTGTCTGTCA ATCGGTGACTGTGTGGGACTTATTGAGGTGGTGCGAAATTCTCACACTATTATGCAAATT CAGTGCAAAGGCGGCTTGAAAGGTGCACTGCAGTTCAACAGCCACACACTACATCAGTGG CTCAAAGACAAGAACAAAGGAGAAATATATGATGCAGCCATTGACCTGTTTACACGTTCA TGTGCTGGATACTGTGTAGCTACCTTCATTTTGGGAATTGGAGATCGTCACAATAGTAAC ATCATGGTGAAAGACGATGGACAACTGTTTCATATAGATTTTGGACACTTTTTGGATCAC AAGAAGAAAAAATTTGGTTATAAACGAGAACGTGTGCCATTTGTTTTGACACAGGATTTC TTAATAGTGATTAGTAAAGGAGCCCAAGAATGCACAAAGACAAGAGAATTTGAGAGGTTT CAGGAGATGTGTTACAAGGCTTATCTAGCTATTCGACAGCATGCCAATCTCTTCATAAAT CTTTTCTCAATGATGCTTGGCTCTGGAATGCCAGAACTACAATCTTTTGATGACATTGCA TACATTCGAAAGACCCTAGCCTTAGATAAAACTGAGCAAGAGGCTTTGGAGTATTTCATG AAACAAATGAATGATGCACATCATGGTGGCTGGACAACAAAAATGGATTGGATCTTCCAC ACAATTAAACAGCATGCATTGAACTGA PF00454 PI3_PI4_kinase PF00792 PI3K_C2 PF00794 PI3K_rbd PF00613 PI3Ka PF02192 PI3K_p85B component phosphoinositide 3-kinase complex component protein complex function transferase activity function inositol or phosphatidylinositol kinase activity function transferase activity, transferring phosphorus-containing groups function kinase activity function phosphotransferase activity, alcohol group as acceptor function lipid kinase activity function phosphoinositide 3-kinase activity function catalytic activity function phosphatidylinositol 3-kinase activity process cellular process process cell communication process signal transduction "
drug:(1S,6BR,9AS,11R,11BR)-9A,11B-DIMETHYL-1-[(METHYLOXY)METHYL]-3,6,9-TRIOXO-1,6,6B,7,8,9,9A,10,11,11B-DECAHYDRO-3H-FURO[4,3,2-DE]INDENO[4,5-H][2]BENZOPYRAN-11-YL ACETATErdfs:label"(1S,6BR,9AS,11R,11BR)-9A,11B-DIMETHYL-1-[(METHYLOXY)METHYL]-3,6,9-TRIOXO-1,6,6B,7,8,9,9A,10,11,11B-DECAHYDRO-3H-FURO[4,3,2-DE]INDENO[4,5-H][2]BENZOPYRAN-11-YL ACETATE"
drug:(1S,6BR,9AS,11R,11BR)-9A,11B-DIMETHYL-1-[(METHYLOXY)METHYL]-3,6,9-TRIOXO-1,6,6B,7,8,9,9A,10,11,11B-DECAHYDRO-3H-FURO[4,3,2-DE]INDENO[4,5-H][2]BENZOPYRAN-11-YL ACETATErdf:typedrugbank:drugs
drug:(1S,6R)-3-{[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]CARBONYL}-6-(2,4,5-TRIFLUOROPHENYL)CYCLOHEX-3-EN-1-AMINEdrugbank:description" experimental This compound belongs to the gamma amino acids and derivatives. These are amino acids having a (-NH2) group attached to the gamma carbon atom. Gamma Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Triazolopyrazines Fluorobenzenes Pyrazines Aryl Fluorides Tertiary Carboxylic Acid Amides Triazoles Tertiary Amines Carboxylic Acids Polyamines Enolates Organofluorides Monoalkylamines Alkyl Fluorides triazolopyrazine fluorobenzene aryl halide aryl fluoride benzene pyrazine 1,2,4-triazole azole triazole tertiary carboxylic acid amide carboxamide group tertiary amine carboxylic acid polyamine enolate primary amine amine organohalogen primary aliphatic amine organofluoride alkyl halide alkyl fluoride organonitrogen compound logP 2.29 ALOGPS logS -4.5 ALOGPS Water Solubility 1.41e-02 g/l ALOGPS logP 1.84 ChemAxon IUPAC Name (1S,6R)-3-{[3-(trifluoromethyl)-5H,6H,7H,8H-[1,2,4]triazolo[4,3-a]pyrazin-7-yl]carbonyl}-6-(2,4,5-trifluorophenyl)cyclohex-3-en-1-amine ChemAxon Traditional IUPAC Name (1S,6R)-3-{[3-(trifluoromethyl)-5H,6H,8H-[1,2,4]triazolo[4,3-a]pyrazin-7-yl]carbonyl}-6-(2,4,5-trifluorophenyl)cyclohex-3-en-1-amine ChemAxon Molecular Weight 445.3616 ChemAxon Monoisotopic Weight 445.133729421 ChemAxon SMILES [H][C@]1(N)CC(=CC[C@]1([H])C1=CC(F)=C(F)C=C1F)C(=O)N1CCN2C(C1)=NN=C2C(F)(F)F ChemAxon Molecular Formula C19H17F6N5O ChemAxon InChI InChI=1S/C19H17F6N5O/c20-12-7-14(22)13(21)6-11(12)10-2-1-9(5-15(10)26)17(31)29-3-4-30-16(8-29)27-28-18(30)19(23,24)25/h1,6-7,10,15H,2-5,8,26H2/t10-,15+/m1/s1 ChemAxon InChIKey InChIKey=NVVSPGQEXMJZIR-BMIGLBTASA-N ChemAxon Polar Surface Area (PSA) 77.04 ChemAxon Refractivity 100.37 ChemAxon Polarizability 38.82 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 9.64 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11974440 PubChem Substance 99444515 ChemSpider 10147795 PDB KIQ BE0000854 Dipeptidyl peptidase 4 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dipeptidyl peptidase 4 Amino acid transport and metabolism Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Plays a role in T-cell activation DPP4 2q24.3 Cell membrane; single-pass type II membrane protein. Processed form:Secreted protein. Note=Also exis 7-28 5.92 88279.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3009 GenAtlas DPP4 GeneCards DPP4 GenBank Gene Database U13735 GenBank Protein Database 535388 UniProtKB P27487 UniProt Accession DPP4_HUMAN ADABP Adenosine deaminase complexing protein 2 Dipeptidyl peptidase IV DPP IV EC 3.4.14.5 T-cell activation antigen CD26 TP103 >Dipeptidyl peptidase 4 MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSL RWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNY VKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNL PSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYL CDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPS EPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISN EYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKY PLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGT FEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWE YYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP >2301 bp ATGAAGACACCGTGGAAGGTTCTTCTGGGACTGCTGGGTGCTGCTGCGCTTGTCACCATC ATCACCGTGCCCGTGGTTCTGCTGAACAAAGGCACAGATGATGCTACAGCTGACAGTCGC AAAACTTACACTCTAACTGATTACTTAAAAAATACTTATAGACTGAAGTTATACTCCTTA AGATGGATTTCAGATCATGAATATCTCTACAAACAAGAAAATAATATCTTGGTATTCAAT GCTGAATATGGAAACAGCTCAGTTTTCTTGGAGAACAGTACATTTGATGAGTTTGGACAT TCTATCAATGATTATTCAATATCTCCTGATGGGCAGTTTATTCTCTTAGAATACAACTAC GTGAAGCAATGGAGGCATTCCTACACAGCTTCATATGACATTTATGATTTAAATAAAAGG CAGCTGATTACAGAAGAGAGGATTCCAAACAACACACAGTGGGTCACATGGTCACCAGTG GGTCATAAATTGGCATATGTTTGGAACAATGACATTTATGTTAAAATTGAACCAAATTTA CCAAGTTACAGAATCACATGGACGGGGAAAGAAGATATAATATATAATGGAATAACTGAC TGGGTTTATGAAGAGGAAGTCTTCAGTGCCTACTCTGCTCTGTGGTGGTCTCCAAACGGC ACTTTTTTAGCATATGCCCAATTTAACGACACAGAAGTCCCACTTATTGAATACTCCTTC TACTCTGATGAGTCACTGCAGTACCCAAAGACTGTACGGGTTCCATATCCAAAGGCAGGA GCTGTGAATCCAACTGTAAAGTTCTTTGTTGTAAATACAGACTCTCTCAGCTCAGTCACC AATGCAACTTCCATACAAATCACTGCTCCTGCTTCTATGTTGATAGGGGATCACTACTTG TGTGATGTGACATGGGCAACACAAGAAAGAATTTCTTTGCAGTGGCTCAGGAGGATTCAG AACTATTCGGTCATGGATATTTGTGACTATGATGAATCCAGTGGAAGATGGAACTGCTTA GTGGCACGGCAACACATTGAAATGAGTACTACTGGCTGGGTTGGAAGATTTAGGCCTTCA GAACCTCATTTTACCCTTGATGGTAATAGCTTCTACAAGATCATCAGCAATGAAGAAGGT TACAGACACATTTGCTATTTCCAAATAGATAAAAAAGACTGCACATTTATTACAAAAGGC ACCTGGGAAGTCATCGGGATAGAAGCTCTAACCAGTGATTATCTATACTACATTAGTAAT GAATATAAAGGAATGCCAGGAGGAAGGAATCTTTATAAAATCCAACTTAGTGACTATACA AAAGTGACATGCCTCAGTTGTGAGCTGAATCCGGAAAGGTGTCAGTACTATTCTGTGTCA TTCAGTAAAGAGGCGAAGTATTATCAGCTGAGATGTTCCGGTCCTGGTCTGCCCCTCTAT ACTCTACACAGCAGCGTGAATGATAAAGGGCTGAGAGTCCTGGAAGACAATTCAGCTTTG GATAAAATGCTGCAGAATGTCCAGATGCCCTCCAAAAAACTGGACTTCATTATTTTGAAT GAAACAAAATTTTGGTATCAGATGATCTTGCCTCCTCATTTTGATAAATCCAAGAAATAT CCTCTACTATTAGATGTGTATGCAGGCCCATGTAGTCAAAAAGCAGACACTGTCTTCAGA CTGAACTGGGCCACTTACCTTGCAAGCACAGAAAACATTATAGTAGCTAGCTTTGATGGC AGAGGAAGTGGTTACCAAGGAGATAAGATCATGCATGCAATCAACAGAAGACTGGGAACA TTTGAAGTTGAAGATCAAATTGAAGCAGCCAGACAATTTTCAAAAATGGGATTTGTGGAC AACAAACGAATTGCAATTTGGGGCTGGTCATATGGAGGGTACGTAACCTCAATGGTCCTG GGATCGGGAAGTGGCGTGTTCAAGTGTGGAATAGCCGTGGCGCCTGTATCCCGGTGGGAG TACTATGACTCAGTGTACACAGAACGTTACATGGGTCTCCCAACTCCAGAAGACAACCTT GACCATTACAGAAATTCAACAGTCATGAGCAGAGCTGAAAATTTTAAACAAGTTGAGTAC CTCCTTATTCATGGAACAGCAGATGATAACGTTCACTTTCAGCAGTCAGCTCAGATCTCC AAAGCCCTGGTCGATGTTGGAGTGGATTTCCAGGCAATGTGGTATACTGATGAAGACCAT GGAATAGCTAGCAGCACAGCACACCAACATATATATACCCACATGAGCCACTTCATAAAA CAATGTTTCTCTTTACCTTAG PF00930 DPPIV_N PF00326 Peptidase_S9 component cell component membrane function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function serine-type peptidase activity function hydrolase activity function dipeptidyl-peptidase IV activity function prolyl oligopeptidase activity process protein metabolism process cellular protein metabolism process physiological process process proteolysis process metabolism process macromolecule metabolism "
drug:(1S,6R)-3-{[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]CARBONYL}-6-(2,4,5-TRIFLUOROPHENYL)CYCLOHEX-3-EN-1-AMINErdfs:label"(1S,6R)-3-{[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]CARBONYL}-6-(2,4,5-TRIFLUOROPHENYL)CYCLOHEX-3-EN-1-AMINE"
drug:(1S,6R)-3-{[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]CARBONYL}-6-(2,4,5-TRIFLUOROPHENYL)CYCLOHEX-3-EN-1-AMINErdf:typedrugbank:drugs
drug:(1S,7S,8S,8AR)-1,2,3,7,8,8A-HEXAHYDRO-7-METHYL-8-[2-[(2R,4R)-TETRAHYDRO-4-HY DROXY-6-OXO-2H-PYRAN-2-YL]ETHYL]-1-NAPHTHALENOLdrugbank:description" experimental This compound belongs to the delta valerolactones. These are cyclic organic compounds containing a 1-hydroxy-3,4,5,6-tetrahydro-1,2-thiazin-1- one moiety. Delta Valerolactones Organic Compounds Heterocyclic Compounds Lactones Delta Valerolactones Oxanes Secondary Alcohols Carboxylic Acid Esters Polyamines oxane secondary alcohol carboxylic acid ester carboxylic acid derivative polyamine alcohol logP 1.73 ALOGPS logS -3.1 ALOGPS Water Solubility 2.60e-01 g/l ALOGPS logP 1.49 ChemAxon IUPAC Name (4R,6S)-6-{2-[(1S,2S,8S,8aR)-8-hydroxy-2-methyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]ethyl}-4-hydroxyoxan-2-one ChemAxon Traditional IUPAC Name (4R,6S)-6-{2-[(1S,2S,8S,8aR)-8-hydroxy-2-methyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]ethyl}-4-hydroxyoxan-2-one ChemAxon Molecular Weight 306.3966 ChemAxon Monoisotopic Weight 306.18310932 ChemAxon SMILES [H][C@]1(O)CC(=O)O[C@@]([H])(CC[C@@]2([H])[C@@]([H])(C)C=CC3=CCC[C@]([H])(O)[C@]23[H])C1 ChemAxon Molecular Formula C18H26O4 ChemAxon InChI InChI=1S/C18H26O4/c1-11-5-6-12-3-2-4-16(20)18(12)15(11)8-7-14-9-13(19)10-17(21)22-14/h3,5-6,11,13-16,18-20H,2,4,7-10H2,1H3/t11-,13+,14-,15-,16-,18-/m0/s1 ChemAxon InChIKey InChIKey=WWSNTLOVYSRDEL-TVKPWXLESA-N ChemAxon Polar Surface Area (PSA) 66.76 ChemAxon Refractivity 85.68 ChemAxon Polarizability 33.96 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 14.91 ChemAxon pKa (strongest basic) -0.85 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 4369567 PubChem Substance 99444695 ChemSpider 3572094 PDB MVB BE0002705 Liver carboxylesterase 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Liver carboxylesterase 1 Lipid transport and metabolism Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl CoA ester CES1 16q13-q22.1 Endoplasmic reticulum None 6.58 62522.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1863 GenAtlas CES1 GenBank Gene Database M73499 UniProtKB P23141 UniProt Accession EST1_HUMAN ACAT Acyl coenzyme A:cholesterol acyltransferase Brain carboxylesterase hBr1 EC 3.1.1.1 Egasyn HMSE Liver carboxylesterase 1 precursor Monocyte/macrophage serine esterase Serine esterase 1 TGH Triacylglycerol hydrolase >Liver carboxylesterase 1 MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPL GPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLN IYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLF HRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLK MKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIP MQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDL IADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPF LKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLK DKEVAFWTNLFAKKAVEKPPQTEHIEL >1704 bp ATGTGGCTCCGTGCCTTTATCCTGGCCACTCTCTCTGCTTCCGCGGCTTGGGGGCATCCG TCCTCGCCACCTGTGGTGGACACCGTGCATGGCAAAGTGCTGGGGAAGTTCGTCAGCTTA GAAGGATTTGCACAGCCTGTGGCCATTTTCCTGGGAATCCCTTTTGCCAAGCCGCCTCTT GGACCCCTGAGGTTTACTCCACCGCAGCCTGCAGAACCATGGAGCTTTGTGAAGAATGCC ACCTCGTACCCTCCTATGTGCACCCAAGATCCCAAGGCGGGGCAGTTACTCTCAGAGCTA TTTACAAACCGAAAGGAGAACATTCCTCTCAAGCTTTCTGAAGACTGTCTTTACCTCAAT ATTTACACTCCTGCTGACTTGACCAAGAAAAACAGGCTGCCGGTGATGGTGTGGATCCAC GGAGGGGGGCTGATGGTGGGTGCGGCATCAACCTATGATGGGCTGGCCCTTGCTGCCCAT GAAAACGTGGTGGTGGTGACCATTCAATATCGCCTGGGCATCTGGGGATTCTTCAGCACA GGGGATGAACACAGCCGGGGGAACTGGGGTCACCTGGACCAGGTGGCTGCCCTGCGCTGG GTCCAGGACAACATTGCCAGCTTTGGAGGGAACCCAGGCTCTGTGACCATCTTTGGAGAG TCAGCGGGAGGAGAAAGTGTCTCTGTTCTTGTTTTGTCTCCATTGGCCAAGAACCTCTTC CACCGGGCCATTTCTGAGAGTGGCGTGGCCCTCACTTCTGTTCTGGTGAAGAAAGGTGAT GTCAAGCCCTTGGCTGAGCAAATTGCTATCACTGCTGGGTGCAAAACCACCACCTCTGCT GTCATGGTTCACTGCCTGCGACAGAAGACGGAAGAGGAGCTCTTGGAGACGACATTGAAA ATGAAATTCTTATCTCTGGACTTACAGGGAGACCCCAGAGAGAGTCAACCCCTTCTGGGC ACTGTGATTGATGGGATGCTGCTGCTGAAAACACCTGAAGAGCTTCAAGCTGAAAGGAAT TTCCACACTGTCCCCTACATGGTCGGAATTAACAAGCAGGAGTTTGGCTGGTTGATTCCA ATGCAGTTGATGAGCTATCCACTCTCCGAAGGGCAACTGGACCAGAAGACAGCCATGTCA CTCCTGTGGAAGTCCTATCCCCTTGTTTGCATTGCTAAGGAACTGATTCCAGAAGCCACT GAGAAATACTTAGGAGGAACAGACGACACTGTCAAAAAGAAAGACCTGTTCCTGGACTTG ATAGCAGATGTGATGTTTGGTGTCCCATCTGTGATTGTGGCCCGGAACCACAGAGATGCT GGAGCACCCACCTACATGTATGAGTTTCAGTACCGTCCAAGCTTCTCATCAGACATGAAA CCCAAGACGGTGATAGGAGACCACGGGGATGAGCTCTTCTCCGTCTTTGGGGCCCCATTT TTAAAAGAGGGTGCCTCAGAAGAGGAGATCAGACTTAGCAAGATGGTGATGAAATTCTGG GCCAACTTTGCTCGCAATGGAAACCCCAATGGGGAAGGGCTGCCCCACTGGCCAGAGTAC AACCAGAAGGAAGGGTATCTGCAGATTGGTGCCAACACCCAGGCGGCCCAGAAGCTGAAG GACAAAGAAGTAGCTTTCTGGACCAACCTCTTTGCCAAGAAGGCAGTGGAGAAGCCACCC CAGACAGAACACATAGAGCTGTGA PF00135 COesterase "
drug:(1S,7S,8S,8AR)-1,2,3,7,8,8A-HEXAHYDRO-7-METHYL-8-[2-[(2R,4R)-TETRAHYDRO-4-HY DROXY-6-OXO-2H-PYRAN-2-YL]ETHYL]-1-NAPHTHALENOLrdfs:label"(1S,7S,8S,8AR)-1,2,3,7,8,8A-HEXAHYDRO-7-METHYL-8-[2-[(2R,4R)-TETRAHYDRO-4-HY DROXY-6-OXO-2H-PYRAN-2-YL]ETHYL]-1-NAPHTHALENOL"
drug:(1S,7S,8S,8AR)-1,2,3,7,8,8A-HEXAHYDRO-7-METHYL-8-[2-[(2R,4R)-TETRAHYDRO-4-HY DROXY-6-OXO-2H-PYRAN-2-YL]ETHYL]-1-NAPHTHALENOLrdf:typedrugbank:drugs
drug:(1Z)-2-HYDROXY-3-OXOHEX-1-EN-1-YL DIHYDROGEN PHOSPHATEdrugbank:description" experimental This compound belongs to the organophosphate esters. These are organic compounds containing phosphoric acid ester functional group. Organophosphate Esters Organic Compounds Organophosphorus Compounds Organic Phosphoric Acids and Derivatives Organophosphate Esters Organic Phosphoric Acids Acryloyl Compounds Enones Enolates Polyamines Aldehydes acryloyl-group enone ketone polyamine enolate aldehyde carbonyl group logP -0.29 ALOGPS logS -1.4 ALOGPS Water Solubility 8.11e+00 g/l ALOGPS logP 0.24 ChemAxon IUPAC Name {[(1Z)-2-hydroxy-3-oxohex-1-en-1-yl]oxy}phosphonic acid ChemAxon Traditional IUPAC Name [(1Z)-2-hydroxy-3-oxohex-1-en-1-yl]oxyphosphonic acid ChemAxon Molecular Weight 210.1217 ChemAxon Monoisotopic Weight 210.029324596 ChemAxon SMILES CCCC(=O)C(\O)=C\OP(O)(O)=O ChemAxon Molecular Formula C6H11O6P ChemAxon InChI InChI=1S/C6H11O6P/c1-2-3-5(7)6(8)4-12-13(9,10)11/h4,8H,2-3H2,1H3,(H2,9,10,11)/b6-4- ChemAxon InChIKey InChIKey=HEBDCWKDNSCZMW-XQRVVYSFSA-N ChemAxon Polar Surface Area (PSA) 104.06 ChemAxon Refractivity 44.89 ChemAxon Polarizability 17.6 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 1.36 ChemAxon pKa (strongest basic) -4.5 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937032 PubChem Substance 99443352 ChemSpider 22376141 PDB 1AE BE0003741 2,3-diketo-5-methylthiopentyl-1-phosphate enolase Geobacillus kaustophilus (strain HTA426) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown 2,3-diketo-5-methylthiopentyl-1-phosphate enolase Carbohydrate transport and metabolism Catalyzes the enolization of 2,3-diketo-5- methylthiopentyl-1-phosphate (DK-MTP-1-P) into 2-hydroxy-3-keto-5- methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) mtnW None 5.36 44905.2 Geobacillus kaustophilus (strain HTA426) GeneCards mtnW GenBank Gene Database BA000043 GenBank Protein Database 56378378 UniProtKB Q5L1E2 UniProt Accession MTNW_GEOKA DK-MTP-1-P enolase RLP RuBisCO-like protein >2,3-diketo-5-methylthiopentyl-1-phosphate enolase MSAVMATYLLHDETDIRKKAEGIALGLTIGTWTDLPALEQEQLRKHKGEVVAIEELGESE RVNAYFGKRLKRAIVKIAYPTVNFSADLPALLVTTFGKLSLDGEVRLLDLEFPDEWKRQF PGPRFGIDGIRDRVGVHNRPLLMSIFKGMIGRDLAYLTSELKKQALGGVDLVKDDEILFD SELLPFEKRITEGKAALQEVYEQTGKRTLYAVNLTGKTFALKDKAKRAAELGADVLLFNV FAYGLDVLQALREDEEIAVPIMAHPAFSGAVTPSEFYGVAPSLWLGKLLRLAGADFVLFP SPYGSVALEREQALGIARALTDDQEPFARAFPVPSAGIHPGLVPLIIRDFGLDTIVNAGG GIHGHPDGAIGGGRAFRAAIDAVLAGRPLRAAAAENEALQKAIDRWGVVEVEA >1353 bp GTGGAAAATATCCATGACTTATGGGATCGCGTGCTCGCGGAGATTGAACAAAAAATCAGC AAGCCGAGCTTTGAAACTTGGCTCAAGTCAACAAAAGCCCACTCTTTACGAGGTGACACG CTCGTCATCGTAGCCCCGAACGAGTTTGCTAGAGATTGGCTTGATTCTCGCTACTCTCAT TTGATTGCGGAAACGATCTACACCATCACGGGCGAAGAATTGGCCGTCAAGTTTATCATT CCGCCAAATCAGGATGATGAAGAACTAGAGTTCCAGTCATCTAAGAAAAAGCAACGGAAA CCGTATGAAGAGACAAACGATTTCCCACAAAGCATGTTAAATCCGAAATACACGTTCGAT ACGTTTGTCATCGGCTCCGGCAACCGGTTCGCCCATGCCGCTTCACTGGCGGTCGCTGAG GCTCCGGCCAAAGCATACAACCCCTTGTTTATCTATGGCGGCGTCGGACTTGGAAAAACA CACTTAATGCACGCGATCGGCCATTACGTGATTGAACATAACCCATCGGCGAAAGTGGTC TATTTATCTTCAGAGAAATTTACGAATGAGTTTATTAACGCCATCCGAGACAACCGCCCT GACGACTTTCGCAACAAGTATCGGAACGTTGACGTCCTACTGATCGATGATATTCAGTTT TTGGCCGGAAAAGAACAAACGCAAGAAGAATTTTTCCATACGTTTAATACGCTGCACGAG GAGAGCAAGCAAATCGTCATCTCAAGCGATCGACCGCCGAAAGAAATCCCAACACTCGAA GACCGCTTGCGTTCGCGCTTTGAGTGGGGGCTCATCACCGACATTACGCCGCCTGATTTG GAGACGCGGATCGCTATCCTCCGCAAAAAGGCGAAGGCGGAGGGGTTTGACATTCCAAAC GAGGTAATGCTTTATATCGCCAATCAAATTGACTCGAACATCCGCGAGCTTGAGGGCGCT CTCATTCGCGTCGTCGCTTATTCGTCGCTCATCAACAAAGAGATCACCGCTGACTTGGCA GCAGAGGCATTGAAAGACATCATCCCGAGCGCAAAGCCGAAGGTAATCACGATTCAAGAC ATTCAGCGCGTTGTTGGACAGCATTTCAACATCAAGATGGAAGATTTTAAAGCGAAAAAG CGAACAAAATCGGTCGCGTTCCCTCGGCAAATTGCCATGTATCTCTCCCGCGAACTGACC GACTGTTCGTTGCCGAAAATCGGCGATGAATTTGGGGGACGCGATCATACAACCGTCATC CACGCCCATGAAAAAATATCAAAGCTTTTGCAAACCGATACGCAGCTGCAAAGGCATATA CAAGAGATTCAAGAAAAGCTGAAGCAACTGTGA PF00016 RuBisCO_large component protein complex component ribulose bisphosphate carboxylase complex component ribulose bisphosphate carboxylase complex (sensu Magnoliophyta) function lyase activity function carbon-carbon lyase activity function carboxy-lyase activity function ribulose-bisphosphate carboxylase activity function catalytic activity process metabolism process carbon utilization process carbon utilization by fixation of carbon dioxide process physiological process "
drug:(1Z)-2-HYDROXY-3-OXOHEX-1-EN-1-YL DIHYDROGEN PHOSPHATErdfs:label"(1Z)-2-HYDROXY-3-OXOHEX-1-EN-1-YL DIHYDROGEN PHOSPHATE"
drug:(1Z)-2-HYDROXY-3-OXOHEX-1-EN-1-YL DIHYDROGEN PHOSPHATErdf:typedrugbank:drugs
drug:(1Z)-4-(4-FLUOROPHENYL)-2-METHYLIDENEBUTAN-1-IMINEdrugbank:description" experimental This compound belongs to the fluorobenzenes. These are compounds containing one or more fluorine atoms attached to a benzene ring. Fluorobenzenes Organic Compounds Benzenoids Benzene and Substituted Derivatives Halobenzenes Aryl Fluorides Polyamines Primary Aldimines Organofluorides aryl halide aryl fluoride aldimine primary aldimine polyamine organohalogen imine organofluoride organonitrogen compound logP 2.49 ALOGPS logS -3.9 ALOGPS Water Solubility 2.26e-02 g/l ALOGPS logP 2.95 ChemAxon IUPAC Name 1-(3-carboximidoylbut-3-en-1-yl)-4-fluorobenzene ChemAxon Traditional IUPAC Name 1-(3-carboximidoylbut-3-en-1-yl)-4-fluorobenzene ChemAxon Molecular Weight 177.2181 ChemAxon Monoisotopic Weight 177.095377594 ChemAxon SMILES FC1=CC=C(CCC(=C)C=N)C=C1 ChemAxon Molecular Formula C11H12FN ChemAxon InChI InChI=1S/C11H12FN/c1-9(8-13)2-3-10-4-6-11(12)7-5-10/h4-8,13H,1-3H2 ChemAxon InChIKey InChIKey=CFVUPEQWSFCCFT-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 23.85 ChemAxon Refractivity 62.71 ChemAxon Polarizability 18.94 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 8.52 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937129 PubChem Substance 99444647 PDB MFG BE0002196 Amine oxidase [flavin-containing] B Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Amine oxidase [flavin-containing] B Amino acid transport and metabolism Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine MAOB Xp11.23 Mitochondrion 490-516 7.55 58764.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6834 GenAtlas MAOB GeneCards MAOB GenBank Gene Database S62734 GenBank Protein Database 398415 UniProtKB P27338 UniProt Accession AOFB_HUMAN EC 1.4.3.4 MAO-B Monoamine oxidase type B >Amine oxidase [flavin-containing] B MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSY VGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWR TMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEV SALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQ TRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVY YKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEER LKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR IYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTT FLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV >1560 bp ATGAGCAACAAATGCGACGTGGTCGTGGTGGGGGGCGGCATCTCAGGTATGGCAGCAGCC AAACTTCTGCATGACTCTGGACTGAATGTGGTTGTTCTGGAAGCCCGGGACCGTGTGGGA GGCAGGACTTACACTCTTAGGAACCAAAAGGTTAAATATGTGGACCTTGGAGGATCCTAT GTTGGACCAACCCAGAATCGTATCTTGAGATTAGCCAAGGAGCTAGGATTGGAGACCTAC AAAGTGAATGAGGTTGAGCGTCTGATCCACCATGTAAAGGGCAAATCATACCCCTTCAGG GGGCCATTCCCACCTGTATGGAATCCAATTACCTACTTAGATCATAACAACTTTTGGAGG ACAATGGATGACATGGGGCGAGAGATTCCGAGTGATGCCCCATGGAAGGCTCCCCTTGCA GAAGAGTGGGACAACATGACAATGAAGGAGCTACTGGACAAGCTCTGCTGGACTGAATCT GCAAAGCAGCTTGCCACTCTCTTTGTGAACCTGTGTGTCACTGCAGAGACCCATGAGGTC TCTGCTCTCTGGTTCCTGTGGTATGTGAAGCAGTGTGGAGGCACAACAAGAATCATCTCG ACAACAAATGGAGGACAGGAGAGGAAATTTGTGGGCGGATCTGGTCAAGTGAGTGAGCGG ATAATGGACCTCCTTGGAGACCGAGTGAAGCTGGAGAGGCCTGTGATCTACATTGACCAG ACAAGAGAAAATGTCCTTGTGGAGACCCTAAACCATGAGATGTATGAGGCTAAATATGTG ATTAGTGCTATTCCTCCTACTCTGGGCATGAAGATTCACTTCAATCCCCCTCTGCCAATG ATGAGAAACCAGATGATCACTCGTGTGCCTTTGGGTTCAGTCATCAAGTGTATAGTTTAT TATAAAGAGCCTTTCTGGAGGAAAAAGGATTACTGTGGAACCATGATTATTGATGGAGAA GAAGCTCCAGTTGCCTACACGTTGGATGATACCAAACCTGAAGGCAACTATGCTGCCATA ATGGGATTTATCCTGGCCCACAAAGCCAGAAAACTGGCACGTCTTACCAAAGAGGAAAGG TTGAAGAAACTTTGTGAACTCTATGCCAAGGTTCTGGGTTCCCTAGAAGCTCTGGAGCCA GTGCATTATGAAGAAAAGAACTGGTGTGAGGAGCAGTACTCTGGGGGCTGCTACACAACT TATTTCCCCCCTGGGATCCTGACTCAATATGGAAGGGTTCTACGCCAGCCAGTGGACAGG ATTTACTTTGCAGGCACCGAGACTGCCACACACTGGAGCGGCTACATGGAGGGGGCTGTA GAGGCCGGGGAGAGAGCAGCCCGAGAGATCCTGCATGCCATGGGGAAGATTCCAGAGGAT GAAATCTGGCAGTCAGAACCAGAGTCTGTGGATGTCCCTGCACAGCCCATCACCACCACC TTTTTGGAGAGACATTTGCCCTCCGTGCCAGGCCTGCTCAGGCTGATTGGATTGACCACC ATCTTTTCAGCAACGGCTCTTGGCTTCCTGGCCCACAAAAGGGGGCTACTTGTGAGAGTC PF01593 Amino_oxidase function catalytic activity function oxidoreductase activity process generation of precursor metabolites and energy process electron transport process physiological process process metabolism process cellular metabolism "
drug:(1Z)-4-(4-FLUOROPHENYL)-2-METHYLIDENEBUTAN-1-IMINErdfs:label"(1Z)-4-(4-FLUOROPHENYL)-2-METHYLIDENEBUTAN-1-IMINE"
drug:(1Z)-4-(4-FLUOROPHENYL)-2-METHYLIDENEBUTAN-1-IMINErdf:typedrugbank:drugs
drug:(1aR,8S,13S,14S,15aR)-5,13,14-trihydroxy-3-methoxy-8-methyl-8,9,13,14,15,15a-hexahydro-6H-oxireno[k][2]benzoxacyclotetradecine-6,12(1aH)-dionedrugbank:description" experimental This compound belongs to the zearalenones. These are macrolides which contains a fourteen-member lactone fused to 1,3-dihydroxybenzene. Zearalenones Organic Compounds Phenylpropanoids and Polyketides Macrolides and Analogues Zearalenones Hydroxybenzoic Acid Derivatives Methoxyphenols and Derivatives Anisoles Alkyl Aryl Ethers Ketones Carboxylic Acid Esters Secondary Alcohols 1,2-Diols Dialkyl Ethers Enols Polyamines Epoxides hydroxybenzoic acid methoxyphenol phenol ether anisole alkyl aryl ether phenol derivative benzene ketone secondary alcohol carboxylic acid ester polyol 1,2-diol oxirane ether dialkyl ether enol carboxylic acid derivative polyamine carbonyl group alcohol logP 0.95 ALOGPS logS -2.3 ALOGPS Water Solubility 1.86e+00 g/l ALOGPS logP 1.63 ChemAxon IUPAC Name (2R,4R,6S,7S,12S)-6,7,16-trihydroxy-18-methoxy-12-methyl-3,13-dioxatricyclo[13.4.0.0^{2,4}]nonadeca-1(19),9,15,17-tetraene-8,14-dione ChemAxon Traditional IUPAC Name (2R,4R,6S,7S,12S)-6,7,16-trihydroxy-18-methoxy-12-methyl-3,13-dioxatricyclo[13.4.0.0^{2,4}]nonadeca-1(19),9,15,17-tetraene-8,14-dione ChemAxon Molecular Weight 378.3732 ChemAxon Monoisotopic Weight 378.13146768 ChemAxon SMILES [H][C@@]12C[C@]([H])(O)[C@]([H])(O)C(=O)\C=C/C[C@]([H])(C)OC(=O)C3=C(O)C=C(OC)C=C3[C@@]1([H])O2 ChemAxon Molecular Formula C19H22O8 ChemAxon InChI InChI=1S/C19H22O8/c1-9-4-3-5-12(20)17(23)14(22)8-15-18(27-15)11-6-10(25-2)7-13(21)16(11)19(24)26-9/h3,5-7,9,14-15,17-18,21-23H,4,8H2,1-2H3/b5-3-/t9-,14-,15+,17+,18+/m0/s1 ChemAxon InChIKey InChIKey=SSNQAUBBJYCSMY-KNTMUCJRSA-N ChemAxon Polar Surface Area (PSA) 125.82 ChemAxon Refractivity 94.98 ChemAxon Polarizability 37.57 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 9.47 ChemAxon pKa (strongest basic) -3.3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 9929643 PubChem Substance 99444376 ChemSpider 8105274 PDB HMY BE0000923 Mitogen-activated protein kinase 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Mitogen-activated protein kinase 1 Involved in MAP kinase activity Involved in both the initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors such as ELK1. Phosphorylates EIF4EBP1; required for initiation of translation. Phosphorylates microtubule-associated protein 2 (MAP2). Phosphorylates SPZ1 MAPK1 22q11.2|22q11.21 None 6.99 41390.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6871 GenAtlas MAPK1 GeneCards MAPK1 GenBank Gene Database M84489 GenBank Protein Database 182191 UniProtKB P28482 UniProt Accession MK01_HUMAN EC 2.7.11.24 ERK-2 ERT1 Extracellular signal-regulated kinase 2 MAP kinase 2 MAPK 2 Mitogen-activated protein kinase 2 p42-MAPK >Mitogen-activated protein kinase 1 MAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFE HQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQH LSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDH TGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHI LGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHK RIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS >1083 bp ATGGCGGCGGCGGCGGCGGCGGGCGCGGGCCCGGAGATGGTCCGCGGGCAGGTGTTCGAC GTGGGGCCGCGCTACACCAACCTCTCGTACATCGGCGAGGGCGCCTACGGCATGGTGTGC TCTGCTTATGATAATGTCAACAAAGTTCGAGTAGCTATCAAGAAAATCAGCCCCTTTGAG CACCAGACCTACTGCCAGAGAACCCTGAGGGAGATAAAAATCTTACTGCGCTTCAGACAT GAGAACATCATTGGAATCAATGACATTATTCGAGCACCAACCATCGAGCAAATGAAAGAT GTATATATAGTACAGGACCTCATGGAAACAGATCTTTACAAGCTCTTGAAGACACAACAC CTCAGCAATGACCATATCTGCTATTTTCTCTACCAGATCCTCAGAGGGTTAAAATATATC CATTCAGCTAACGTTCTGCACCGTGACCTCAAGCCTTCCAACCTGCTGCTCAACACCACC TGTGATCTCAAGATCTGTGACTTTGGCCTGGCCCGTGTTGCAGATCCAGACCATGATCAC ACAGGGTTCCTGACAGAATATGTGGCCACACGTTGGTACAGGGCTCCAGAAATTATGTTG AATTCCAAGGGCTACACCAAGTCCATTGATATTTGGTCTGTAGGCTGCATTCTGGCAGAA ATGCTTTCCAACAGGCCCATCTTTCCAGGGAAGCATTATCTTGACCAGCTGAATCACATT TTGGGTATTCTTGGATCCCCATCACAAGAAGACCTGAATTGTATAATAAATTTAAAAGCT AGGAACTATTTGCTTTCTCTTCCACACAAAAATAAGGTGCCATGGAACAGGCTGTTCCCA AATGCTGACTCCAAAGCTCTGGACTTATTGGACAAAATGTTGACATTCAACCCACACAAG AGGATTGAAGTAGAACAGGCTCTGGCCCACCCATATCTGGAGCAGTATTACGACCCGAGT GACGAGCCCATCGCCGAAGCACCATTCAAGTTCGACATGGAATTGGATGACTTGCCTAAG GAAAAGCTAAAAGAACTAATTTTTGAAGAGACTGCTAGATTCCAGCCAGGATACAGATCT TAA PF00069 Pkinase function protein serine/threonine kinase activity function receptor signaling protein serine/threonine kinase activity function nucleotide binding function MAP kinase activity function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation "
drug:(1aR,8S,13S,14S,15aR)-5,13,14-trihydroxy-3-methoxy-8-methyl-8,9,13,14,15,15a-hexahydro-6H-oxireno[k][2]benzoxacyclotetradecine-6,12(1aH)-dionerdfs:label"(1aR,8S,13S,14S,15aR)-5,13,14-trihydroxy-3-methoxy-8-methyl-8,9,13,14,15,15a-hexahydro-6H-oxireno[k][2]benzoxacyclotetradecine-6,12(1aH)-dione"
drug:(1aR,8S,13S,14S,15aR)-5,13,14-trihydroxy-3-methoxy-8-methyl-8,9,13,14,15,15a-hexahydro-6H-oxireno[k][2]benzoxacyclotetradecine-6,12(1aH)-dionerdf:typedrugbank:drugs
drug:(1h-Indol-3-Yl)-(2-Mercapto-Ethoxyimino)-Acetic Aciddrugbank:description" experimental This compound belongs to the indole-3-acetic acid derivatives. These are compounds containing an acetic acid (or a derivative) linked to the C3 carbon atom of an indole. Indole-3-acetic Acid Derivatives Organic Compounds Heterocyclic Compounds Indoles and Derivatives Indolyl Carboxylic Acids and Derivatives Alpha Amino Acids and Derivatives Indoles Substituted Pyrroles Benzene and Substituted Derivatives Enolates Carboxylic Acids Polyamines Alkylthiols alpha-amino acid or derivative indole substituted pyrrole benzene pyrrole alkylthiol polyamine enolate carboxylic acid derivative carboxylic acid amine organonitrogen compound logP 1.27 ALOGPS logS -3.4 ALOGPS Water Solubility 1.06e-01 g/l ALOGPS logP 1.42 ChemAxon IUPAC Name (2R)-2-(1H-indol-3-yl)-2-[(2-sulfanylethoxy)amino]acetic acid ChemAxon Traditional IUPAC Name (R)-1H-indol-3-yl[(2-sulfanylethoxy)amino]acetic acid ChemAxon Molecular Weight 266.316 ChemAxon Monoisotopic Weight 266.072513014 ChemAxon SMILES [H][C@](NOCCS)(C(O)=O)C1=CNC2=C1C=CC=C2 ChemAxon Molecular Formula C12H14N2O3S ChemAxon InChI InChI=1S/C12H14N2O3S/c15-12(16)11(14-17-5-6-18)9-7-13-10-4-2-1-3-8(9)10/h1-4,7,11,13-14,18H,5-6H2,(H,15,16)/t11-/m1/s1 ChemAxon InChIKey InChIKey=FJAWIBGKKKXXAL-LLVKDONJSA-N ChemAxon Polar Surface Area (PSA) 74.35 ChemAxon Refractivity 80.66 ChemAxon Polarizability 27.27 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 4.38 ChemAxon pKa (strongest basic) 2.65 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 447066 PubChem Substance 46507395 ChemSpider 394263 PDB MPE BE0001029 Interleukin-2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Interleukin-2 Involved in interleukin-2 receptor binding Produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Can stimulate B-cells, monocytes, lymphokine- activated killer cells, natural killer cells, and glioma cells IL2 4q26-q27 Secreted protein None 7.95 17628.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6001 GenAtlas IL2 GeneCards IL2 GenBank Gene Database J00264 GenBank Protein Database 5729676 UniProtKB P60568 UniProt Accession IL2_HUMAN Aldesleukin IL-2 Interleukin-2 precursor T-cell growth factor TCGF >Interleukin-2 precursor MYRMQLLSCIALSLALVTNSAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRML TFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSE TTFMCEYADETATIVEFLNRWITFCQSIISTLT >462 bp ATGTACAGGATGCAACTCCTGTCTTGCATTGCACTAAGTCTTGCACTTGTCACAAACAGT GCACCTACTTCAAGTTCTACAAAGAAAACACAGCTACAACTGGAGCATTTACTGCTGGAT TTACAGATGATTTTGAATGGAATTAATAATTACAAGAATCCCAAACTCACCAGGATGCTC ACATTTAAGTTTTACATGCCCAAGAAGGCCACAGAACTGAAACATCTTCAGTGTCTAGAA GAAGAACTCAAACCTCTGGAGGAAGTGCTAAATTTAGCTCAAAGCAAAAACTTTCACTTA AGACCCAGGGACTTAATCAGCAATATCAACGTAATAGTTCTGGAACTAAAGGGATCTGAA ACAACATTCATGTGTGAATATGCTGATGAGACAGCAACCATTGTAGAATTTCTGAACAGA TGGATTACCTTTTGTCAAAGCATCATCTCAACACTGACTTGA PF00715 IL2 component extracellular region function growth factor activity function receptor binding function cytokine activity function hematopoietin/interferon-class (D200-domain) cytokine receptor binding function interleukin-2 receptor binding function signal transducer activity process response to stimulus process response to biotic stimulus process defense response process immune response "
drug:(1h-Indol-3-Yl)-(2-Mercapto-Ethoxyimino)-Acetic Acidrdfs:label"(1h-Indol-3-Yl)-(2-Mercapto-Ethoxyimino)-Acetic Acid"
drug:(1h-Indol-3-Yl)-(2-Mercapto-Ethoxyimino)-Acetic Acidowl:sameAsdrug:EXPT02219
drug:(1h-Indol-3-Yl)-(2-Mercapto-Ethoxyimino)-Acetic Acidrdf:typedrugbank:drugs
drug:(1n)-4-N-Butoxyphenylsulfonyl-(2r)-N-Hydroxycarboxamido-(4s)-Methanesulfonylamino-Pyrrolidinedrugbank:description" experimental This compound belongs to the alpha amino acid amides. These are amide derivatives of alpha amino acids. Alpha Amino Acid Amides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Benzenesulfonamides Phenol Ethers Pyrrolidinecarboxamides Alkyl Aryl Ethers Sulfonyls Sulfonamides Hydroxamic Acids Enolates Polyamines benzenesulfonamide pyrrolidine carboxylic acid or derivative phenol ether pyrrolidine-2-carboxamide alkyl aryl ether benzene sulfonic acid derivative sulfonyl sulfonamide pyrrolidine carboxamide group hydroxamic acid polyamine enolate ether amine organonitrogen compound logP 0.2 ALOGPS logS -3 ALOGPS Water Solubility 4.59e-01 g/l ALOGPS logP -0.46 ChemAxon IUPAC Name (2R,4S)-1-[(4-butoxybenzene)sulfonyl]-N-hydroxy-4-methanesulfonamidopyrrolidine-2-carboxamide ChemAxon Traditional IUPAC Name (2R,4S)-1-(4-butoxybenzenesulfonyl)-N-hydroxy-4-methanesulfonamidopyrrolidine-2-carboxamide ChemAxon Molecular Weight 435.516 ChemAxon Monoisotopic Weight 435.113391549 ChemAxon SMILES CCCCOC1=CC=C(C=C1)S(=O)(=O)N1C[C@H](C[C@@H]1C(=O)NO)NS(C)(=O)=O ChemAxon Molecular Formula C16H25N3O7S2 ChemAxon InChI InChI=1S/C16H25N3O7S2/c1-3-4-9-26-13-5-7-14(8-6-13)28(24,25)19-11-12(18-27(2,22)23)10-15(19)16(20)17-21/h5-8,12,15,18,21H,3-4,9-11H2,1-2H3,(H,17,20)/t12-,15+/m0/s1 ChemAxon InChIKey InChIKey=ULDXUWXTVRRUND-SWLSCSKDSA-N ChemAxon Polar Surface Area (PSA) 142.11 ChemAxon Refractivity 101.32 ChemAxon Polarizability 43.6 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 8.71 ChemAxon pKa (strongest basic) -4.9 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 5287415 PubChem Substance 46506803 ChemSpider 1222 PDB 111 BE0001116 Stromelysin-1 Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Stromelysin-1 Involved in protease activity Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase MMP3 11q22.3 Cytoplasmic None 6.07 53978.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7173 GenAtlas MMP3 GeneCards MMP3 GenBank Gene Database X05232 GenBank Protein Database 36633 UniProtKB P08254 UniProt Accession MMP3_HUMAN EC 3.4.24.17 Matrix metalloproteinase-3 MMP-3 SL-1 Stromelysin-1 precursor Transin-1 >Stromelysin-1 precursor MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPV VKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVN YTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNV LAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLY HSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVS TLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQF WAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEP GFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC >1434 bp ATGAAGAGTCTTCCAATCCTACTGTTGCTGTGCGTGGCAGTTTGCTCAGCCTATCCATTG GATGGAGCTGCAAGGGGTGAGGACACCAGCATGAACCTTGTTCAGAAATATCTAGAAAAC TACTACGACCTCAAAAAAGATGTGAAACAGTTTGTTAGGAGAAAGGACAGTGGTCCTGTT GTTAAAAAAATCCGAGAAATGCAGAAGTTCCTTGGATTGGAGGTGACGGGGAAGCTGGAC TCCGACACTCTGGAGGTGATGCGCAAGCCCAGGTGTGGAGTTCCTGATGTTGGTCACTTC AGAACCTTTCCTGGCATCCCGAAGTGGAGGAAAACCCACCTTACATACAGGATTGTGAAT TATACACCAGATTTGCCAAAAGATGCTGTTGATTCTGCTGTTGAGAAAGCTCTGAAAGTC TGGGAAGAGGTGACTCCACTCACATTCTCCAGGCTGTATGAAGGAGAGGCTGATATAATG ATCTCTTTTGCAGTTAGAGAACATGGAGACTTTTACCCTTTTGATGGACCTGGAAATGTT TTGGCCCATGCCTATGCCCCTGGGCCAGGGATTAATGGAGATGCCCACTTTGATGATGAT GAACAATGGACAAAGGATACAACAGGGACCAATTTATTTCTCGTTGCTGCTCATGAAATT GGCCACTCCCTGGGTCTCTTTCACTCAGCCAACACTGAAGCTTTGATGTACCCACTCTAT CACTCACTCACAGACCTGACTCGGTTCCGCCTGTCTCAAGATGATATAAATGGCATTCAG TCCCTCTATGGACCTCCCCCTGACTCCCCTGAGACCCCCCTGGTACCCACGGAACCTGTC CCTCCAGAACCTGGGACGCCAGCCAACTGTGATCCTGCTTTGTCCTTTGATGCTGTCAGC ACTCTGAGGGGAGAAATCCTGATCTTTAAAGACAGGCACTTTTGGCGCAAATCCCTCAGG AAGCTTGAACCTGAATTGCATTTGATCTCTTCATTTTGGCCATCTCTTCCTTCAGGCGTG GATGCCGCATATGAAGTTACTAGCAAGGACCTCGTTTTCATTTTTAAAGGAAATCAATTC TGGGCCATCAGAGGAAATGAGGTACGAGCTGGATACCCAAGAGGCATCCACACCCTAGGT TTCCCTCCAACCGTGAGGAAAATCGATGCAGCCATTTCTGATAAGGAAAAGAACAAAACA TATTTCTTTGTAGAGGACAAATACTGGAGATTTGATGAGAAGAGAAATTCCATGGAGCCA GGCTTTCCCAAGCAAATAGCTGAAGACTTTCCAGGGATTGACTCAAAGATTGATGCTGTT TTTGAAGAATTTGGGTTCTTTTATTTCTTTACTGGATCTTCACAGTTGGAGTTTGACCCA AATGCAAAGAAAGTGACACACACTTTGAAGAGTAACAGCTGGCTTAATTGTTGA PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 component extracellular matrix (sensu Metazoa) component extracellular matrix function catalytic activity function hydrolase activity function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process "
drug:(1n)-4-N-Butoxyphenylsulfonyl-(2r)-N-Hydroxycarboxamido-(4s)-Methanesulfonylamino-Pyrrolidinerdfs:label"(1n)-4-N-Butoxyphenylsulfonyl-(2r)-N-Hydroxycarboxamido-(4s)-Methanesulfonylamino-Pyrrolidine"
drug:(1n)-4-N-Butoxyphenylsulfonyl-(2r)-N-Hydroxycarboxamido-(4s)-Methanesulfonylamino-Pyrrolidineowl:sameAsdrug:EXPT00010
drug:(1n)-4-N-Butoxyphenylsulfonyl-(2r)-N-Hydroxycarboxamido-(4s)-Methanesulfonylamino-Pyrrolidinerdf:typedrugbank:drugs
drug:(1r)-4-[(1e,3e,5e,7z,9e,11z,13e,15e)-17-Hydroxy-3,7,12,16-Tetramethylheptadeca-1,3,5,7,9,11,13,15-Octaen-1-Yl]-3,5,5-Trimethylcyclohex-3-En-1-Oldrugbank:description" experimental This compound belongs to the diterpenes. These are terpene compounds formed by four isoprene units. Diterpenes Organic Compounds Lipids Prenol Lipids Diterpenes Fatty Alcohols Cyclitols and Derivatives Secondary Alcohols Primary Alcohols Polyamines fatty alcohol cyclitol derivative cyclic alcohol secondary alcohol polyamine primary alcohol alcohol logP 6.84 ALOGPS logS -5.4 ALOGPS Water Solubility 1.57e-03 g/l ALOGPS logP 5.9 ChemAxon IUPAC Name (1R)-4-[(1E,3E,5E,7Z,9E,11Z,13E,15E)-17-hydroxy-3,7,12,16-tetramethylheptadeca-1,3,5,7,9,11,13,15-octaen-1-yl]-3,5,5-trimethylcyclohex-3-en-1-ol ChemAxon Traditional IUPAC Name (1R)-4-[(1E,3E,5E,7Z,9E,11Z,13E,15E)-17-hydroxy-3,7,12,16-tetramethylheptadeca-1,3,5,7,9,11,13,15-octaen-1-yl]-3,5,5-trimethylcyclohex-3-en-1-ol ChemAxon Molecular Weight 434.6533 ChemAxon Monoisotopic Weight 434.318480588 ChemAxon SMILES OC\C(C)=C\C=C\C(\C)=C/C=C/C=C(/C)\C=C\C=C(/C)\C=C\C1=C(C)C[C@@H](O)CC1(C)C ChemAxon Molecular Formula C30H42O2 ChemAxon InChI InChI=1S/C30H42O2/c1-23(12-8-9-13-24(2)15-11-17-26(4)22-31)14-10-16-25(3)18-19-29-27(5)20-28(32)21-30(29,6)7/h8-19,28,31-32H,20-22H2,1-7H3/b9-8+,14-10+,15-11+,19-18+,23-12-,24-13-,25-16+,26-17+/t28-/m1/s1 ChemAxon InChIKey InChIKey=FNAJVVMDXCOSFY-VFGOXHQXSA-N ChemAxon Polar Surface Area (PSA) 40.46 ChemAxon Refractivity 149.43 ChemAxon Polarizability 55.26 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 16.76 ChemAxon pKa (strongest basic) -1.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon ChEBI 39930 PubChem Compound 5287502 PubChem Substance 46506703 ChemSpider 21239499 PDB 3ON BE0002716 Apocarotenoid-15,15'-oxygenase Synechocystis sp. (strain PCC 6803 / Kazusa) unknown Apocarotenoid-15,15'-oxygenase Secondary metabolites biosynthesis, transport and catabolism sll1541 None 6.16 54287.0 Synechocystis sp. (strain PCC 6803 / Kazusa) GenBank Gene Database BA000022 UniProtKB P74334 UniProt Accession ACOX_SYNY3 >Lignostilbene-alpha,beta-dioxygenase MVTSPPTSSPSQRSYSPQDWLRGYQSQPQEWDYWVEDVEGSIPPDLQGTLYRNGPGLLEI GDRPLKHPFDGDGMVTAFKFPGDGRVHFQSKFVRTQGYVEEQKAGKMIYRGVFGSQPAGG WLKTIFDLRLKNIANTNITYWGDRLLALWEGGQPHRLEPSNLATIGLDDLGGILAEGQPL SAHPRIDPASTFDGGQPCYVTFSIKSSLSSTLTLLELDPQGKLLRQKTETFPGFAFIHDF AITPHYAIFLQNNVTLNGLPYLFGLRGAGECVQFHPDKPAQIILVPRDGGEIKRIPVQAG FVFHHANAFEENGKIILDSICYNSLPQVDTDGDFRSTNFDNLDPGQLWRFTIDPAAATVE KQLMVSRCCEFPVVHPQQVGRPYRYVYMGAAHHSTGNAPLQAILKVDLESGTETLRSFAP HGFAGEPIFVPRPGGVAEDDGWLLCLIYKADLHRSELVILDAQDITAPAIATLKLKHHIP YPLHGSWAQT >1473 bp TCAAGTCTGGGCCCAGGAACCGTGCAGGGGATAGGGAATGTGATGCTTTAACTTCAAAGT GGCGATCGCCGGAGCAGTAATGTCCTGAGCATCAAGAATCACTAGTTCGGAACGGTGCAA ATCAGCTTTATAAATCAAGCAGAGCAACCAACCATCATCTTCAGCCACGCCACCGGGTCG GGGCACAAAAATAGGTTCCCCGGCAAAACCATGGGGGGCAAAGGAACGTAGAGTTTCAGT GCCGGACTCTAGATCTACTTTGAGAATGGCCTGAAGGGGAGCATTGCCTGTGCTATGGTG TGCGGCTCCCATGTAAACATAGCGATATGGACGGCCAACCTGCTGGGGATGGACAACGGG AAACTCGCAACAACGACTAACCATTAACTGTTTTTCCACCGTGGCTGCTGCGGGATCAAT GGTGAAACGCCATAACTGTCCGGGATCTAAATTATCGAAATTCGTACTACGAAAATCCCC ATCGGTGTCTACCTGGGGCAGGGAATTGTAACAAATGGAATCGAGGATTATTTTGCCATT TTCCTCAAAAGCGTTGGCATGGTGAAAAACAAAGCCTGCCTGTACCGGAATTCTTTTTAT TTCTCCACCGTCCCTAGGAACGAGAATAATTTGAGCAGGTTTATCGGGATGAAATTGCAC ACATTCCCCTGCTCCTCGCAAACCGAAAAGGTAGGGTAACCCGTTGAGAGTAACGTTATT TTGCAGAAAAATGGCGTAATGGGGCGTGATCGCAAAATCATGAATAAAAGCAAAACCAGG AAAAGTTTCAGTTTTTTGCCGCAACAATTTACCCTGGGGGTCTAGCTCTAACAGGGTGAG GGTACTGCTCAAGCTGGATTTAATTGAAAAGGTCACATAGCAGGGTTGGCCCCCATCAAA AGTTGAAGCCGGATCAATGCGGGGATGGGCCGACAGGGGTTGCCCTTCCGCAAGAATGCC GCCCAAATCATCCAACCCAATGGTTGCTAAGTTTGATGGTTCCAAGCGATGGGGTTGTCC CCCTTCCCATAGGGCCAAGAGGCGATCGCCCCAGTAGGTAATGTTGGTGTTGGCAATGTT TTTTAGCCGTAAGTCAAAGATAGTTTTGAGCCAGCCCCCCGCCGGTTGGGAACCAAAGAC GCCCCGATAGATCATTTTTCCCGCTTTTTGCTCTTCCACGTAACCCTGGGTGCGGACAAA TTTGCTCTGGAAATGTACTCGACCGTCCCCAGGAAATTTAAAGGCTGTCACCATGCCGTC CCCGTCAAAGGGATGCTTCAAAGGGCGATCGCCAATTTCCAATAATCCAGGGCCGTTGCG ATAGAGCGTTCCCTGGAGGTCTGGGGGTATGCTCCCTTCCACGTCTTCGACCCAATAATC CCACTCCTGGGGCTGGGACTGGTAACCTCTCAGCCAATCCTGCGGACTGTAGGAGCGCTG CGATGGGGAACTGGTTGGGGGGGAAGTGACCAT PF03055 RPE65 "
drug:(1r)-4-[(1e,3e,5e,7z,9e,11z,13e,15e)-17-Hydroxy-3,7,12,16-Tetramethylheptadeca-1,3,5,7,9,11,13,15-Octaen-1-Yl]-3,5,5-Trimethylcyclohex-3-En-1-Olrdfs:label"(1r)-4-[(1e,3e,5e,7z,9e,11z,13e,15e)-17-Hydroxy-3,7,12,16-Tetramethylheptadeca-1,3,5,7,9,11,13,15-Octaen-1-Yl]-3,5,5-Trimethylcyclohex-3-En-1-Ol"
drug:(1r)-4-[(1e,3e,5e,7z,9e,11z,13e,15e)-17-Hydroxy-3,7,12,16-Tetramethylheptadeca-1,3,5,7,9,11,13,15-Octaen-1-Yl]-3,5,5-Trimethylcyclohex-3-En-1-Olowl:sameAsdrug:EXPT00185
drug:(1r)-4-[(1e,3e,5e,7z,9e,11z,13e,15e)-17-Hydroxy-3,7,12,16-Tetramethylheptadeca-1,3,5,7,9,11,13,15-Octaen-1-Yl]-3,5,5-Trimethylcyclohex-3-En-1-Olrdf:typedrugbank:drugs
drug:(1r,4s)-2-Azabornanedrugbank:description" experimental This compound belongs to the piperidines. These are compounds containing a piperidine ring, which is a saturated aliphatic six-member ring with one nitrogen atom and five carbon atoms. Piperidines Organic Compounds Heterocyclic Compounds Piperidines Pyrrolidines Polyamines Dialkylamines pyrrolidine secondary aliphatic amine polyamine secondary amine amine organonitrogen compound logP 2.06 ALOGPS logS -1.5 ALOGPS Water Solubility 4.38e+00 g/l ALOGPS logP 1.63 ChemAxon IUPAC Name (1S,4R)-1,7,7-trimethyl-2-azabicyclo[2.2.1]heptane ChemAxon Traditional IUPAC Name (1r,4s)-2-azabornane ChemAxon Molecular Weight 139.238 ChemAxon Monoisotopic Weight 139.136099549 ChemAxon SMILES CC1(C)[C@H]2CC[C@]1(C)NC2 ChemAxon Molecular Formula C9H17N ChemAxon InChI InChI=1S/C9H17N/c1-8(2)7-4-5-9(8,3)10-6-7/h7,10H,4-6H2,1-3H3/t7-,9-/m0/s1 ChemAxon InChIKey InChIKey=OLTRGBMOWPXXIG-CBAPKCEASA-N ChemAxon Polar Surface Area (PSA) 12.03 ChemAxon Refractivity 42.75 ChemAxon Polarizability 17.02 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 11.35 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 46936374 PubChem Substance 46509082 ChemSpider 3668001 PDB 2BN "
drug:(1r,4s)-2-Azabornanerdfs:label"(1r,4s)-2-Azabornane"
drug:(1r,4s)-2-Azabornaneowl:sameAsdrug:EXPT00106
drug:(1r,4s)-2-Azabornanerdf:typedrugbank:drugs
drug:(1s)-1(9-Deazahypoxanthin-9yl)1,4-Dideoxy-1,4-Imino-D-Ribitol-5-Phosphatedrugbank:description" experimental This compound belongs to the pyrrolopyrimidines. These are compounds containing a pyrrolopyrimidine moiety, which consists of a pyrrole ring fused to a pyrimidine. Pyrrolopyrimidines Organic Compounds Heterocyclic Compounds Pyrrolopyrimidines Pyrimidones Substituted Pyrroles Organic Phosphoric Acids Organophosphate Esters Pyrrolidines Secondary Alcohols 1,2-Diols 1,2-Aminoalcohols Dialkylamines Polyamines pyrimidone organic phosphate substituted pyrrole phosphoric acid ester pyrimidine pyrrolidine pyrrole 1,2-diol 1,2-aminoalcohol secondary alcohol polyamine secondary amine secondary aliphatic amine amine alcohol organonitrogen compound logP -1.9 ALOGPS logS -1.8 ALOGPS Water Solubility 5.19e+00 g/l ALOGPS logP -4.4 ChemAxon IUPAC Name {[(2S,3S,4S,5S)-3,4-dihydroxy-5-{4-oxopyrrolo[3,2-d]pyrimidin-7-yl}pyrrolidin-2-yl]methoxy}phosphonic acid ChemAxon Traditional IUPAC Name [(2S,3S,4S,5S)-3,4-dihydroxy-5-{4-oxopyrrolo[3,2-d]pyrimidin-7-yl}pyrrolidin-2-yl]methoxyphosphonic acid ChemAxon Molecular Weight 345.2252 ChemAxon Monoisotopic Weight 345.060010334 ChemAxon SMILES O[C@H]1[C@H](COP(O)(O)=O)N[C@H]([C@@H]1O)c1cnc2c1N=CNC2=O ChemAxon Molecular Formula C11H14N4O7P ChemAxon InChI InChI=1S/C11H14N4O7P/c16-9-5(2-22-23(19,20)21)15-7(10(9)17)4-1-12-8-6(4)13-3-14-11(8)18/h1,3,5,7,9-10,15-17H,2H2,(H,13,14,18)(H2,19,20,21)/t5-,7-,9-,10-/m0/s1 ChemAxon InChIKey InChIKey=BNBLIPPJYHOAER-YNAXYJCJSA-N ChemAxon Polar Surface Area (PSA) 177.89 ChemAxon Refractivity 72.38 ChemAxon Polarizability 30.21 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 9 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) 1.5 ChemAxon pKa (strongest basic) 8.68 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon PubChem Compound 46936297 PubChem Substance 46507599 PDB IRP BE0001516 Hypoxanthine-guanine-xanthine phosphoribosyltransferase Plasmodium falciparum (isolate FCR-3 / Gambia) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Hypoxanthine-guanine-xanthine phosphoribosyltransferase Nucleotide transport and metabolism Works with guanine, hypoxanthine and xanthine LACZ Cytoplasm None 7.49 26349.0 Plasmodium falciparum (isolate FCR-3 / Gambia) GenBank Gene Database X16279 GenBank Protein Database 9914 UniProtKB P20035 UniProt Accession HGXR_PLAFG EC 2.4.2.- HGPRT HGXPRT HGXPRTase >Hypoxanthine-guanine-xanthine phosphoribosyltransferase MPIPNNPGAGENAFDPVFVNDDDGYDLDSFMIPAHYKKYLTKVLVPNGVIKNRIEKLAYD IKKVYNNEEFHILCLLKGSRGFFTALLKHLSRIHNYSAVETSKPLFGEHYVRVKSYCNDQ STGTLEIVSEDLSCLKGKHVLIVEDIIDTGKTLVKFCEYLKKFEIKTVAIACLFIKRTPL WNGFKADFVGFSIPDHFVVGYSLDYNEIFRDLDHCCLVNDEGKKKYKATSL >696 bp ATGCCAATACCAAATAATCCAGGAGCTGGTGAAAATGCCTTTGATCCCGTTTTCGTAAAC GATGACGATGGTTATGACCTTGATTCTTTTATGATCCCTGCACATTATAAAAAATATCTT ACCAAGGTCTTAGTTCCAAATGGTGTCATAAAAAACCGTATTGAGAAATTGGCTTATGAT ATTAAAAAGGTGTACAACAATGAAGAGTTTCATATTCTTTGTTTGTTGAAAGGTTCTCGT GGTTTTTTCACTGCTCTCTTAAAGCATTTAAGTAGAATACATAATTATAGTGCCGTTGAG ACGTCCAAACCATTATTTGGAGAACACTACGTACGTGTGAAATCCTATTGTAATGACCAA TCAACAGGTACATTAGAAATTGTAAGTGAAGATTTATCTTGTTTAAAAGGAAAACATGTA TTAATTGTTGAAGATATTATTGATACTGGTAAAACATTAGTAAAGTTTTGTGAATACTTA AAGAAATTTGAAATAAAAACCGTTGCCATCGCTTGTCTTTTTATTAAAAGAACACCTTTG TGGAATGGTTTTAAAGCTGATTTCGTTGGATTCTCAATTCCTGATCACTTTGTTGTTGGT TATAGTTTAGACTATAATGAAATTTTCAGAGATCTTGACCATTGTTGTTTGGTTAATGAT GAGGGAAAAAAGAAATATAAAGCAACTTCATTATAA PF00156 Pribosyltran component cell component intracellular component cytoplasm function transferase activity function transferase activity, transferring glycosyl groups function transferase activity, transferring pentosyl groups function hypoxanthine phosphoribosyltransferase activity function catalytic activity process metabolism process purine salvage process cellular metabolism process purine ribonucleoside salvage process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process physiological process process nucleoside metabolism "
drug:(1s)-1(9-Deazahypoxanthin-9yl)1,4-Dideoxy-1,4-Imino-D-Ribitol-5-Phosphaterdfs:label"(1s)-1(9-Deazahypoxanthin-9yl)1,4-Dideoxy-1,4-Imino-D-Ribitol-5-Phosphate"
drug:(1s)-1(9-Deazahypoxanthin-9yl)1,4-Dideoxy-1,4-Imino-D-Ribitol-5-Phosphateowl:sameAsdrug:EXPT01929
drug:(1s)-1(9-Deazahypoxanthin-9yl)1,4-Dideoxy-1,4-Imino-D-Ribitol-5-Phosphaterdf:typedrugbank:drugs
drug:(1s)-1-(9-Deazaadenin-9-Yl)-1,4,5-Trideoxy-1,4-Imino-5-Methylthio-D-Ribitoldrugbank:description" experimental This compound belongs to the pyrrolopyrimidines. These are compounds containing a pyrrolopyrimidine moiety, which consists of a pyrrole ring fused to a pyrimidine. Pyrrolopyrimidines Organic Compounds Heterocyclic Compounds Pyrrolopyrimidines Substituted Pyrroles Pyrrolidines Secondary Alcohols 1,2-Aminoalcohols 1,2-Diols Polyamines Dialkylamines Thioethers Carboxamidines Monoalkylamines substituted pyrrole pyrrole pyrrolidine 1,2-aminoalcohol secondary alcohol 1,2-diol amidine secondary amine secondary aliphatic amine thioether polyamine carboxylic acid amidine primary aliphatic amine alcohol amine primary amine organonitrogen compound logP -1.6 ALOGPS logS -2.5 ALOGPS Water Solubility 8.76e-01 g/l ALOGPS logP -1.4 ChemAxon IUPAC Name (2S,3S,4R,5S)-2-[(4R)-4-amino-3H,4H,5H-pyrrolo[3,2-d]pyrimidin-7-yl]-5-[(methylsulfanyl)methyl]pyrrolidine-3,4-diol ChemAxon Traditional IUPAC Name (2S,3S,4R,5S)-2-[(4R)-4-amino-3H,4H,5H-pyrrolo[3,2-d]pyrimidin-7-yl]-5-[(methylsulfanyl)methyl]pyrrolidine-3,4-diol ChemAxon Molecular Weight 297.377 ChemAxon Monoisotopic Weight 297.125945567 ChemAxon SMILES CSC[C@H]1N[C@H]([C@H](O)[C@@H]1O)C1=CNC2=C1N=CN[C@H]2N ChemAxon Molecular Formula C12H19N5O2S ChemAxon InChI InChI=1S/C12H19N5O2S/c1-20-3-6-10(18)11(19)8(17-6)5-2-14-9-7(5)15-4-16-12(9)13/h2,4,6,8,10-12,14,17-19H,3,13H2,1H3,(H,15,16)/t6-,8+,10-,11+,12-/m1/s1 ChemAxon InChIKey InChIKey=YLCQGEBEQIBOOJ-XKBJCNPTSA-N ChemAxon Polar Surface Area (PSA) 118.69 ChemAxon Refractivity 79.17 ChemAxon Polarizability 31.06 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) 12.93 ChemAxon pKa (strongest basic) 8.64 ChemAxon Physiological Charge 2 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon PubChem Compound 46936314 PubChem Substance 46508814 PDB MTM BE0001128 S-methyl-5'-thioadenosine phosphorylase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown S-methyl-5'-thioadenosine phosphorylase Nucleotide transport and metabolism Plays a major role in polyamine metabolism and is important for the salvage of both adenine and methionine MTAP 9p21 Cytoplasm None 7.21 31236.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7413 GenAtlas MTAP GeneCards MTAP GenBank Gene Database U22233 GenBank Protein Database 847724 UniProtKB Q13126 UniProt Accession MTAP_HUMAN 5'- methylthioadenosine phosphorylase EC 2.4.2.28 MTA phosphorylase MTAPase >S-methyl-5-thioadenosine phosphorylase MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLAR HGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTMR PQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR AESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTL KENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH >852 bp ATGGCCTCTGGCACCACCACCACCGCCGTGAAGATTGGAATAATTGGTGGAACAGGCCTG GATGATCCAGAAATTTTAGAAGGAAGAACTGAAAAATATGTGGATACTCCATTTGGCAAG CCATCTGATGCCTTAATTTTGGGGAAGATAAAAAATGTTGATTGCATCCTCCTTGCAAGG CATGGAAGGCAGCACACCATCATGCCTTCAAAGGTCAACTACCAGGCGAACATCTGGGCT TTGAAGGAAGAGGGCTGTACACATGTCATAGTGACCACAGCTTGTGGCTCCTTGAGGGAG GAGATTCAGCCCGGCGATATTGTCATTATTGATCAGTTCATTGACAGGACCACTATGAGA CCTCAGTCCTTCTATGATGGAAGTCATTCTTGTGCCAGAGGAGTGTGCCATATTCCAATG GCTGAGCCGTTTTGCCCCAAAACGAGAGAGGTTCTTATAGAGACTGCTAAGAAGCTAGGA CTCCGGTGCCACTCAAAGGGGACAATGGTCACAATCGAGGGACCTCGTTTTAGCTCCCGG GCAGAAAGCTTCATGTTCCGCACCTGGGGGGCGGATGTTATCAACATGACCACAGTTCCA GAGGTGGTTCTTGCTAAGGAGGCTGGAATTTGTTACGCAAGTATCGCCATGGCGACAGAT TATGACTGCTGGAAGGAGCACGAGGAAGCAGTTTCGGTGGACCGGGTCTTAAAGACCCTG AAAGAAAACGCTAATAAAGCCAAAAGCTTACTGCTCACTACCATACCTCAGATAGGGTCC ACAGAATGGTCAGAAACCCTCCATAACCTGAAGAATATGGCCCAGTTTTCTGTTTTATTA CCAAGACATTAA BE0002007 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase Nucleotide transport and metabolism Responsible for cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) mtnN Cytoplasmic None 4.9 24354.0 Escherichia coli (strain K12) GenBank Gene Database U24438 GenBank Protein Database 2981267 UniProtKB P0AF12 UniProt Accession MTNN_ECOLI 5'-methylthioadenosine nucleosidase EC 3.2.2.9 P46 S-adenosylhomocysteine nucleosidase >MTA/SAH nucleosidase MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGAT LLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFK ADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAH VCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG >699 bp ATGAAAATCGGCATCATTGGTGCAATGGAAGAAGAAGTTACGCTGCTGCGTGACAAAATC GAAAACCGTCAAACTATCAGTCTCGGCGGTTGCGAAATCTATACCGGCCAACTGAATGGA ACCGAGGTTGCGCTTCTGAAATCGGGCATCGGTAAAGTCGCTGCGGCGCTGGGTGCCACT TTGCTGTTGGAACACTGCAAGCCAGATGTGATTATTAACACCGGTTCTGCCGGTGGCCTG GCACCAACGTTGAAAGTGGGCGATATCGTTGTCTCGGACGAAGCACGTTATCACGACGCG GATGTCACGGCATTTGGTTATGAATACGGTCAGTTACCAGGCTGTCCGGCAGGCTTTAAA GCTGACGATAAACTGATCGCTGCCGCTGAGGCCTGCATTGCCGAACTGAATCTTAACGCT GTACGTGGCCTGATTGTTAGCGGCGACGCTTTCATCAACGGTTCTGTTGGTCTGGCGAAA ATCCGCCACAACTTCCCACAGGCCATTGCTGTAGAGATGGAAGCGACGGCAATCGCCCAT GTCTGCCACAATTTCAACGTCCCGTTTGTTGTCGTACGCGCCATCTCCGACGTGGCCGAT CAACAGTCTCATCTTAGCTTCGATGAGTTCCTGGCTGTTGCCGCTAAACAGTCCAGCCTG ATGGTTGAGTCACTGGTGCAGAAACTTGCACATGGCTAA PF01048 PNP_UDP_1 function methylthioadenosine nucleosidase activity function adenosylhomocysteine nucleosidase activity function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing N-glycosyl compounds function catalytic activity process methionine metabolism process metabolism process cellular metabolism process amino acid metabolism process methionine salvage process amino acid and derivative metabolism process nucleoside catabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process nucleoside metabolism process sulfur amino acid metabolism process physiological process "
drug:(1s)-1-(9-Deazaadenin-9-Yl)-1,4,5-Trideoxy-1,4-Imino-5-Methylthio-D-Ribitolrdfs:label"(1s)-1-(9-Deazaadenin-9-Yl)-1,4,5-Trideoxy-1,4-Imino-5-Methylthio-D-Ribitol"
drug:(1s)-1-(9-Deazaadenin-9-Yl)-1,4,5-Trideoxy-1,4-Imino-5-Methylthio-D-Ribitolowl:sameAsdrug:EXPT02247
drug:(1s)-1-(9-Deazaadenin-9-Yl)-1,4,5-Trideoxy-1,4-Imino-5-Methylthio-D-Ribitolrdf:typedrugbank:drugs
drug:(1s,2s)-1-Amino-1-(1,3-Thiazol-2-Yl)Propan-2-Oldrugbank:description" experimental This compound belongs to the thiazoles. These are heterocyclic compounds containing a five-member aromatic ring made up of one sulfur atom, one nitrogen, and three carbon atoms. Thiazoles Organic Compounds Heterocyclic Compounds Azoles Thiazoles Secondary Alcohols 1,2-Aminoalcohols Polyamines Monoalkylamines 1,2-aminoalcohol secondary alcohol polyamine primary amine amine primary aliphatic amine alcohol organonitrogen compound logP -0.28 ALOGPS logS -1.4 ALOGPS Water Solubility 5.67e+00 g/l ALOGPS logP -0.23 ChemAxon IUPAC Name (1R,2R)-1-amino-1-(1,3-thiazol-2-yl)propan-2-ol ChemAxon Traditional IUPAC Name (1R,2R)-1-amino-1-(1,3-thiazol-2-yl)propan-2-ol ChemAxon Molecular Weight 158.221 ChemAxon Monoisotopic Weight 158.051383642 ChemAxon SMILES C[C@@H](O)[C@@H](N)C1=NC=CS1 ChemAxon Molecular Formula C6H10N2OS ChemAxon InChI InChI=1S/C6H10N2OS/c1-4(9)5(7)6-8-2-3-10-6/h2-5,9H,7H2,1H3/t4-,5-/m1/s1 ChemAxon InChIKey InChIKey=QWDNYLFSFTUIKH-RFZPGFLSSA-N ChemAxon Polar Surface Area (PSA) 59.14 ChemAxon Refractivity 39.52 ChemAxon Polarizability 15.97 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 14.54 ChemAxon pKa (strongest basic) 7.67 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 46936770 PubChem Substance 46505336 PDB XAA "
drug:(1s,2s)-1-Amino-1-(1,3-Thiazol-2-Yl)Propan-2-Olrdfs:label"(1s,2s)-1-Amino-1-(1,3-Thiazol-2-Yl)Propan-2-Ol"
drug:(1s,2s)-1-Amino-1-(1,3-Thiazol-2-Yl)Propan-2-Olowl:sameAsdrug:EXPT03250
drug:(1s,2s)-1-Amino-1-(1,3-Thiazol-2-Yl)Propan-2-Olrdf:typedrugbank:drugs
drug:(1s,3r,4r,6s)-1,3,4,6-Tetrapkisphosphatedrugbank:description" experimental This compound belongs to the inositol phosphates. These are compounds containing a phosphate group attached to an inositol (or cyclohexanehexol) moiety. Inositol Phosphates Organic Compounds Organooxygen Compounds Alcohols and Polyols Cyclic Alcohols and Derivatives Cyclohexanols Organophosphate Esters Organic Phosphoric Acids Polyamines cyclohexanol phosphoric acid ester organic phosphate secondary alcohol polyamine logP -0.45 ALOGPS logS -1.6 ALOGPS Water Solubility 1.15e+01 g/l ALOGPS logP -4.3 ChemAxon IUPAC Name {[(1S,2s,3R,4R,5s,6S)-2,5-dihydroxy-3,4,6-tris(phosphonooxy)cyclohexyl]oxy}phosphonic acid ChemAxon Traditional IUPAC Name [(1S,2s,3R,4R,5s,6S)-2,5-dihydroxy-3,4,6-tris(phosphonooxy)cyclohexyl]oxyphosphonic acid ChemAxon Molecular Weight 500.0755 ChemAxon Monoisotopic Weight 499.928709756 ChemAxon SMILES O[C@H]1[C@H](OP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@H](O)[C@@H](OP(O)(O)=O)[C@@H]1OP(O)(O)=O ChemAxon Molecular Formula C6H16O18P4 ChemAxon InChI InChI=1S/C6H16O18P4/c7-1-3(21-25(9,10)11)5(23-27(15,16)17)2(8)6(24-28(18,19)20)4(1)22-26(12,13)14/h1-8H,(H2,9,10,11)(H2,12,13,14)(H2,15,16,17)(H2,18,19,20)/t1-,2-,3-,4+,5-,6+ ChemAxon InChIKey InChIKey=ZAWIXNGTTZTBKV-NIPYSYMMSA-N ChemAxon Polar Surface Area (PSA) 307.5 ChemAxon Refractivity 79.27 ChemAxon Polarizability 34.16 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 14 ChemAxon H Bond Donor Count 10 ChemAxon pKa (strongest acidic) 0.35 ChemAxon Physiological Charge -8 ChemAxon Number of Rings 1 ChemAxon Bioavailability 0 ChemAxon PubChem Compound 121969 PubChem Substance 46506539 PDB I4P "
drug:(1s,3r,4r,6s)-1,3,4,6-Tetrapkisphosphaterdfs:label"(1s,3r,4r,6s)-1,3,4,6-Tetrapkisphosphate"
drug:(1s,3r,4r,6s)-1,3,4,6-Tetrapkisphosphateowl:sameAsdrug:EXPT01814
drug:(1s,3r,4r,6s)-1,3,4,6-Tetrapkisphosphaterdf:typedrugbank:drugs
drug:(1s,3s,4s)-1,3,4-Triphospho-Myo-Inositoldrugbank:description" experimental This compound belongs to the inositol phosphates. These are compounds containing a phosphate group attached to an inositol (or cyclohexanehexol) moiety. Inositol Phosphates Organic Compounds Organooxygen Compounds Alcohols and Polyols Cyclic Alcohols and Derivatives Cyclohexanols Organophosphate Esters Organic Phosphoric Acids 1,2-Diols Polyamines cyclohexanol phosphoric acid ester organic phosphate polyol 1,2-diol secondary alcohol polyamine logP -0.86 ALOGPS logS -1.4 ALOGPS Water Solubility 1.48e+01 g/l ALOGPS logP -4.2 ChemAxon IUPAC Name {[(1S,2R,3R,4S,5S,6S)-2,3,5-trihydroxy-4,6-bis(phosphonooxy)cyclohexyl]oxy}phosphonic acid ChemAxon Traditional IUPAC Name [(1S,2R,3R,4S,5S,6S)-2,3,5-trihydroxy-4,6-bis(phosphonooxy)cyclohexyl]oxyphosphonic acid ChemAxon Molecular Weight 420.0956 ChemAxon Monoisotopic Weight 419.962379346 ChemAxon SMILES O[C@@H]1[C@@H](O)[C@H](OP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@@H](O)[C@H]1OP(O)(O)=O ChemAxon Molecular Formula C6H15O15P3 ChemAxon InChI InChI=1S/C6H15O15P3/c7-1-2(8)5(20-23(13,14)15)6(21-24(16,17)18)3(9)4(1)19-22(10,11)12/h1-9H,(H2,10,11,12)(H2,13,14,15)(H2,16,17,18)/t1-,2-,3+,4+,5+,6+/m1/s1 ChemAxon InChIKey InChIKey=MMWCIQZXVOZEGG-MLQGYMEPSA-N ChemAxon Polar Surface Area (PSA) 260.97 ChemAxon Refractivity 68.39 ChemAxon Polarizability 29.69 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 12 ChemAxon H Bond Donor Count 9 ChemAxon pKa (strongest acidic) 0.54 ChemAxon pKa (strongest basic) -3.7 ChemAxon Physiological Charge -6 ChemAxon Number of Rings 1 ChemAxon Bioavailability 0 ChemAxon PubChem Compound 439455 PubChem Substance 46506250 ChemSpider 784 PDB I3S "
drug:(1s,3s,4s)-1,3,4-Triphospho-Myo-Inositolrdfs:label"(1s,3s,4s)-1,3,4-Triphospho-Myo-Inositol"
drug:(1s,3s,4s)-1,3,4-Triphospho-Myo-Inositolowl:sameAsdrug:EXPT01812
drug:(1s,3s,4s)-1,3,4-Triphospho-Myo-Inositolrdf:typedrugbank:drugs
drug:(1s,6s,7r,8r,8ar)-1,6,7,8-Tetrahydroxyindolizidinedrugbank:description" 79831-76-8 experimental This compound belongs to the indolizidines. These are polycyclic compounds containing an indolizidine, which is a bicyclic heterocycle containing a saturated six-member ring fused to a saturated five-member ring, one of the bridging atoms being nitrogen. Indolizidines Organic Compounds Heterocyclic Compounds Indolizidines Piperidines Pyrrolidines Tertiary Amines 1,2-Diols Secondary Alcohols Polyamines piperidine pyrrolidine tertiary amine secondary alcohol polyol 1,2-diol polyamine amine alcohol organonitrogen compound logP -2.1 ALOGPS logS 0.77 ALOGPS Water Solubility 1.11e+03 g/l ALOGPS logP -2.6 ChemAxon IUPAC Name (1S,6S,7R,8R,8aS)-octahydroindolizine-1,6,7,8-tetrol ChemAxon Traditional IUPAC Name (1S,6S,7R,8R,8aS)-octahydroindolizine-1,6,7,8-tetrol ChemAxon Molecular Weight 189.209 ChemAxon Monoisotopic Weight 189.100107973 ChemAxon SMILES O[C@H]1CCN2C[C@H](O)[C@@H](O)[C@H](O)[C@H]12 ChemAxon Molecular Formula C8H15NO4 ChemAxon InChI InChI=1S/C8H15NO4/c10-4-1-2-9-3-5(11)7(12)8(13)6(4)9/h4-8,10-13H,1-3H2/t4-,5-,6-,7+,8+/m0/s1 ChemAxon InChIKey InChIKey=JDVVGAQPNNXQDW-QYYLWSOASA-N ChemAxon Polar Surface Area (PSA) 84.16 ChemAxon Refractivity 44.44 ChemAxon Polarizability 18.68 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 12.89 ChemAxon pKa (strongest basic) 8.96 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 11063191 PubChem Substance 46507978 KEGG Compound C02256 ChemSpider 2494 PDB CTS BE0001345 Glucan 1,3-beta-glucosidase Yeast # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Glucan 1,3-beta-glucosidase Carbohydrate transport and metabolism Beta-glucanases participate in the metabolism of beta- glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase XOG1 Secreted protein None 5.37 50022.0 Yeast GenBank Gene Database X56556 GenBank Protein Database 578126 UniProtKB P29717 UniProt Accession EXG_CANAL EC 3.2.1.58 Exo-1,3-beta- glucanase Glucan 1,3-beta-glucosidase precursor >Glucan 1,3-beta-glucosidase precursor MQLSFILTSSVFILLLEFVKASVISNPFKPNGNLKFKRGGGHNVAWDYDNNVIRGVNLGG WFVLEPYMTPSLFEPFQNGNDQSGVPVDEYHWTQTLGKEAALRILQKHWSTWITEQDFKQ ISNLGLNFVRIPIGYWAFQLLDNDPYVQGQVQYLEKALGWARKNNIRVWIDLHGAPGSQN GFDNSGLRDSYNSQNGDNTQVTLNVLNTIFKKYGGNEYSDVVIGIELLNEPLGPVLNMDK LKQFFLDGYNSLRQTGSVTPVIIHDAFQVFGYWNNFLTVAEGQWNVVVDHHHYQVFSGGE LSRNINDHISVACNWGWDAKKESHWNVAGEWSAALTDCAKWLNGVNRGARYEGAYDNAPY IGSCQPMLDISQWSDEHKTDTRRYIEAQLDAFEYTGGWVFWSWKTENAPEWSFQTLTYNG LFPQPVTDRQFPNQCGFH >1317 bp ATGCAGTTATCATTTATCTTAACATCATCGGTATTTATATTATTGCTTGAATTTGTTAAA GCCCTGGTTATTTCTAATCCATTTAAACCAAATGGAAACTTGAAATTCAAGAGAGGAGGC GGACATAATGTTGCTTGGGATTATGATAATAATGTTATCAGAGGTGTCAATTTGGGTGGT TGGTTTGTCCTTGAACCATATATGACACCATCACTTTTTGAACCATTCCAAAATGGAAAT GATCAGTCTGGAGTTCCAGTTGACGAATATCACTGGACACAAACTTTGGGTAAGGAAGCT GCTCTGAGAATTTTGCAAAAACATTGGAGTACTTGGATCACTGAACAAGACTTTAAACAA ATTAGTAATTTGGGATTGAACTTTGTTCGTATTCCTATTGGTTATTGGGCTTTCCAATTG TTGGATAATGATCCATACGTCCAAGGTCAAGTTCAGTATTTGGAAAAGGCTTTGGGCTGG GCCAGAAAGAATAATATCAGAGTTTGGATTGATTTGCACGGTGCACCAGGCTCTCAAAAT GGGTTTGACAACTCCGGTTTAAGAGATAGCTACAATTTCCAAAACGGTGATAACACCCAA GTTACTTTGAATGTATTGAATACTATTTTCAAAAAGTATGGTGGCAACGAATACTCTGAC GTTGTTATTGGTATTGAATTGCTTAATGAACCATTGGGTCCAGTTTTGAATATGGATAAA TTGAAACAATTTTTCTTGGATGGTTACAACTCTCTTAGACAAACTGGATCAGTCACCCCA GTTATCATTCACGATGCTTTCCAAGTCTTTGGCTATTGGAATAACTTTTTGACTGTTGCT GAAGGTCAATGGAATGTTGTTGTTGACCATCATCATTACCAAGTGTTTTCCGGTGGTGAA TTATCTCGTAACATTAACGACCACATTTCAGTTGCTTGTAACTGGGGTTGGGATGCTAAA AAGGAATCCCATTGGAACGTCGCTGGTGAATGGTCTGCTGCTTTGACAGATTGTGCTAAA TGGTTGAATGGTGTCAACAGAGGAGCACGTTATGAGGGTGCTTACGATAATGCTCCATAC ATTGGATCCTGTCAACCATTGTTGGATATTTCCCAATGGTCTGATGAACACAAAACCGAC ACAAGAAGATACATTGAGGCTCAATTGGATGCTTTTGAATACACTGGAGGCTGGGTCTTC TGGAGTTGGAAGACTGAAAATGCCCCTGAATGGAGTTTCCAAACCTTGACTTACAATGGT CTTTTCCCACAACCAGTTACTGATAGACAATTCCCAAACCAATGTGGCTTTCACTGA PF00150 Cellulase function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity function hydrolase activity process carbohydrate metabolism process physiological process process metabolism process macromolecule metabolism "
drug:(1s,6s,7r,8r,8ar)-1,6,7,8-Tetrahydroxyindolizidinerdfs:label"(1s,6s,7r,8r,8ar)-1,6,7,8-Tetrahydroxyindolizidine"
drug:(1s,6s,7r,8r,8ar)-1,6,7,8-Tetrahydroxyindolizidineowl:sameAsdrug:EXPT01055
drug:(1s,6s,7r,8r,8ar)-1,6,7,8-Tetrahydroxyindolizidinerdf:typedrugbank:drugs
drug:(2,2-DIPHOSPHONOETHYL)(DODECYL)DIMETHYLPHOSPHONIUMdrugbank:description" experimental This compound belongs to the organic phosphonic acids. These are organic compounds containing phosphonic acid. Organic Phosphonic Acids Organic Compounds Organophosphorus Compounds Organic Phosphonic Acids and Derivatives Organic Phosphonic Acids Polyamines polyamine logP 3.02 ALOGPS logS -3.6 ALOGPS Water Solubility 1.14e-01 g/l ALOGPS logP 2.77 ChemAxon IUPAC Name [2-(dodecyldimethylphosphaniumyl)-1-phosphonoethyl]phosphonic acid ChemAxon Traditional IUPAC Name 2-(dodecyldimethylphosphaniumyl)-1-phosphonoethylphosphonic acid ChemAxon Molecular Weight 419.3906 ChemAxon Monoisotopic Weight 419.188123484 ChemAxon SMILES CCCCCCCCCCCC[P+](C)(C)CC(P(O)(O)=O)P(O)(O)=O ChemAxon Molecular Formula C16H38O6P3 ChemAxon InChI InChI=1S/C16H37O6P3/c1-4-5-6-7-8-9-10-11-12-13-14-23(2,3)15-16(24(17,18)19)25(20,21)22/h16H,4-15H2,1-3H3,(H3-,17,18,19,20,21,22)/p+1 ChemAxon InChIKey InChIKey=QCMHKGWUOSRYCF-UHFFFAOYSA-O ChemAxon Polar Surface Area (PSA) 115.06 ChemAxon Refractivity 104.31 ChemAxon Polarizability 43.69 ChemAxon Rotatable Bond Count 15 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 1.15 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 24836815 PubChem Substance 99443692 ChemSpider 22376377 PDB 742 BE0003570 Geranylgeranyl pyrophosphate synthase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Geranylgeranyl pyrophosphate synthase Coenzyme transport and metabolism Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins GGPS1 1q43 Cytoplasm None 6.06 34870.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:4249 GeneCards GGPS1 GenBank Gene Database AB017971 GenBank Protein Database 4520350 UniProtKB O95749 UniProt Accession GGPPS_HUMAN Dimethylallyltranstransferase Farnesyltranstransferase Geranylgeranyl diphosphate synthase Geranyltranstransferase GGPP synthetase GGPPSase >Geranylgeranyl pyrophosphate synthetase MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNAS LLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLL ELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTL GLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN IDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE PF00348 polyprenyl_synt process primary metabolism process lipid metabolism process cellular lipid metabolism process isoprenoid metabolism process isoprenoid biosynthesis process physiological process process metabolism "
drug:(2,2-DIPHOSPHONOETHYL)(DODECYL)DIMETHYLPHOSPHONIUMrdfs:label"(2,2-DIPHOSPHONOETHYL)(DODECYL)DIMETHYLPHOSPHONIUM"
drug:(2,2-DIPHOSPHONOETHYL)(DODECYL)DIMETHYLPHOSPHONIUMrdf:typedrugbank:drugs
drug:(2,6-DIMETHYL-PHENOXY)-ACETIC ACIDdrugbank:description" experimental This compound belongs to the phenoxyacetic acid derivatives. These are compounds containing an anisole where the methane group is linked to an acetic acid or a derivative. Phenoxyacetic Acid Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenoxyacetic Acid Derivatives Phenol Ethers Toluenes Alkyl Aryl Ethers Polyols Enolates Carboxylic Acids Polyamines phenol ether alkyl aryl ether toluene polyol polyamine ether carboxylic acid carboxylic acid derivative enolate logP 2.07 ALOGPS logS -2.2 ALOGPS Water Solubility 1.17e+00 g/l ALOGPS logP 2.32 ChemAxon IUPAC Name 2-(2,6-dimethylphenoxy)acetic acid ChemAxon Traditional IUPAC Name 2,6-dimethylphenoxyacetic acid ChemAxon Molecular Weight 180.2005 ChemAxon Monoisotopic Weight 180.07864425 ChemAxon SMILES CC1=CC=CC(C)=C1OCC(O)=O ChemAxon Molecular Formula C10H12O3 ChemAxon InChI InChI=1S/C10H12O3/c1-7-4-3-5-8(2)10(7)13-6-9(11)12/h3-5H,6H2,1-2H3,(H,11,12) ChemAxon InChIKey InChIKey=MLBCURLNKYKBEQ-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 46.53 ChemAxon Refractivity 48.69 ChemAxon Polarizability 18.84 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 4.04 ChemAxon pKa (strongest basic) -4.9 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 101369 PubChem Substance 99444105 ChemSpider 91599 PDB DBA BE0001732 Gag-Pol polyprotein HIV-2 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Gag-Pol polyprotein Involved in RNA binding Integrase performs the integration of the newly synthesized dsDNA copy of the viral genome into the host chromosome. The integrated DNA is called provirus gag-pol Nucleus. Cytoplasm (By similarity). Note=Following virus entry, the nuclear localization signal (NLS None 8.67 164647.0 HIV-2 GenBank Gene Database X05291 UniProtKB P04584 UniProt Accession POL_HV2RO Pr160Gag-Pol >Gag-Pol polyprotein MGARNSVLRGKKADELERIRLRPGGKKKYRLKHIVWAANKLDRFGLAESLLESKEGCQKI LTVLDPMVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVRRHLVAETGTAEKMPS TSRPTAPSSEKGGNYPVQHVGGNYTHIPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEG CTPYDINQMLNCVGDHQAAMQIIREIINEEAAEWDVQHPIPGPLPAGQLREPRGSDIAGT TSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDIKQGPKEPFQSYVD RFYKSLRAEQTDPAVKNWMTQTLLVQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQ KARLMAEALKEVIGPAPIPFAAAQQRKAFKCWNCGKEGHSARQCRAPRRQGCWKCGKPGH IMTNCPDRQAGFLRTGPLGKEAPQLPRGPSSAGADTNSTPSGSSSGSTGEIYAAREKTER AERETIQGSDRGLTAPRAGGDTIQGATNRGLAAPQFSLWKRPVVTAYIEGQPVEVLLDTG ADDSIVAGIELGNNYSPKIVGGIGGFINTKEYKNVEIEVLNKKVRATIMTGDTPINIFGR NILTALGMSLNLPVAKVEPIKIMLKPGKDGPKLRQWPLTKEKIEALKEICEKMEKEGQLE EAPPTNPYNTPTFAIKKKDKNKWRMLIDFRELNKVTQDFTEIQLGIPHPAGLAKKRRITV LDVGDAYFSIPLHEDFRPYTAFTLPSVNNAEPGKRYIYKVLPQGWKGSPAIFQHTMRQVL EPFRKANKDVIIIQYMDDILIASDRTDLEHDRVVLQLKELLNGLGFSTPDEKFQKDPPYH WMGYELWPTKWKLQKIQLPQKEIWTVNDIQKLVGVLNWAAQLYPGIKTKHLCRLIRGKMT LTEEVQWTELAEAELEENRIILSQEQEGHYYQEEKELEATVQKDQENQWTYKIHQEEKIL KVGKYAKVKNTHTNGIRLLAQVVQKIGKEALVIWGRIPKFHLPVEREIWEQWWDNYWQVT WIPDWDFVSTPPLVRLAFNLVGDPIPGAETFYTDGSCNRQSKEGKAGYVTDRGKDKVKKL EQTTNQQAELEAFAMALTDSGPKVNIIVDSQYVMGISASQPTESESKIVNQIIEEMIKKE AIYVAWVPAHKGIGGNQEVDHLVSQGIRQVLFLEKIEPAQEEHEKYHSNVKELSHKFGIP NLVARQIVNSCAQCQQKGEAIHGQVNAELGTWQMDCTHLEGKIIIVAVHVASGFIEAEVI PQESGRQTALFLLKLASRWPITHLHTDNGANFTSQEVKMVAWWIGIEQSFGVPYNPQSQG VVEAMNHHLKNQISRIREQANTIETIVLMAIHCMNFKRRGGIGDMTPSERLINMITTEQE IQFLQAKNSKLKDFRVYFREGRDQLWKGPGELLWKGEGAVLVKVGTDIKIIPRRKAKIIR DYGGRQEMDSGSHLEGAREDGEMA PF00078 RVT_1 PF00540 Gag_p17 PF00607 Gag_p24 PF00552 Integrase PF02022 Integrase_Zn PF00075 RnaseH PF00665 rve PF00077 RVP PF06815 RVT_connect PF06817 RVT_thumb PF00098 zf-CCHC function endoribonuclease activity, producing 5'-phosphomonoesters function catalytic activity function nucleic acid binding function ribonuclease H activity function RNA binding function structural molecule activity function nucleotidyltransferase activity function integrase activity function hydrolase activity function aspartic-type endopeptidase activity function ion binding function cation binding function peptidase activity function nuclease activity function transition metal ion binding function endopeptidase activity function RNA-directed DNA polymerase activity function transferase activity function binding function endonuclease activity function zinc ion binding function hydrolase activity, acting on ester bonds function endoribonuclease activity function transferase activity, transferring phosphorus-containing groups function DNA binding process DNA replication process metabolism process DNA metabolism process RNA-dependent DNA replication process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA recombination process macromolecule metabolism process DNA integration process protein metabolism process cellular protein metabolism process viral life cycle process proteolysis process physiological process "
drug:(2,6-DIMETHYL-PHENOXY)-ACETIC ACIDrdfs:label"(2,6-DIMETHYL-PHENOXY)-ACETIC ACID"
drug:(2,6-DIMETHYL-PHENOXY)-ACETIC ACIDrdf:typedrugbank:drugs
drug:(2-ACETYL-5-METHYLANILINO)(2,6-DIBROMOPHENYL)ACETAMIDEdrugbank:description" experimental This compound belongs to the alpha amino acid amides. These are amide derivatives of alpha amino acids. Alpha Amino Acid Amides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Acetophenones Benzoyl Derivatives Toluenes Bromobenzenes Aryl Bromides Primary Carboxylic Acid Amides Ketones Carboxylic Acids Enolates Polyamines Secondary Amines Organobromides acetophenone benzoyl toluene bromobenzene aryl bromide aryl halide benzene carboxamide group ketone primary carboxylic acid amide enolate secondary amine carboxylic acid polyamine organobromide organohalogen carbonyl group amine organonitrogen compound logP 4.21 ALOGPS logS -5.6 ALOGPS Water Solubility 1.04e-03 g/l ALOGPS logP 4.31 ChemAxon IUPAC Name (2S)-2-[(2-acetyl-5-methylphenyl)amino]-2-(2,6-dibromophenyl)acetamide ChemAxon Traditional IUPAC Name (2S)-2-[(2-acetyl-5-methylphenyl)amino]-2-(2,6-dibromophenyl)acetamide ChemAxon Molecular Weight 440.129 ChemAxon Monoisotopic Weight 437.95785306 ChemAxon SMILES [H][C@@](NC1=CC(C)=CC=C1C(C)=O)(C(N)=O)C1=C(Br)C=CC=C1Br ChemAxon Molecular Formula C17H16Br2N2O2 ChemAxon InChI InChI=1S/C17H16Br2N2O2/c1-9-6-7-11(10(2)22)14(8-9)21-16(17(20)23)15-12(18)4-3-5-13(15)19/h3-8,16,21H,1-2H3,(H2,20,23)/t16-/m0/s1 ChemAxon InChIKey InChIKey=FELUFXCUIYHAPB-INIZCTEOSA-N ChemAxon Polar Surface Area (PSA) 72.19 ChemAxon Refractivity 99.21 ChemAxon Polarizability 37 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 12.16 ChemAxon pKa (strongest basic) -0.67 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 446106 PubChem Substance 99443798 ChemSpider 393550 PDB AAA BE0002050 Gag-Pol polyprotein HIV-1 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Gag-Pol polyprotein Integrase performs the integration of the newly synthesized dsDNA copy of the viral genome into the host chromosome. The integrated DNA is called provirus gag-pol Nucleus. Cytoplasm (By similarity). Note=Following virus entry, the nuclear localization signal (NLS None 9.11 163290.0 HIV-1 GenBank Gene Database M15654 GenBank Protein Database 326388 UniProtKB P03366 UniProt Accession POL_HV1B1 CA Capsid protein p24 EC 2.7.7.49 EC 2.7.7.7 EC 3.1.26.4 EC 3.4.23.16 IN] Integrase MA NC Nucleocapsid protein p7 p15 p51 RT p6-pol p6* p66 RT PR Pr160Gag-Pol[Contains: Matrix protein p17 Protease Retropepsin Reverse transcriptase/ribonuclease H Spacer peptide p2 TF Transframe peptide >Gag-Pol polyprotein MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQI LGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAA DTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGAT PQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTT STLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRF YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKA RVLAEAMSQVTNTATIMMQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEG HQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTISSEQTRANSPTRRELQVWGR DNNSPSEAGADRQGTVSFNFPQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPG RWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFP ISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVF AIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLD EDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIY QYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTV QPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAEL ELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAH TNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPP LVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQA IYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKG IGGNEQVDKLVSAGIRKILFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCD KCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFL LKLAGRWPVKTIHTDNGSNFTSATVKAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKI IGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQ NFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCV ASRQDED >1539 bp ATGGGTGCGAGAGCGTCAGTATTAAGCGGGGGAGAATTAGATCGATGGGAAAAAATTCGG TTAAGGCCAGGGGGAAAGAAAAAATATAAATTAAAACATATAGTATGGGCAAGCAGGGAG CTAGAACGATTCGCAGTTAATCCTGGCCTGTTAGAAACATCAGAAGGCTGTAGACAAATA CTGGGACAGCTACAACCATCCCTTCAGACAGGATCAGAAGAACTTAGATCATTATATAAT ACAGTAGCAACCCTCTATTGTGTGCATCAAAGGATAGAGATAAAAGACACCAAGGAAGCT TTAGACAAGATAGAGGAAGAGCAAAACAAAAGTAAGAAAAAAGCACAGCAAGCAGCAGCT GACACAGGACACAGCAGTCAGGTCAGCCAAAATTACCCTATAGTGCAGAACATCCAGGGG CAAATGGTACATCAGGCCATATCACCTAGAACTTTAAATGCATGGGTAAAAGTAGTAGAA GAGAAGGCTTTCAGCCCAGAAGTAATACCCATGTTTTCAGCATTATCAGAAGGAGCCACC CCACAAGATTTAAACACCATGCTAAACACAGTGGGGGGACATCAAGCAGCCATGCAAATG TTAAAAGAGACCATCAATGAGGAAGCTGCAGAATGGGATAGAGTACATCCAGTGCATGCA GGGCCTATTGCACCAGGCCAGATGAGAGAACCAAGGGGAAGTGACATAGCAGGAACTACT AGTACCCTTCAGGAACAAATAGGATGGATGACAAATAATCCACCTATCCCAGTAGGAGAA ATTTATAAAAGATGGATAATCCTGGGATTAAATAAAATAGTAAGAATGTATAGCCCTACC AGCATTCTGGACATAAGACAAGGACCAAAAGAACCTTTTAGAGACTATGTAGACCGGTTC TATAAAACTCTAAGAGCCGAGCAAGCTTCACAGGAGGTAAAAAATTGGATGACAGAAACC TTGTTGGTCCAAAATGCGAACCCAGATTGTAAGACTATTTTAAAAGCATTGGGACCAGCG GCTACACTAGAAGAAATGATGACAGCATGTCAGGGAGTAGGAGGACCCGGCCATAAGGCA AGAGTTTTGGCTGAAGCAATGAGCCAAGTAACAAATACAGCTACCATAATGATGCAGAGA GGCAATTTTAGGAACCAAAGAAAGATGGTTAAGTGTTTCAATTGTGGCAAAGAAGGGCAC ACAGCCAGAAATTGCAGGGCCCCTAGGAAAAAGGGCTGTTGGAAATGTGGAAAGGAAGGA CACCAAATGAAAGATTGTACTGAGAGACAGGCTAATTTTTTAGGGAAGATCTGGCCTTCC TACAAGGGAAGGCCAGGGAATTTTCTTCAGAGCAGACCAGAGCCAACAGCCCCACCATTT CTTCAGAGCAGACCAGAGCCAACAGCCCCACCAGAAGAGAGCTTCAGGTCTGGGGTAGAG ACAACAACTCCCCCTCAGAAGCAGGAGCCGATAGACAAGGAACTGTATCCTTTAACTTCC CTCAGATCACTCTTTGGCAACGACCCCTCGTCACAATAA PF00078 RVT_1 PF00540 Gag_p17 PF00607 Gag_p24 PF00552 Integrase PF02022 Integrase_Zn PF00075 RnaseH PF00665 rve PF00077 RVP PF06815 RVT_connect PF06817 RVT_thumb PF00098 zf-CCHC function nucleotidyltransferase activity function hydrolase activity function integrase activity function aspartic-type endopeptidase activity function ion binding function cation binding function peptidase activity function nuclease activity function transition metal ion binding function endopeptidase activity function RNA-directed DNA polymerase activity function transferase activity function binding function endonuclease activity function zinc ion binding function hydrolase activity, acting on ester bonds function endoribonuclease activity function transferase activity, transferring phosphorus-containing groups function DNA binding function catalytic activity function endoribonuclease activity, producing 5'-phosphomonoesters function nucleic acid binding function ribonuclease H activity function RNA binding function structural molecule activity process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA recombination process macromolecule metabolism process DNA integration process protein metabolism process cellular protein metabolism process viral life cycle process proteolysis process physiological process process DNA replication process metabolism process DNA metabolism process cellular metabolism process RNA-dependent DNA replication BE0003804 Gag-Pol polyprotein HIV-1 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Gag-Pol polyprotein Involved in aspartic-type endopeptidase activity Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre- integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allow the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity) gag-pol Integrase:Virion (Potential). Host nucleus (Potential). Host cytoplasm (Potential) None 9.02 163278.4 HIV-1 GeneCards gag-pol GenBank Gene Database K02013 GenBank Protein Database 326420 UniProtKB P03367 UniProt Accession POL_HV1BR CA Capsid protein p24 IN Integrase MA Matrix protein p17 NC Nucleocapsid protein p7 p15 p51 RT p6-pol p6* p66 RT PR Pr160Gag-Pol Protease Retropepsin Reverse transcriptase/ribonuclease H Spacer peptide p2 TF Transframe peptide >Gag-Pol polyprotein MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQI LGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAA DTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGAT PQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTT STLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRF YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKA RVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGHIARNCRAPRKKGCWKCGKEG HQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTISSEQTRANSPTRRELQVWGR DNNSLSEAGADRQGTVSFNFPQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPG RWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFP ISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVF AIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLD EDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIY QYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTV QPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAEL ELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARTRGAH TNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPP LVKLWYQLEKEPIVGAETFYVDGAASRETKLGKAGYVTNRGRQKVVTLTDTTNQKTELQA IHLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKG IGGNEQVDKLVSAGIRKVLFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCD KCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFL LKLAGRWPVKTIHTDNGSNFTSTTVKAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKI IGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQ NFRVYYRDSRDPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCV ASRQDED >1539 bp CGGAGGCTAGAAGGAGAGAGATGGGTGCGAGAGCGTCAGTATTAAGCGGGGGAGAATTAG ATCGATGGGAAAAAATTCGGTTAAGGCCAGGGGGAAAGAAAAAATATAAATTAAAACATA TAGTATGGGCAAGCAGGGAGCTAGAACGATTCGCAGTTAATCCTGGCCTGTTAGAAACAT CAGAAGGCTGTAGACAAATACTGGGACAGCTACAACCATCCCTTCAGACAGGATCAGAAG AACTTAGATCATTATATAATACAGTAGCAACCCTCTATTGTGTGCATCAAAGGATAGAGA TAAAAGACACCAAGGAAGCTTTAGACAAGATAGAGGAAGAGCAAAACAAAAGTAAGAAAA AAGCACAGCAAGCAGCAGCTGACACAGGACACAGCAGCCAGGTCAGCCAAAATTACCCTA TAGTGCAGAACATCCAGGGGCAAATGGTACATCAGGCCATATCACCTAGAACTTTAAATG CATGGGTAAAAGTAGTAGAAGAGAAGGCTTTCAGCCCAGAAGTGATACCCATGTTTTCAG CATTATCAGAAGGAGCCACCCCACAAGATTTAAACACCATGCTAAACACAGTGGGGGGAC ATCAAGCAGCCATGCAAATGTTAAAAGAGACCATCAATGAGGAAGCTGCAGAATGGGATA GAGTGCATCCAGTGCATGCAGGGCCTATTGCACCAGGCCAGATGAGAGAACCAAGGGGAA GTGACATAGCAGGAACTACTAGTACCCTTCAGGAACAAATAGGATGGATGACAAATAATC CACCTATCCCAGTAGGAGAAATTTATAAAAGATGGATAATCCTGGGATTAAATAAAATAG TAAGAATGTATAGCCCTACCAGCATTCTGGACATAAGACAAGGACCAAAAGAACCCTTTA GAGACTATGTAGACCGGTTCTATAAAACTCTAAGAGCCGAGCAAGCTTCACAGGAGGTAA AAAATTGGATGACAGAAACCTTGTTGGTCCAAAATGCGAACCCAGATTGTAAGACTATTT TAAAAGCATTGGGACCAGCAGCTACACTAGAAGAAATGATGACAGCATGTCAGGGAGTGG GAGGACCCGGCCATAAGGCAAGAGTTTTGGCTGAAGCAATGAGCCAAGTAACAAATTCAG CTACCATAATGATGCAAAGAGGCAATTTTAGGAACCAAAGAAAGATTGTTAAGTGTTTCA ATTGTGGCAAAGAAGGGCACATAGCCAGAAATTGCAGGGCCCCTAGGAAAAAGGGCTGTT GGAAATGTGGAAAGGAAGGACACCAAATGAAAGATTGTACTGAGAGACAGGCTAATTTTT TAGGGAAGATCTGGCCTTCCTACAAGGGAAGGCCAGGGAATTTTCTTCAGAGCAGACCAG AGCCAACAGCCCCACCATTTCTTCAGAGCAGACCAGAGCCAACAGCCCCACCAGAAGAGA GCTTCAGGTCTGGGGTAGAGACAACAACTCCCTCTCAGAAGCAGGAGCCGATAGACAAGG AACTGTATCCTTTAACTTCCCTCAGATCACTCTTTGGCA PF00078 RVT_1 PF00540 Gag_p17 PF00607 Gag_p24 PF00552 Integrase PF02022 Integrase_Zn PF00075 RnaseH PF00665 rve PF00077 RVP PF06815 RVT_connect PF06817 RVT_thumb PF00098 zf-CCHC function endoribonuclease activity, producing 5'-phosphomonoesters function catalytic activity function nucleic acid binding function ribonuclease H activity function RNA binding function structural molecule activity function nucleotidyltransferase activity function integrase activity function hydrolase activity function aspartic-type endopeptidase activity function ion binding function cation binding function peptidase activity function nuclease activity function transition metal ion binding function endopeptidase activity function RNA-directed DNA polymerase activity function transferase activity function binding function endonuclease activity function zinc ion binding function hydrolase activity, acting on ester bonds function endoribonuclease activity function transferase activity, transferring phosphorus-containing groups function DNA binding process DNA replication process metabolism process DNA metabolism process RNA-dependent DNA replication process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA recombination process macromolecule metabolism process DNA integration process protein metabolism process cellular protein metabolism process viral life cycle process proteolysis process physiological process "
drug:(2-ACETYL-5-METHYLANILINO)(2,6-DIBROMOPHENYL)ACETAMIDErdfs:label"(2-ACETYL-5-METHYLANILINO)(2,6-DIBROMOPHENYL)ACETAMIDE"
drug:(2-ACETYL-5-METHYLANILINO)(2,6-DIBROMOPHENYL)ACETAMIDErdf:typedrugbank:drugs
drug:(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONEdrugbank:description" experimental This compound belongs to the acetophenones. These are organic compounds containing the acetophenone structure. Acetophenones Organic Compounds Benzenoids Benzene and Substituted Derivatives Acetophenones Benzoyl Derivatives 2,5-disubstituted Oxazoles Bromobenzenes Primary Aromatic Amines Aryl Bromides Ketones Polyamines Enolates Organobromides benzoyl 2,5-disubstituted 1,3-oxazole bromobenzene primary aromatic amine aryl halide aryl bromide azole oxazole ketone enolate polyamine carbonyl group organohalogen primary amine organobromide organonitrogen compound amine logP 2.05 ALOGPS logS -3 ALOGPS Water Solubility 3.03e-01 g/l ALOGPS logP 1.92 ChemAxon IUPAC Name 5-[(3-bromophenyl)carbonyl]-1,3-oxazol-2-amine ChemAxon Traditional IUPAC Name 5-[(3-bromophenyl)carbonyl]-1,3-oxazol-2-amine ChemAxon Molecular Weight 267.079 ChemAxon Monoisotopic Weight 265.969090125 ChemAxon SMILES NC1=NC=C(O1)C(=O)C1=CC(Br)=CC=C1 ChemAxon Molecular Formula C10H7BrN2O2 ChemAxon InChI InChI=1S/C10H7BrN2O2/c11-7-3-1-2-6(4-7)9(14)8-5-13-10(12)15-8/h1-5H,(H2,12,13) ChemAxon InChIKey InChIKey=YDCMMVTWXORJGO-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 69.12 ChemAxon Refractivity 59.02 ChemAxon Polarizability 22.1 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 13.58 ChemAxon pKa (strongest basic) 1.32 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 25271554 PubChem Substance 99444785 PDB OA1 BE0004154 Biotin carboxylase Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Biotin carboxylase Lipid transport and metabolism This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA accC None 7.12 49320.3 Escherichia coli (strain K12) GeneCards accC GenBank Gene Database M79446 GenBank Protein Database 145896 UniProtKB P24182 UniProt Accession ACCC_ECOLI ACC Acetyl-CoA carboxylase subunit A >Biotin carboxylase MLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADETVCIGPAPSVKSY LNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVERSGFIFIGPKAETIRLMGDKVSAI AAMKKAGVPCVPGSDGPLGDDMDKNRAIAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQ SISMTRAEAKAAFSNDMVYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVV EEAPAPGITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEHPVT EMITGVDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTFLPSPGKITRFHAP GGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDVAIARMKNALQELIIDGIKTNVDL QIRIMNDENFQHGGTNIHYLEKKLGLQEK >1350 bp ATGCTGGATAAAATTGTTATTGCCAACCGCGGCGAGATTGCATTGCGTATTCTTCGTGCC TGTAAAGAACTGGGCATCAAGACTGTCGCTGTGCACTCCAGCGCGGATCGCGATCTAAAA CACGTATTACTGGCAGATGAAACGGTCTGTATTGGCCCTGCTCCGTCAGTAAAAAGTTAT CTGAACATCCCGGCAATCATCAGCGCCGCTGAAATCACCGGCGCAGTAGCAATCCATCCG GGTTACGGCTTCCTCTCCGAGAACGCCAACTTTGCCGAGCAGGTTGAACGCTCCGGCTTT ATCTTCATTGGCCCGAAAGCAGAAACCATTCGCCTGATGGGCGACAAAGTATCCGCAATC GCGGCGATGAAAAAAGCGGGCGTCCCTTGCGTACCGGGTTCTGACGGCCCGCTGGGCGAC GATATGGATAAAAACCGTGCCATTGCTAAACGCATTGGTTATCCGGTGATTATCAAAGCC TCCGGCGGCGGCGGCGGTCGCGGTATGCGCGTAGTGCGCGGCGACGCTGAACTGGCACAA TCCATCTCCATGACCCGTGCGGAAGCGAAAGCTGCTTTCAGCAACGATATGGTTTACATG GAGAAATACCTGGAAAATCCTCGCCACGTCGAGATTCAGGTACTGGCTGACGGTCAGGGC AACGCTATCTATCTGGCGGAACGTGACTGCTCCATGCAACGCCGCCACCAGAAAGTGGTC GAAGAAGCGCCAGCACCGGGCATTACCCCGGAACTGCGTCGCTACATCGGCGAACGTTGC GCTAAAGCGTGTGTTGATATCGGCTATCGCGGTGCAGGTACTTTCGAGTTCCTGTTCGAA AACGGCGAGTTCTATTTCATCGAAATGAACACCCGTATTCAGGTAGAACACCCGGTTACA GAAATGATCACCGGCGTTGACCTGATCAAAGAACAGATGCGTATCGCTGCCGGTCAACCG CTGTCGATCAAGCAAGAAGAAGTTCACGTTCGCGGCCATGCGGTGGAATGTCGTATCAAC GCCGAAGATCCGAACACCTTCCTGCCAAGTCCGGGCAAAATCACCCGTTTCCACGCACCT GGCGGTTTTGGCGTACGTTGGGAGTCTCATATCTACGCGGGCTACACCGTACCGCCGTAC TATGACTCAATGATCGGTAAGCTGATTTGCTACGGTGAAAACCGTGACGTGGCGATTGCC CGCATGAAGAATGCGCTGCAGGAGCTGATCATCGACGGTATCAAAACCAACGTTGATCTG CAGATCCGCATCATGAATGACGAGAACTTCCAGCATGGTGGCACTAACATCCACTATCTG GAGAAAAAACTCGGTCTTCAGGAAAAATAA PF02785 Biotin_carb_C PF00289 CPSase_L_chain PF02786 CPSase_L_D2 function ATP binding function ligase activity function biotin binding function binding function catalytic activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function vitamin binding process physiological process process metabolism "
drug:(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONErdfs:label"(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONE"
drug:(2-AMINO-1,3-OXAZOL-5-YL)-(3-BROMOPHENYL)METHANONErdf:typedrugbank:drugs
drug:(2-AMINO-3-PHENYL-BICYCLO[2.2.1]HEPT-2-YL)-PHENYL-METHANONEdrugbank:description" experimental This compound belongs to the linear diarylheptanoids. These are diarylheptanoids with an open heptane chain. The two aromatic rings are linked only by the heptane chain. Linear Diarylheptanoids Organic Compounds Phenylpropanoids and Polyketides Diarylheptanoids Linear Diarylheptanoids Chalcones and Dihydrochalcones Acetophenones Benzoyl Derivatives Ketones Enolates Polyamines Monoalkylamines chalcone or dihydrochalcone acetophenone benzoyl benzene ketone enolate polyamine amine primary aliphatic amine carbonyl group primary amine organonitrogen compound logP 3.56 ALOGPS logS -5 ALOGPS Water Solubility 3.23e-03 g/l ALOGPS logP 3.88 ChemAxon IUPAC Name (1R,2R,3S,4S)-2-benzoyl-3-phenylbicyclo[2.2.1]heptan-2-amine ChemAxon Traditional IUPAC Name (1R,2R,3S,4S)-2-benzoyl-3-phenylbicyclo[2.2.1]heptan-2-amine ChemAxon Molecular Weight 291.3868 ChemAxon Monoisotopic Weight 291.162314299 ChemAxon SMILES [H][C@]12CC[C@]([H])(C1)[C@](N)(C(=O)C1=CC=CC=C1)[C@]2([H])C1=CC=CC=C1 ChemAxon Molecular Formula C20H21NO ChemAxon InChI InChI=1S/C20H21NO/c21-20(19(22)15-9-5-2-6-10-15)17-12-11-16(13-17)18(20)14-7-3-1-4-8-14/h1-10,16-18H,11-13,21H2/t16-,17+,18+,20+/m0/s1 ChemAxon InChIKey InChIKey=XJQDTOANLAPEIM-JRBPQWBISA-N ChemAxon Polar Surface Area (PSA) 43.09 ChemAxon Refractivity 88.06 ChemAxon Polarizability 32.19 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 7.94 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 446476 PubChem Substance 99444354 ChemSpider 393817 PDB HBC BE0002815 Ig gamma-1 chain C region Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Ig gamma-1 chain C region IGHG1 14q32.33 None 8.31 36106.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:5525 GenAtlas IGHG1 UniProtKB P01857 UniProt Accession IGHG1_HUMAN >Ig gamma-1 chain C region ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYN STYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDE LTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRW QQGNVFSCSVMHEALHNHYTQKSLSLSPGK PF07654 C1-set "
drug:(2-AMINO-3-PHENYL-BICYCLO[2.2.1]HEPT-2-YL)-PHENYL-METHANONErdfs:label"(2-AMINO-3-PHENYL-BICYCLO[2.2.1]HEPT-2-YL)-PHENYL-METHANONE"
drug:(2-AMINO-3-PHENYL-BICYCLO[2.2.1]HEPT-2-YL)-PHENYL-METHANONErdf:typedrugbank:drugs
drug:(2-BROMOETHYL)(2-'FORMYL-4'-AMINOPHENYL) ACETATEdrugbank:description" experimental This compound belongs to the phenylacetic acid derivatives. These are compounds containing a phenylacetic acid moiety, which consists of a phenyl group substituted at the second position by an acetic acid. Phenylacetic Acid Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenylacetic Acid Derivatives Benzoyl Derivatives Anilines Primary Aromatic Amines Carboxylic Acid Esters Enolates Ethers Polyamines Organobromides Alkyl Bromides Aldehydes benzoyl aniline primary aromatic amine carboxylic acid ester carboxylic acid derivative polyamine enolate ether organohalogen organobromide amine primary amine organonitrogen compound alkyl halide alkyl bromide aldehyde logP 1.82 ALOGPS logS -3.4 ALOGPS Water Solubility 1.19e-01 g/l ALOGPS logP 1.49 ChemAxon IUPAC Name 2-bromoethyl 2-(4-amino-2-formylphenyl)acetate ChemAxon Traditional IUPAC Name 2-bromoethyl 2-(4-amino-2-formylphenyl)acetate ChemAxon Molecular Weight 286.122 ChemAxon Monoisotopic Weight 285.000055902 ChemAxon SMILES NC1=CC(C=O)=C(CC(=O)OCCBr)C=C1 ChemAxon Molecular Formula C11H12BrNO3 ChemAxon InChI InChI=1S/C11H12BrNO3/c12-3-4-16-11(15)6-8-1-2-10(13)5-9(8)7-14/h1-2,5,7H,3-4,6,13H2 ChemAxon InChIKey InChIKey=SMKXVWWBCFWRMP-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 69.39 ChemAxon Refractivity 65.75 ChemAxon Polarizability 24.82 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 3.14 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 4634717 PubChem Substance 99444426 ChemSpider 3824992 PDB IBR BE0003758 Chymotrypsin-like elastase family member 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Chymotrypsin-like elastase family member 1 Involved in calcium ion binding Acts upon elastin CELA1 12q13 Secreted None 8.38 27798.0 Human HUGO Gene Nomenclature Committee (HGNC) GNC:3308 GeneCards CELA1 GenBank Gene Database AF120493 GenBank Protein Database 4731318 UniProtKB Q9UNI1 UniProt Accession CELA1_HUMAN Elastase-1 >Chymotrypsin-like elastase family member 1 MLVLYGHSTQDLPETNARVVGGTEAGRNSWPSQISLQYRSGGSRYHTCGGTLIRQNWVMT AAHCVDYQKTFRVVAGDHNLSQNDGTEQYVSVQKIVVHPYWNSDNVAAGYDIALLRLAQS VTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGQLAQTLQQAYLPSVDYAICSSSS YWGSTVKNTMVCAGGDGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFVSSRGCNVSRKPTV FTQVSAYISWINNVIASN >777 bp ATGCTGGTCCTTTATGGACACAGCACCCAGGACCTTCCGGAAACCAATGCCCGCGTAGTC GGAGGGACTGAGGCCGGGAGGAATTCCTGGCCCTCTCAGATTTCCCTCCAGTACCGGTCT GGAGGTTCCCGGTATCACACCTGTGGAGGGACCCTTATCAGACAGAACTGGGTGATGACA GCTGCTCACTGCGTGGATTACCAGAAGACTTTCCGCGTGGTGGCTGGAGACCATAACCTG AGCCAGAATGATGGCACTGAGCAGTACGTGAGTGTGCAGAAGATCGTGGTGCATCCATAC TGGAACAGCGATAACGTGGCTGCCGGCTATGACATCGCCCTGCTGCGCCTGGCCCAGAGC GTTACCCTCAATAGCTATGTCCAGCTGGGTGTTCTGCCCCAGGAGGGAGCCATCCTGGCT AACAACAGTCCCTGCTACATCACAGGCTGGGGCAAGACCAAGACCAATGGGCAGCTGGCC CAGACCCTGCAGCAGGCTTACCTGCCCTCTGTGGACTATGCCATCTGCTCCAGCTCCTCC TACTGGGGCTCCACTGTGAAGAACACCATGGTGTGTGCTGGTGGAGATGGAGTTCGCTCT GGATGCCAGGGTGACTCTGGGGGCCCCCTCCATTGCTTGGTGAATGGCAAGTATTCTCTC CATGGAGTGACCAGCTTTGTGTCCAGCCGGGGCTGTAATGTCTCCAGGAAGCCTACAGTC TTCACCCAGGTCTCTGCTTACATCTCCTGGATAAATAATGTCATCGCCTCCAACTGA PF00089 Trypsin function hydrolase activity function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity process metabolism process macromolecule metabolism process protein metabolism process cellular protein metabolism process proteolysis process physiological process "
drug:(2-BROMOETHYL)(2-'FORMYL-4'-AMINOPHENYL) ACETATErdfs:label"(2-BROMOETHYL)(2-'FORMYL-4'-AMINOPHENYL) ACETATE"
drug:(2-BROMOETHYL)(2-'FORMYL-4'-AMINOPHENYL) ACETATErdf:typedrugbank:drugs
drug:(2-CARBAMOYLMETHYL-5-PROPYL-OCTAHYDRO-INDOL-7-YL)ACETIC ACIDdrugbank:description" experimental This compound belongs to the indolyl carboxylic acids and derivatives. These are compounds containing a carboxylic acid chain (of at least 2 carbon atoms) linked to an indole ring. Indolyl Carboxylic Acids and Derivatives Organic Compounds Heterocyclic Compounds Indoles and Derivatives Indolyl Carboxylic Acids and Derivatives Indoles Substituted Pyrroles Benzene and Substituted Derivatives Primary Carboxylic Acid Amides Enolates Carboxylic Acids Polyamines indole benzene substituted pyrrole pyrrole primary carboxylic acid amide carboxamide group carboxylic acid derivative enolate polyamine carboxylic acid amine organonitrogen compound logP 1.77 ALOGPS logS -3.7 ALOGPS Water Solubility 5.02e-02 g/l ALOGPS logP 1.86 ChemAxon IUPAC Name 2-[2-(carbamoylmethyl)-5-propyl-1H-indol-7-yl]acetic acid ChemAxon Traditional IUPAC Name [2-(carbamoylmethyl)-5-propyl-1H-indol-7-yl]acetic acid ChemAxon Molecular Weight 274.315 ChemAxon Monoisotopic Weight 274.131742452 ChemAxon SMILES CCCC1=CC2=C(NC(CC(N)=O)=C2)C(CC(O)=O)=C1 ChemAxon Molecular Formula C15H18N2O3 ChemAxon InChI InChI=1S/C15H18N2O3/c1-2-3-9-4-10-6-12(8-13(16)18)17-15(10)11(5-9)7-14(19)20/h4-6,17H,2-3,7-8H2,1H3,(H2,16,18)(H,19,20) ChemAxon InChIKey InChIKey=OMLOGGCSARAIGZ-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 96.18 ChemAxon Refractivity 75.7 ChemAxon Polarizability 29.83 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 4.6 ChemAxon pKa (strongest basic) -3.2 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 447739 PubChem Substance 99444429 ChemSpider 394751 PDB IDA BE0003768 Group IIE secretory phospholipase A2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Group IIE secretory phospholipase A2 Involved in calcium ion binding PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids PLA2G2E 1p36.13 Secreted None 8.28 15988.5 Human HUGO Gene Nomenclature Committee (HGNC) GNC:13414 GeneCards PLA2G2E GenBank Gene Database AF189279 GenBank Protein Database 7108923 UniProtKB Q9NZK7 UniProt Accession PA2GE_HUMAN GIIE sPLA2 Phosphatidylcholine 2-acylhydrolase GIIE sPLA(2)-IIE >Group IIE secretory phospholipase A2 MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL GTYNRKYAHYPNKLCTGPTPPC PF00068 Phospholip_A2_1 function calcium ion binding function hydrolase activity, acting on ester bonds function binding function carboxylic ester hydrolase activity function lipase activity function catalytic activity function phospholipase activity function phospholipase A2 activity function hydrolase activity function ion binding function cation binding process lipid metabolism process physiological process process metabolism process lipid catabolism process primary metabolism "
drug:(2-CARBAMOYLMETHYL-5-PROPYL-OCTAHYDRO-INDOL-7-YL)ACETIC ACIDrdfs:label"(2-CARBAMOYLMETHYL-5-PROPYL-OCTAHYDRO-INDOL-7-YL)ACETIC ACID"
drug:(2-CARBAMOYLMETHYL-5-PROPYL-OCTAHYDRO-INDOL-7-YL)ACETIC ACIDrdf:typedrugbank:drugs
drug:(2-Sulfanyl-3-Phenylpropanoyl)-Phe-Tyrdrugbank:description" experimental This compound belongs to the peptides. These are compounds containing an amide derived from two or more amino carboxylic acid molecules (the same or different) by formation of a covalent bond from the carbonyl carbon of one to the nitrogen atom of another. Peptides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues N-acyl-alpha Amino Acids Alpha Amino Acid Amides Phenylpropanoic Acids Amphetamines and Derivatives Phenylpropylamines Phenols and Derivatives Amino Fatty Acids Secondary Carboxylic Acid Amides Enols Enolates Carboxylic Acids Polyamines Alkylthiols n-acyl-alpha-amino acid n-acyl-alpha amino acid or derivative alpha-amino acid amide 3-phenylpropanoic-acid amphetamine or derivative alpha-amino acid or derivative phenylpropylamine phenol derivative benzene carboxamide group secondary carboxylic acid amide polyamine alkylthiol enol enolate carboxylic acid organonitrogen compound amine logP 3.62 ALOGPS logS -5.6 ALOGPS Water Solubility 1.35e-03 g/l ALOGPS logP 4.16 ChemAxon IUPAC Name (2R)-3-(4-hydroxyphenyl)-2-[(2R)-3-phenyl-2-[(2S)-3-phenyl-2-sulfanylpropanamido]propanamido]propanoic acid ChemAxon Traditional IUPAC Name (2R)-3-(4-hydroxyphenyl)-2-[(2R)-3-phenyl-2-[(2S)-3-phenyl-2-sulfanylpropanamido]propanamido]propanoic acid ChemAxon Molecular Weight 492.587 ChemAxon Monoisotopic Weight 492.171892706 ChemAxon SMILES OC(=O)[C@@H](CC1=CC=C(O)C=C1)NC(=O)[C@@H](CC1=CC=CC=C1)NC(=O)[C@@H](S)CC1=CC=CC=C1 ChemAxon Molecular Formula C27H28N2O5S ChemAxon InChI InChI=1S/C27H28N2O5S/c30-21-13-11-20(12-14-21)16-23(27(33)34)29-25(31)22(15-18-7-3-1-4-8-18)28-26(32)24(35)17-19-9-5-2-6-10-19/h1-14,22-24,30,35H,15-17H2,(H,28,32)(H,29,31)(H,33,34)/t22-,23-,24+/m1/s1 ChemAxon InChIKey InChIKey=GIVBBFGMRNXKPE-SMIHKQSGSA-N ChemAxon Polar Surface Area (PSA) 115.73 ChemAxon Refractivity 135.4 ChemAxon Polarizability 50.69 ChemAxon Rotatable Bond Count 11 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 3.74 ChemAxon pKa (strongest basic) -4.1 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 46936840 PubChem Substance 46505869 PDB TI2 BE0001346 Thermolysin Geobacillus stearothermophilus # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Thermolysin Amino acid transport and metabolism Extracellular zinc metalloprotease nprS Secreted protein None 6.15 60617.0 Geobacillus stearothermophilus GenBank Gene Database M34237 GenBank Protein Database 143254 UniProtKB P43133 UniProt Accession THER_GEOSE Bacillolysin precursor EC 3.4.24.28 Neutral protease >Bacillolysin precursor MKRKMKMKLVRFGLAAGLAAQVFFLPYNALASTEHVTWNQQFQTPQFISGDLLKVNGTSP EELVYQYVEKNENKFKFHENAKDTLQLKEKKNDNLGFTFMRFQQTYKGIPVFGAVVTAHV KDGTLTALSGTLIPNLDTKGSLKSGKKLSEKQARDIAEKDLVANVTKEVPEYEQGKDTEF VVYVNGDEASLAYVVNLNFLTPEPGNWLYIIDAVDGKILNKFNQLDAAKPGDVKSITGTS TVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFAS YDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDG DGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPD WEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLIS QGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVAS VKQAFDAVGVK >1656 bp ATGAAAAGGAAAATGAAAATGAAATTAGTACGTTTTGGTCTTGCAGCAGGACTAGCGGCC CAAGTATTTTTTTTACCTTACAATGCGCTGGCTTCAACGGAACACGTTACATGGAACCAA CAATTTCAAACCCCTCAATTCATCTCCGGTGATCTGCTGAAAGTGAATGGCACATCCCCA GAAGAACTCGTCTATCAATATGTTGAAAAAAACGAAAACAAGTTTAAATTTCATGAAAAC GCTAAGGATACTCTACAATTGAAAGAAAAGAAAAATGATAACCTTGGTTTTACGTTTATG CGCTTCCAACAAACGTATAAAGGGATTCCTGTGTTTGGAGCAGTAGTAACTGCGCACGTG AAAGATGGCACGCTGACGGCGCTATCAGGGACACTGATTCCGAATTTGGACACGAAAGGA TCCTTAAAAAGCGGGAAGAAATTGAGTGAGAAACAAGCGCGTGACATTGCTGAAAAAGAT TTAGTGGCAAATGTAACAAAGGAAGTACCGGAATATGAACAGGGAAAAGACACCGAGTTT GTTGTTTATGTCAATGGGGACGAGGCTTCTTTAGCGTACGTTGTCAATTTAAACTTTTTA ACTCCTGAACCAGGAAACTGGCTGTATATCATTGATGCCGTAGACGGAAAAATTTTAAAT AAATTTAACCAACTTGACGCCGCAAAACCAGGTGATGTGAAGTCGATAACAGGAACATCA ACTGTCGGAGTGGGAAGAGGAGTACTTGGTGATCAAAAAAATATTAATACAACCTACTCT ACGTACTACTATTTACAAGATAATACGCGTGGAAATGGGATTTTCACGTATGATGCGAAA TACCGTACGACATTGCCGGGAAGCTTATGGGCAGATGCAGATAACCAATTTTTTGCGAGC TATGATGCTCCAGCGGTTGATGCTCATTATTACGCTGGTGTGACATATGACTACTATAAA AATGTTCATAACCGTCTCAGTTACGACGGAAATAATGCAGCTATTAGATCATCCGTTCAT TATAGCCAAGGCTATAATAACGCATTTTGGAACGGTTCGCAAATGGTGTATGGCGATGGT GATGGTCAAACATTTATTCCACTTTCTGGTGGTATTGATGTGGTCGCACATGAGTTAACG CATGCGGTAACCGATTATACAGCCGGACTCATTTATCAAAACGAATCTGGTGCAATTAAT GAGGCAATATCTGATATTTTTGGAACGTTAGTCGAATTTTACGCTAACAAAAATCCAGAT TGGGAAATTGGAGAGGATGTGTATACACCTGGTATTTCAGGGGATTCGCTCCGTTCGATG TCCGATCCGGCAAAGTATGGTGATCCAGATCACTATTCAAAGCGCTATACAGGCACGCAA GATAATGGCGGGGTTCATATCAATAGCGGAATTATCAACAAAGCCGCTTATTTGATTAGC CAAGGCGGTACGCATTACGGTGTGAGTGTTGTCGGAATCGGACGCGATAAATTGGGGAAA ATTTTCTATCGTGCATTAACGCAATATTTAACACCAACGTCCAACTTTAGCCAACTTCGT GCTGCCGCTGTTCAATCAGCCACTGACTTGTACGGTTCGACAAGCCAGGAAGTCGCTTCT GTGAAGCAGGCCTTTGATGCGGTAGGGGTGAAATAA PF07504 FTP PF03413 PepSY PF01447 Peptidase_M4 PF02868 Peptidase_M4_C component extracellular region function metallopeptidase activity function ion binding function metalloendopeptidase activity function cation binding function transition metal ion binding function zinc ion binding function binding function peptidase activity function catalytic activity function endopeptidase activity function hydrolase activity process macromolecule metabolism process protein metabolism process cellular protein metabolism process physiological process process metabolism process proteolysis "
drug:(2-Sulfanyl-3-Phenylpropanoyl)-Phe-Tyrrdfs:label"(2-Sulfanyl-3-Phenylpropanoyl)-Phe-Tyr"
drug:(2-Sulfanyl-3-Phenylpropanoyl)-Phe-Tyrowl:sameAsdrug:EXPT03061
drug:(2-Sulfanyl-3-Phenylpropanoyl)-Phe-Tyrrdf:typedrugbank:drugs
drug:(2-[2-Ketopropylthio]Ethanesulfonatedrugbank:description" experimental This compound belongs to the sulfonic acids. These are compounds containing the sulfonic acid group, which has the general structure RS(=O)2OH (R ≠ H). Sulfonic Acids Organic Compounds Organic Acids and Derivatives Sulfonic Acids and Derivatives Sulfonic Acids Organic Sulfites Sulfonyls Ketones Polyamines Thioethers Enolates ketone thioether enolate polyamine carbonyl group logP -1.4 ALOGPS logS -0.92 ALOGPS Water Solubility 2.39e+01 g/l ALOGPS logP -0.52 ChemAxon IUPAC Name 2-[(2-oxopropyl)sulfanyl]ethane-1-sulfonic acid ChemAxon Traditional IUPAC Name 2-oxopropyl-CoM ChemAxon Molecular Weight 198.26 ChemAxon Monoisotopic Weight 198.002050188 ChemAxon SMILES CC(=O)CSCCS(O)(=O)=O ChemAxon Molecular Formula C5H10O4S2 ChemAxon InChI InChI=1S/C5H10O4S2/c1-5(6)4-10-2-3-11(7,8)9/h2-4H2,1H3,(H,7,8,9) ChemAxon InChIKey InChIKey=CRNXHFXAXBWIRH-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 71.44 ChemAxon Refractivity 43.56 ChemAxon Polarizability 18.73 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) -1 ChemAxon pKa (strongest basic) -7.5 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 443231 PubChem Substance 46505444 PDB KPC BE0001784 2-oxopropyl-CoM reductase, carboxylating Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown 2-oxopropyl-CoM reductase, carboxylating Energy production and conversion Catalyzes the reductive cleavage of the thioether linkage of 2-ketopropyl-coenzyme M, and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M xecC None 5.9 57348.0 Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) GenBank Gene Database X79863 GenBank Protein Database 929914 UniProtKB Q56839 UniProt Accession XECC_XANP2 2-KPCC Aliphatic epoxide carboxylation component II EC 1.8.1.5 NADPH:2- ketopropyl-CoM carboxylase/oxidoreductase >2-oxopropyl-CoM reductase, carboxylating MKVWNARNDHLTINQWATRIDEILEAPDGGEVIYNVDENDPREYDAIFIGGGAAGRFGSA YLRAMGGRQLIVDRWPFLGGSCPHNACVPHHLFSDCAAELMLARTFSGQYWFPDMTEKVV GIKEVVDLFRAGRNGPHGIMNFQSKEQLNLEYILNCPAKVIDNHTVEAAGKVFKAKNLIL AVGAGPGTLDVPGVNAKGVFDHATLVEELDYEPGSTVVVVGGSKTAVEYGCFFNATGRRT VMLVRTEPLKLIKDNETRAYVLDRMKEQGMEIISGSNVTRIEEDANGRVQAVVAMTPNGE MRIETDFVFLGLGEQPRSAELAKILGLDLGPKGEVLVNEYLQTSVPNVYAVGDLIGGPME MFKARKSGCYAARNVMGEKISYTPKNYPDFLHTHYEVSFLGMGEEEARAAGHEIVTIKMP PDTENGLNVALPASDRTMLYAFGKGTAHMSGFQKIVIDAKTRKVLGAHHVGYGAKDAFQY LNVLIKQGLTVDELGDMDELFLNPTHFIQLSRLRAGSKNLVSL >1572 bp GTGAAAGTCTGGAACGCCCGAAACGACCATCTCACCATCAATCAATGGGCCACGCGGATC GATGAGATCCTCGAGGCGCCCGATGGCGGAGAGGTCATCTACAACGTGGACGAGAACGAT CCACGCGAATACGACGCCATCTTCATCGGCGGCGGCGCCGCCGGGCGCTTCGGCTCGGCC TATCTGCGCGCCATGGGCGGCCGGCAGCTCATCGTCGACCGCTGGCCGTTCCTGGGCGGC TCGTGCCCGCACAATGCGTGCGTGCCGCACCATCTGTTCTCCGACTGCGCGGCCGAGCTG ATGCTCGCGCGCACCTTCTCGGGCCAGTACTGGTTCCCGGACATGACCGAGAAGGTGGTC GGCATCAAGGAGGTGGTCGATCTGTTCCGCGCCGGGCGCAACGGCCCGCACGGCATCATG AACTTCCAGTCCAAGGAACAGCTCAACCTCGAATACATCCTCAACTGCCCGGCCAAGGTG ATCGATAATCACACCGTCGAGGCGGCCGGCAAGGTGTTCAAGGCCAAGAACCTGATCCTC GCGGTGGGCGCGGGGCCGGGCACGCTCGACGTGCCGGGCGTCAACGCCAAGGGCGTCTTC GACCACGCGACGCTGGTGGAGGAGCTCGACTACGAGCCCGGCAGCACCGTGGTCGTGGTG GGCGGCTCGAAGACCGCGGTCGAATATGGCTGCTTCTTCAACGCCACCGGCCGGCGCACC GTGATGCTGGTGCGCACCGAGCCGCTCAAGCTCATCAAGGACAACGAGACCCGCGCCTAC GTGCTCGACCGCATGAAGGAGCAGGGCATGGAGATCATCTCCGGCTCCAACGTCACGCGC ATCGAGGAGGACGCCAACGGCCGCGTTCAGGCGGTGGTGGCCATGACGCCCAACGGCGAG ATGCGCATCGAGACCGACTTCGTCTTCCTCGGCCTCGGCGAGCAGCCCCGCTCGGCGGAG CTGGCGAAGATCCTGGGCCTCGATCTCGGCCCCAAGGGCGAGGTGCTGGTCAACGAATAT CTTCAGACCAGCGTGCCCAACGTCTACGCGGTGGGCGACCTCATCGGCGGGCCCATGGAG ATGTTCAAGGCCCGCAAGTCCGGCTGCTATGCCGCGCGCAACGTCATGGGCGAGAAGATC TCCTACACGCCCAAGAATTATCCCGACTTCCTGCACACCCATTACGAGGTCAGCTTCCTC GGCATGGGCGAGGAGGAAGCCCGCGCGGCGGGGCACGAGATCGTCACCATCAAGATGCCG CCGGACACGGAGAACGGCCTCAACGTGGCGCTGCCGGCCTCCGACCGCACCATGCTCTAC GCCTTCGGCAAGGGCACGGCCCACATGTCGGGCTTCCAGAAGATCGTCATCGACGCCAAG ACCCGCAAGGTGCTCGGCGCCCATCACGTGGGCTATGGCGCGAAGGACGCGTTCCAATAC CTGAACGTGCTCATCAAGCAGGGGCTCACCGTCGACGAACTGGGGGACATGGACGAATTG TTCCTCAATCCGACCCACTTCATCCAGCTCTCGCGCCTGCGCGCGGGCTCGAAGAATCTG GTGAGCCTGTGA PF00070 Pyr_redox PF07992 Pyr_redox_2 PF02852 Pyr_redox_dim component cell component intracellular component cytoplasm function disulfide oxidoreductase activity function catalytic activity function oxidoreductase activity process electron transport process physiological process process metabolism process cellular metabolism process generation of precursor metabolites and energy "
drug:(2-[2-Ketopropylthio]Ethanesulfonaterdfs:label"(2-[2-Ketopropylthio]Ethanesulfonate"
drug:(2-[2-Ketopropylthio]Ethanesulfonateowl:sameAsdrug:EXPT01980
drug:(2-[2-Ketopropylthio]Ethanesulfonaterdf:typedrugbank:drugs
drug:(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC ACIDdrugbank:description" experimental This compound belongs to the phenoxyacetic acid derivatives. These are compounds containing an anisole where the methane group is linked to an acetic acid or a derivative. Phenoxyacetic Acid Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenoxyacetic Acid Derivatives Salicylamides Benzamides Phenol Ethers Benzoyl Derivatives Chlorobenzenes Fluorobenzenes Alkyl Aryl Ethers Bromobenzenes Aryl Chlorides Aryl Bromides Aryl Fluorides Secondary Carboxylic Acid Amides Carboxylic Acids Polyamines Enolates Organofluorides Organobromides Organochlorides benzamide benzoyl phenol ether alkyl aryl ether bromobenzene chlorobenzene fluorobenzene aryl chloride aryl bromide aryl halide aryl fluoride carboxamide group secondary carboxylic acid amide ether carboxylic acid polyamine carboxylic acid derivative enolate organofluoride amine organohalogen organobromide organochloride organonitrogen compound logP 3.77 ALOGPS logS -5.1 ALOGPS Water Solubility 3.55e-03 g/l ALOGPS logP 3.61 ChemAxon IUPAC Name 2-(2-{[(4-bromo-2-fluorophenyl)methyl]carbamoyl}-5-chlorophenoxy)acetic acid ChemAxon Traditional IUPAC Name 2-{[(4-bromo-2-fluorophenyl)methyl]carbamoyl}-5-chlorophenoxyacetic acid ChemAxon Molecular Weight 416.626 ChemAxon Monoisotopic Weight 414.962226436 ChemAxon SMILES OC(=O)COC1=CC(Cl)=CC=C1C(=O)NCC1=C(F)C=C(Br)C=C1 ChemAxon Molecular Formula C16H12BrClFNO4 ChemAxon InChI InChI=1S/C16H12BrClFNO4/c17-10-2-1-9(13(19)5-10)7-20-16(23)12-4-3-11(18)6-14(12)24-8-15(21)22/h1-6H,7-8H2,(H,20,23)(H,21,22) ChemAxon InChIKey InChIKey=ZLIGBZRXAQNUFO-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 75.63 ChemAxon Refractivity 89.84 ChemAxon Polarizability 35.58 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 2.97 ChemAxon pKa (strongest basic) -1.4 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 16058629 PubChem Substance 99443499 ChemSpider 17218348 PDB 388 BE0000747 Aldose reductase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aldose reductase Involved in oxidoreductase activity Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies AKR1B1 7q35 Cytoplasm None 6.99 35723.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:381 GenAtlas AKR1B1 GeneCards AKR1B1 GenBank Gene Database J04795 GenBank Protein Database 178487 UniProtKB P15121 UniProt Accession ALDR_HUMAN Aldehyde reductase AR EC 1.1.1.21 >Aldose reductase ASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQE KLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKE FFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPA VNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKH NKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCAL LSCTSHKDYPFHEEF >951 bp ATGGCAAGCCGTCTCCTGCTCAACAACGGCGCCAAGATGCCCATCCTGGGGTTGGGTACC TGGAAGTCCCCTCCAGGGCAGGTGACTGAGGCCGTGAAGGTGGCCATTGACGTCGGGTAC CGCCACATCGACTGTGCCCATGTGTACCAGAATGAGAATGAGGTGGGGGTGGCCATTCAG GAGAAGCTCAGGGAGCAGGTGGTGAAGCGTGAGGAGCTCTTCATCGTCAGCAAGCTGTGG TGCACGTACCATGAGAAGGGCCTGGTGAAAGGAGCCTGCCAGAAGACACTCAGCGACCTG AAGCTGGACTACCTGGACCTCTACCTTATTCACTGGCCGACTGGCTTTAAGCCTGGGAAG GAATTTTTCCCATTGGATGAGTCGGGCAATGTGGTTCCCAGTGACACCAACATTCTGGAC ACGTGGGCGGCCATGGAAGAGCTGGTGGATGAAGGGCTGGTGAAAGCTATTGGCATCTCC AACTTCAACCATCTCCAGGTGGAGATGATCTTAAACAAACCTGGCTTGAAGTATAAGCCT GCAGTTAACCAGATTGAGTGCCACCCATATCTCACTCAGGAGAAGTTAATCCAGTACTGC CAGTCCAAAGGCATCGTGGTGACCGCCTACAGCCCCCTCGGCTCTCCTGACAGGCCCTGG GCCAAGCCCGAGGACCCTTCTCTCCTGGAGGATCCCAGGATCAAGGCGATCGCAGCCAAG CACAATAAAACTACAGCCCAGGTCCTGATCCGGTTCCCCATGCAGAGGAACTTGGTGGTG ATCCCCAAGTCTGTGACACCAGAACGCATTGCTGAGAACTTTAAGGTCTTTGACTTTGAA CTGAGCAGCCAGGATATGACCACCTTACTCAGCTACAACAGGAACTGGAGGGTCTGTGCC TTGTTGAGCTGTACCTCCCACAAGGATTACCCCTTCCATGAAGAGTTTTGA PF00248 Aldo_ket_red function oxidoreductase activity function catalytic activity "
drug:(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC ACIDrdfs:label"(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC ACID"
drug:(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC ACIDrdf:typedrugbank:drugs
drug:(20S)-19,20,21,22-TETRAHYDRO-19-OXO-5H-18,20-ETHANO-12,14-ETHENO-6,10-METHENO-18H-BENZ[D]IMIDAZO[4,3-K][1,6,9,12]OXATRIAZA-CYCLOOCTADECOSINE-9-CARBONITRILEdrugbank:description" experimental This compound belongs to the diarylethers. These are organic compounds containing the dialkyl ether functional group, with the formula ROR', where R and R' are aryl groups. Diarylethers Organic Compounds Organooxygen Compounds Ethers Diarylethers Naphthalenes Benzonitriles Pyrrolidones N-substituted Imidazoles Tertiary Carboxylic Acid Amides Lactams Tertiary Amines Dialkylamines Polyamines Carboxylic Acids Nitriles benzonitrile pyrrolidone benzene n-substituted imidazole tertiary carboxylic acid amide azole imidazole pyrrolidine carboxamide group lactam tertiary amine polyamine secondary aliphatic amine carbonitrile nitrile carboxylic acid derivative secondary amine carboxylic acid amine organonitrogen compound logP 2.51 ALOGPS logS -3.6 ALOGPS Water Solubility 1.00e-01 g/l ALOGPS logP 2.53 ChemAxon IUPAC Name (5R)-30-oxo-19-oxa-2,6,10,12-tetraazahexacyclo[18.6.2.1^{2,5}.1^{14,18}.0^{8,12}.0^{23,27}]triaconta-1(27),8,10,14(29),15,17,20(28),21,23,25-decaene-17-carbonitrile ChemAxon Traditional IUPAC Name (5R)-30-oxo-19-oxa-2,6,10,12-tetraazahexacyclo[18.6.2.1^{2,5}.1^{14,18}.0^{8,12}.0^{23,27}]triaconta-1(27),8,10,14(29),15,17,20(28),21,23,25-decaene-17-carbonitrile ChemAxon Molecular Weight 435.4772 ChemAxon Monoisotopic Weight 435.169524941 ChemAxon SMILES [H][C@@]12CCN(C1=O)C1=C3C=C(OC4=C(C=CC(CN5C=NC=C5CN2)=C4)C#N)C=CC3=CC=C1 ChemAxon Molecular Formula C26H21N5O2 ChemAxon InChI InChI=1S/C26H21N5O2/c27-12-19-5-4-17-10-25(19)33-21-7-6-18-2-1-3-24(22(18)11-21)31-9-8-23(26(31)32)29-14-20-13-28-16-30(20)15-17/h1-7,10-11,13,16,23,29H,8-9,14-15H2/t23-/m1/s1 ChemAxon InChIKey InChIKey=USPFJPDEADLGIG-HSZRJFAPSA-N ChemAxon Polar Surface Area (PSA) 83.18 ChemAxon Refractivity 124.12 ChemAxon Polarizability 44.76 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 17.65 ChemAxon pKa (strongest basic) 6.68 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 6 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PDB U49 BE0002373 Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Involved in protein prenyltransferase activity Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate FNTA 8p11 None 4.72 44409.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3782 GenAtlas FNTA GeneCards FNTA GenBank Gene Database L10413 UniProtKB P49354 UniProt Accession FNTA_HUMAN CAAX farnesyltransferase alpha subunit EC 2.5.1.58 EC 2.5.1.59 FTase-alpha GGTase-I-alpha Ras proteins prenyltransferase alpha Type I protein geranyl-geranyltransferase alpha subunit >Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDS PSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLT RDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLR DPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQR YFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLL DLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIG RSLQSKHSTENDSPTNVQQ >1140 bp ATGGCGGCCACCGAGGGGGTCGGGGAGGCTGCGCAAGGGGGCGAGCCCGGGCAGCCGGCG CAACCCCCGCCCCAGCCGCACCCACCGCCGCCCCAGCAGCAGCACAAGGAAGAGATGGCG GCCGAGGCTGGGGAAGCCGTGGCGTCCCCCATGGACGACGGGTTTGTGAGCCTGGACTCG CCCTCCTATGTCCTGTACAGGGACAGAGCAGAATGGGCTGATATAGATCCGGTGCCGCAG AATGATGGCCCCAATCCCGTGGTCCAGATCATTTATAGTGACAAATTTAGAGATGTTTAT GATTACTTCCGAGCTGTCCTGCAGCGTGATGAAAGAAGTGAACGAGCTTTTAAGCTAACC CGGGATGCTATTGAGTTAAATGCAGCCAATTATACAGTGTGGCATTTCCGGAGAGTTCTT TTGAAGTCACTTCAGAAGGATCTACATGAGGAAATGAACTACATCACTGCAATAATTGAG GAGCAGCCCAAAAACTATCAAGTTTGGCATCATAGGCGAGTATTAGTGGAATGGCTAAGA GATCCATCTCAGGAGCTTGAATTTATTGCTGATATTCTTAATCAGGATGCAAAGAATTAT CATGCCTGGCAGCATCGACAATGGGTTATTCAGGAATTTAAACTTTGGGATAATGAGCTG CAGTATGTGGACCAACTTCTGAAAGAGGATGTGAGAAATAACTCTGTCTGGAACCAAAGA TACTTCGTTATTTCTAACACCACTGGCTACAATGATCGTGCTGTATTGGAGAGAGAAGTC CAATACACTCTGGAAATGATTAAACTAGTACCACATAATGAAAGTGCATGGAACTATTTG AAAGGGATTTTGCAGGATCGTGGTCTTTCCAAATATCCTAATCTGTTAAATCAATTACTT GATTTACAACCAAGTCATAGTTCCCCCTACCTAATTGCCTTTCTTGTGGATATCTATGAA GACATGCTAGAAAATCAGTGTGACAATAAGGAAGACATTCTTAATAAAGCATTAGAGTTA TGTGAAATCCTAGCTAAAGAAAAGGACACTATAAGAAAGGAATATTGGAGATACATTGGA AGATCCCTTCAAAGCAAACACAGCACAGAAAATGACTCACCAACAAATGTACAGCAATAA PF01239 PPTA function protein prenyltransferase activity function catalytic activity function transferase activity function transferase activity, transferring alkyl or aryl (other than methyl) groups function prenyltransferase activity process physiological process process protein prenylation process metabolism process protein amino acid prenylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification process protein amino acid lipidation BE0002372 Protein farnesyltransferase subunit beta Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Protein farnesyltransferase subunit beta Involved in catalytic activity Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding FNTB 14q23-q24 None 5.67 48774.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3785 GenAtlas FNTB GeneCards FNTB GenBank Gene Database L00635 UniProtKB P49356 UniProt Accession FNTB_HUMAN CAAX farnesyltransferase subunit beta EC 2.5.1.58 FTase-beta RAS proteins prenyltransferase beta >Protein farnesyltransferase subunit beta MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFS SYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ IVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQY LYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIG GVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCY SFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDF YHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPV PGFEELKDETSAEPATD >1314 bp ATGGCTTCTCCGAGTTCTTTCACCTACTATTGCCCTCCATCTTCCTCCCCCGTCTGGTCA GAGCCGCTGTACAGTCTGAGGCCCGAGCACGCGCGAGAGCGGTTGCAGGACGACTCGGTG GAAACAGTCACGTCCATAGAACAGGCAAAAGTAGAAGAAAAGATCCAAGAGGTCTTCAGT TCTTACAAGTTCAACCACCTTGTACCAAGGCTTGTTTTGCAGAGGGAGAAGCACTTCCAT TATCTGAAAAGAGGCCTTCGACAACTGACAGATGCCTATGAGTGTCTGGATGCCAGCCGC CCATGGCTCTGCTATTGGATCCTGCACAGCTTGGAACTGCTAGATGAACCCATCCCCCAG ATAGTGGCTACAGATGTGTGTCAGTTCCTGGAGCTGTGTCAGAGCCCAGAAGGTGGCTTT GGAGGAGGACCCGGTCAGTATCCACACCTTGCACCCACATATGCAGCAGTCAATGCATTG TGCATCATTGGCACCGAGGAGGCCTATGACATCATTAACAGAGAGAAGCTTCTTCAGTAT TTGTACTCCCTGAAGCAACCTGACGGCTCCTTTCTCATGCATGTCGGAGGTGAGGTGGAT GTGAGAAGCGCATACTGTGCTGCCTCCGTAGCCTCGCTGACCAACATCATCACTCCAGAC CTCTTTGAGGGCACTGCTGAATGGATAGCAAGGTGTCAGAACTGGGAAGGTGGCATTGGC GGGGTACCAGGGATGGAAGCCCATGGTGGCTATACCTTCTGTGGCCTGGCCGCGCTGGTA ATCCTCAAGAGGGAACGTTCCTTGAACTTGAAGAGCTTATTACAATGGGTGACAAGCCGG CAGATGCGATTTGAAGGAGGATTTCAGGGCCGCTGCAACAAGCTGGTGGATGGCTGCTAC TCCTTCTGGCAGGCGGGGCTCCTGCCCCTGCTCCACCGCGCACTGCACGCCCAAGGTGAC CCTGCCCTTAGCATGAGCCACTGGATGTTCCATCAGCAGGCCCTGCAGGAGTACATCCTG ATGTGCTGCCAGTGCCCTGCGGGGGGGCTTCTGGATAAACCTGGCAAGTCGCGTGATTTC TACCACACCTGCTACTGCCTGAGCGGCCTGTCCATAGCCCAGCACTTCGGCAGCGGAGCC ATGTTGCATGATGTGGTCCTGGGTGTGCCCGAAAACGCTCTGCAGCCCACTCACCCAGTG TACAACATTGGACCAGACAAGGTGATCCAGGCCACTACATACTTTCTACAGAAGCCAGTC CCAGGTTTTGAGGAGCTTAAGGATGAGACATCGGCAGAGCCTGCAACCGACTAG PF00432 Prenyltrans function catalytic activity "
drug:(20S)-19,20,21,22-TETRAHYDRO-19-OXO-5H-18,20-ETHANO-12,14-ETHENO-6,10-METHENO-18H-BENZ[D]IMIDAZO[4,3-K][1,6,9,12]OXATRIAZA-CYCLOOCTADECOSINE-9-CARBONITRILErdfs:label"(20S)-19,20,21,22-TETRAHYDRO-19-OXO-5H-18,20-ETHANO-12,14-ETHENO-6,10-METHENO-18H-BENZ[D]IMIDAZO[4,3-K][1,6,9,12]OXATRIAZA-CYCLOOCTADECOSINE-9-CARBONITRILE"
drug:(20S)-19,20,21,22-TETRAHYDRO-19-OXO-5H-18,20-ETHANO-12,14-ETHENO-6,10-METHENO-18H-BENZ[D]IMIDAZO[4,3-K][1,6,9,12]OXATRIAZA-CYCLOOCTADECOSINE-9-CARBONITRILErdf:typedrugbank:drugs
drug:(20S)-19,20,22,23-TETRAHYDRO-19-OXO-5H,21H-18,20-ETHANO-12,14-ETHENO-6,10-METHENOBENZ[D]IMIDAZO[4,3-L][1,6,9,13]OXATRIAZACYCLONOADECOSINE-9-CARBONITRILEdrugbank:description" experimental This compound belongs to the naphthalenes. These are compounds containing a naphthalene moiety, which consists of two fused benzene rings. Naphthalenes Organic Compounds Benzenoids Acenes and Derivatives Naphthalenes Alkyl Aryl Ethers N-substituted Imidazoles Pyrrolidones Benzene and Substituted Derivatives Tertiary Carboxylic Acid Amides Tertiary Amines Lactams Nitriles Carboxylic Acids Polyamines Dialkylamines alkyl aryl ether pyrrolidone benzene n-substituted imidazole tertiary carboxylic acid amide azole imidazole pyrrolidine tertiary amine lactam carboxamide group carbonitrile polyamine secondary aliphatic amine carboxylic acid derivative nitrile secondary amine ether carboxylic acid amine organonitrogen compound logP 2.43 ALOGPS logS -3.6 ALOGPS Water Solubility 1.16e-01 g/l ALOGPS logP 1.68 ChemAxon IUPAC Name (5S,18R,19S)-31-oxo-20-oxa-2,6,11,13-tetraazahexacyclo[19.6.2.1^{2,5}.1^{15,19}.0^{9,13}.0^{24,28}]hentriaconta-1(28),9,11,15,21(29),22,24,26-octaene-18-carbonitrile ChemAxon Traditional IUPAC Name (5S,18R,19S)-31-oxo-20-oxa-2,6,11,13-tetraazahexacyclo[19.6.2.1^{2,5}.1^{15,19}.0^{9,13}.0^{24,28}]hentriaconta-1(28),9,11,15,21(29),22,24,26-octaene-18-carbonitrile ChemAxon Molecular Weight 453.5356 ChemAxon Monoisotopic Weight 453.216475133 ChemAxon SMILES [H][C@]12CCN(C1=O)C1=CC=CC3=CC=C(O[C@@]4([H])CC(CN5C=NC=C5CCN2)=CC[C@]4([H])C#N)C=C13 ChemAxon Molecular Formula C27H27N5O2 ChemAxon InChI InChI=1S/C27H27N5O2/c28-14-20-5-4-18-12-26(20)34-22-7-6-19-2-1-3-25(23(19)13-22)32-11-9-24(27(32)33)30-10-8-21-15-29-17-31(21)16-18/h1-4,6-7,13,15,17,20,24,26,30H,5,8-12,16H2/t20-,24+,26+/m1/s1 ChemAxon InChIKey InChIKey=GBEQWWUQNVMGMR-PSUQPPDWSA-N ChemAxon Polar Surface Area (PSA) 83.18 ChemAxon Refractivity 129.92 ChemAxon Polarizability 49.25 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 17.66 ChemAxon pKa (strongest basic) 7.61 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 6 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PDB U66 BE0002373 Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Involved in protein prenyltransferase activity Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate FNTA 8p11 None 4.72 44409.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3782 GenAtlas FNTA GeneCards FNTA GenBank Gene Database L10413 UniProtKB P49354 UniProt Accession FNTA_HUMAN CAAX farnesyltransferase alpha subunit EC 2.5.1.58 EC 2.5.1.59 FTase-alpha GGTase-I-alpha Ras proteins prenyltransferase alpha Type I protein geranyl-geranyltransferase alpha subunit >Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDS PSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLT RDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLR DPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQR YFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLL DLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIG RSLQSKHSTENDSPTNVQQ >1140 bp ATGGCGGCCACCGAGGGGGTCGGGGAGGCTGCGCAAGGGGGCGAGCCCGGGCAGCCGGCG CAACCCCCGCCCCAGCCGCACCCACCGCCGCCCCAGCAGCAGCACAAGGAAGAGATGGCG GCCGAGGCTGGGGAAGCCGTGGCGTCCCCCATGGACGACGGGTTTGTGAGCCTGGACTCG CCCTCCTATGTCCTGTACAGGGACAGAGCAGAATGGGCTGATATAGATCCGGTGCCGCAG AATGATGGCCCCAATCCCGTGGTCCAGATCATTTATAGTGACAAATTTAGAGATGTTTAT GATTACTTCCGAGCTGTCCTGCAGCGTGATGAAAGAAGTGAACGAGCTTTTAAGCTAACC CGGGATGCTATTGAGTTAAATGCAGCCAATTATACAGTGTGGCATTTCCGGAGAGTTCTT TTGAAGTCACTTCAGAAGGATCTACATGAGGAAATGAACTACATCACTGCAATAATTGAG GAGCAGCCCAAAAACTATCAAGTTTGGCATCATAGGCGAGTATTAGTGGAATGGCTAAGA GATCCATCTCAGGAGCTTGAATTTATTGCTGATATTCTTAATCAGGATGCAAAGAATTAT CATGCCTGGCAGCATCGACAATGGGTTATTCAGGAATTTAAACTTTGGGATAATGAGCTG CAGTATGTGGACCAACTTCTGAAAGAGGATGTGAGAAATAACTCTGTCTGGAACCAAAGA TACTTCGTTATTTCTAACACCACTGGCTACAATGATCGTGCTGTATTGGAGAGAGAAGTC CAATACACTCTGGAAATGATTAAACTAGTACCACATAATGAAAGTGCATGGAACTATTTG AAAGGGATTTTGCAGGATCGTGGTCTTTCCAAATATCCTAATCTGTTAAATCAATTACTT GATTTACAACCAAGTCATAGTTCCCCCTACCTAATTGCCTTTCTTGTGGATATCTATGAA GACATGCTAGAAAATCAGTGTGACAATAAGGAAGACATTCTTAATAAAGCATTAGAGTTA TGTGAAATCCTAGCTAAAGAAAAGGACACTATAAGAAAGGAATATTGGAGATACATTGGA AGATCCCTTCAAAGCAAACACAGCACAGAAAATGACTCACCAACAAATGTACAGCAATAA PF01239 PPTA function protein prenyltransferase activity function catalytic activity function transferase activity function transferase activity, transferring alkyl or aryl (other than methyl) groups function prenyltransferase activity process physiological process process protein prenylation process metabolism process protein amino acid prenylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification process protein amino acid lipidation BE0002372 Protein farnesyltransferase subunit beta Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Protein farnesyltransferase subunit beta Involved in catalytic activity Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding FNTB 14q23-q24 None 5.67 48774.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3785 GenAtlas FNTB GeneCards FNTB GenBank Gene Database L00635 UniProtKB P49356 UniProt Accession FNTB_HUMAN CAAX farnesyltransferase subunit beta EC 2.5.1.58 FTase-beta RAS proteins prenyltransferase beta >Protein farnesyltransferase subunit beta MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFS SYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ IVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQY LYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIG GVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCY SFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDF YHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPV PGFEELKDETSAEPATD >1314 bp ATGGCTTCTCCGAGTTCTTTCACCTACTATTGCCCTCCATCTTCCTCCCCCGTCTGGTCA GAGCCGCTGTACAGTCTGAGGCCCGAGCACGCGCGAGAGCGGTTGCAGGACGACTCGGTG GAAACAGTCACGTCCATAGAACAGGCAAAAGTAGAAGAAAAGATCCAAGAGGTCTTCAGT TCTTACAAGTTCAACCACCTTGTACCAAGGCTTGTTTTGCAGAGGGAGAAGCACTTCCAT TATCTGAAAAGAGGCCTTCGACAACTGACAGATGCCTATGAGTGTCTGGATGCCAGCCGC CCATGGCTCTGCTATTGGATCCTGCACAGCTTGGAACTGCTAGATGAACCCATCCCCCAG ATAGTGGCTACAGATGTGTGTCAGTTCCTGGAGCTGTGTCAGAGCCCAGAAGGTGGCTTT GGAGGAGGACCCGGTCAGTATCCACACCTTGCACCCACATATGCAGCAGTCAATGCATTG TGCATCATTGGCACCGAGGAGGCCTATGACATCATTAACAGAGAGAAGCTTCTTCAGTAT TTGTACTCCCTGAAGCAACCTGACGGCTCCTTTCTCATGCATGTCGGAGGTGAGGTGGAT GTGAGAAGCGCATACTGTGCTGCCTCCGTAGCCTCGCTGACCAACATCATCACTCCAGAC CTCTTTGAGGGCACTGCTGAATGGATAGCAAGGTGTCAGAACTGGGAAGGTGGCATTGGC GGGGTACCAGGGATGGAAGCCCATGGTGGCTATACCTTCTGTGGCCTGGCCGCGCTGGTA ATCCTCAAGAGGGAACGTTCCTTGAACTTGAAGAGCTTATTACAATGGGTGACAAGCCGG CAGATGCGATTTGAAGGAGGATTTCAGGGCCGCTGCAACAAGCTGGTGGATGGCTGCTAC TCCTTCTGGCAGGCGGGGCTCCTGCCCCTGCTCCACCGCGCACTGCACGCCCAAGGTGAC CCTGCCCTTAGCATGAGCCACTGGATGTTCCATCAGCAGGCCCTGCAGGAGTACATCCTG ATGTGCTGCCAGTGCCCTGCGGGGGGGCTTCTGGATAAACCTGGCAAGTCGCGTGATTTC TACCACACCTGCTACTGCCTGAGCGGCCTGTCCATAGCCCAGCACTTCGGCAGCGGAGCC ATGTTGCATGATGTGGTCCTGGGTGTGCCCGAAAACGCTCTGCAGCCCACTCACCCAGTG TACAACATTGGACCAGACAAGGTGATCCAGGCCACTACATACTTTCTACAGAAGCCAGTC CCAGGTTTTGAGGAGCTTAAGGATGAGACATCGGCAGAGCCTGCAACCGACTAG PF00432 Prenyltrans function catalytic activity "
drug:(20S)-19,20,22,23-TETRAHYDRO-19-OXO-5H,21H-18,20-ETHANO-12,14-ETHENO-6,10-METHENOBENZ[D]IMIDAZO[4,3-L][1,6,9,13]OXATRIAZACYCLONOADECOSINE-9-CARBONITRILErdfs:label"(20S)-19,20,22,23-TETRAHYDRO-19-OXO-5H,21H-18,20-ETHANO-12,14-ETHENO-6,10-METHENOBENZ[D]IMIDAZO[4,3-L][1,6,9,13]OXATRIAZACYCLONOADECOSINE-9-CARBONITRILE"
drug:(20S)-19,20,22,23-TETRAHYDRO-19-OXO-5H,21H-18,20-ETHANO-12,14-ETHENO-6,10-METHENOBENZ[D]IMIDAZO[4,3-L][1,6,9,13]OXATRIAZACYCLONOADECOSINE-9-CARBONITRILErdf:typedrugbank:drugs
drug:(21S)-1AZA-4,4-DIMETHYL-6,19-DIOXA-2,3,7,20-TETRAOXOBICYCLO[19.4.0] PENTACOSANEdrugbank:description" experimental This compound belongs to the macrolide lactams. These are cyclic polyketides containing both a cyclic amide and a cyclic ester group. Macrolide Lactams Organic Compounds Phenylpropanoids and Polyketides Macrolide Lactams Alpha Amino Acid Esters Macrolides and Analogues Macrolactams Piperidines Hydropyridines Tertiary Carboxylic Acid Amides Tertiary Amines Carboxylic Acid Esters Ketones Polyamines Carboxylic Acids hydropyridine piperidine tertiary carboxylic acid amide carboxamide group ketone tertiary amine carboxylic acid ester polyamine carboxylic acid derivative carboxylic acid organonitrogen compound amine carbonyl group logP 3.86 ALOGPS logS -5.4 ALOGPS Water Solubility 1.57e-03 g/l ALOGPS logP 5.14 ChemAxon IUPAC Name (24aS)-17,17-dimethyl-docosahydropyrido[2,1-c]1,9-dioxa-4-azacyclohenicosane-1,14,18,19-tetrone ChemAxon Traditional IUPAC Name (24aS)-17,17-dimethyl-hexadecahydro-3H-pyrido[2,1-c]1,9-dioxa-4-azacyclohenicosane-1,14,18,19-tetrone ChemAxon Molecular Weight 437.5696 ChemAxon Monoisotopic Weight 437.277737985 ChemAxon SMILES [H][C@@]12CCCCN1C(=O)C(=O)C(C)(C)COC(=O)CCCCCCCCCCCOC2=O ChemAxon Molecular Formula C24H39NO6 ChemAxon InChI InChI=1S/C24H39NO6/c1-24(2)18-31-20(26)15-10-8-6-4-3-5-7-9-13-17-30-23(29)19-14-11-12-16-25(19)22(28)21(24)27/h19H,3-18H2,1-2H3/t19-/m0/s1 ChemAxon InChIKey InChIKey=VUCSBBBCFXBFFY-IBGZPJMESA-N ChemAxon Polar Surface Area (PSA) 89.98 ChemAxon Refractivity 116.68 ChemAxon Polarizability 48.74 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest basic) -2.6 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Ghose Filter true ChemAxon PubChem Compound 445646 PubChem Substance 99444991 PDB SB1 BE0000695 Peptidyl-prolyl cis-trans isomerase FKBP1A Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Peptidyl-prolyl cis-trans isomerase FKBP1A Posttranslational modification, protein turnover, chaperones May play a role in modulation of ryanodine receptor isoform-1 (RYR-1), a component of the calcium release channel of skeletal muscle sarcoplasmic reticulum. There are four molecules of FKBP12 per skeletal muscle RYR. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides FKBP1A 20p13 Cytoplasm None 8.48 11820.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3711 GenAtlas FKBP1A GeneCards FKBP1A GenBank Gene Database M34539 GenBank Protein Database 182628 UniProtKB P62942 UniProt Accession FKB1A_HUMAN 12 kDa FKBP EC 5.2.1.8 FKBP-12 Immunophilin FKBP12 Peptidyl-prolyl cis-trans isomerase PPIase Rotamase >FK506-binding protein 1A GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWE EGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE >327 bp ATGGGAGTGCAGGTGGAAACCATCTCCCCAGGAGACGGGCGCACCTTCCCCAAGCGCGGC CAGACCTGCGTGGTGCACTACACCGGGATGCTTGAAGATGGAAAGAAATTTGATTCCTCC CGGGACAGAAACAAGCCCTTTAAGTTTATGCTAGGCAAGCAGGAGGTGATCCGAGGCTGG GAAGAAGGGGTTGCCCAGATGAGTGTGGGTCAGAGAGCCAAACTGACTATATCTCCAGAT TATGCCTATGGTGCCACTGGGCACCCAGGCATCATCCCACCACATGCCACTCTCGTCTTC GATGTGGAGCTTCTAAAACTGGAATGA PF00254 FKBP_C process protein folding process physiological process process metabolism process macromolecule metabolism process protein metabolism process cellular protein metabolism "
drug:(21S)-1AZA-4,4-DIMETHYL-6,19-DIOXA-2,3,7,20-TETRAOXOBICYCLO[19.4.0] PENTACOSANErdfs:label"(21S)-1AZA-4,4-DIMETHYL-6,19-DIOXA-2,3,7,20-TETRAOXOBICYCLO[19.4.0] PENTACOSANE"
drug:(21S)-1AZA-4,4-DIMETHYL-6,19-DIOXA-2,3,7,20-TETRAOXOBICYCLO[19.4.0] PENTACOSANErdf:typedrugbank:drugs
drug:(2E)-1-[(6-chloropyridin-3-yl)methyl]-N-nitroimidazolidin-2-iminedrugbank:description" experimental This compound belongs to the pyridines and derivatives. These are compounds containing a pyridine ring, which is a six-member aromatic heterocycle which consists of one nitrogen atom and five carbon atoms. Pyridines and Derivatives Organic Compounds Heterocyclic Compounds Pyridines and Derivatives Aryl Chlorides Imidazolidines Nitro Compounds Tertiary Amines Guanidines Polyamines Imines Organochlorides imidazolidine nitro compound tertiary amine guanidine polyamine organochloride organohalogen imine amine organonitrogen compound logP 0.65 ALOGPS logS -2.9 ALOGPS Water Solubility 3.46e-01 g/l ALOGPS logP 0.76 ChemAxon IUPAC Name 2-chloro-5-{[(2E)-2-(nitroimino)imidazolidin-1-yl]methyl}pyridine ChemAxon Traditional IUPAC Name imidacloprid ChemAxon Molecular Weight 255.661 ChemAxon Monoisotopic Weight 255.052302296 ChemAxon SMILES [O-][N+](=O)\N=C1/NCCN1CC1=CN=C(Cl)C=C1 ChemAxon Molecular Formula C9H10ClN5O2 ChemAxon InChI InChI=1S/C9H10ClN5O2/c10-8-2-1-7(5-12-8)6-14-4-3-11-9(14)13-15(16)17/h1-2,5H,3-4,6H2,(H,11,13) ChemAxon InChIKey InChIKey=YWTYJOPNNQFBPC-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 86.34 ChemAxon Refractivity 63.55 ChemAxon Polarizability 23.28 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 2.5 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 86418 PubChem Substance 99444451 ChemSpider 77934 PDB IM4 BE0003963 CHRNA7-FAM7A fusion protein Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown CHRNA7-FAM7A fusion protein Involved in extracellular ligand-gated ion channel acti CHRFAM7A 15q13.1 Membrane 144-164 172-192 205-225 240-254 380-400 6.55 46217.3 Human HUGO Gene Nomenclature Committee (HGNC) GNC:15781 GeneCards CHRFAM7A GenBank Gene Database AK292984 GenBank Protein Database 158259429 UniProtKB Q494W8 UniProt Accession CRFM7_HUMAN CHRNA7-DR1 D-10 >CHRNA7-FAM7A fusion protein MQKYCIYQHFQFQLLIQHLWIAANCDIADERFDATFHTNVLVNSSGHCQYLPPGIFKSSC YIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPGKRSERFY ECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLL SLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPDGGKMPKW TRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLASVEMSAVAPPPASNGNLLYIGFR GLDGVHCVPTPDSGVVCGRMACSPTHDEHLLHGGQPPEGDPDLAKILEEVRYIANRFRCQ DESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDFA >1239 bp ATGCAAAAATATTGCATCTACCAGCATTTTCAGTTCCAATTGCTAATCCAGCATTTGTGG ATAGCTGCAAACTGTGATATTGCTGATGAGCGCTTTGACGCCACATTCCACACTAACGTG TTGGTGAATTCTTCTGGGCATTGCCAGTACCTGCCTCCAGGCATATTCAAGAGTTCCTGC TACATCGATGTACGCTGGTTTCCCTTTGATGTGCAGCACTGCAAACTGAAGTTTGGGTCC TGGTCTTACGGAGGCTGGTCCTTGGATCTGCAGATGCAGGAGGCAGATATCAGTGGCTAT ATCCCCAATGGAGAATGGGACCTAGTGGGAATCCCCGGCAAGAGGAGTGAAAGGTTCTAT GAGTGCTGCAAAGAGCCCTACCCTGATGTCACCTTCACAGTGACCATGCGCCGCAGGACA CTCTACTATGGCCTCAACCTGCTGATCCCCTGTGTGCTCATCTCCGCCCTCGCCCTGCTG GTGTTCCTGCTTCCTGCAGATTCCGGGGAGAAGATTTCCCTGGGGATAACAGTCTTACTC TCTCTTACCGTCTTCATGCTGCTCGTGGCTGAGATCATGCCCGCAACATCCGATTCGGTA CCATTGATAGCCCAGTACTTCGCCAGCACCATGATCATCGTGGGCCTCTCGGTGGTGGTG ACGGTGATCGTGCTGCAGTACCACCACCACGACCCCGACGGGGGCAAGATGCCCAAGTGG ACCAGAGTCATCCTTCTGAACTGGTGCGCGTGGTTCCTGCGAATGAAGAGGCCCGGGGAG GACAAGGTGCGCCCGGCCTGCCAGCACAAGCAGCGGCGCTGCAGCCTGGCCAGTGTGGAG ATGAGCGCCGTGGCGCCGCCGCCCGCCAGCAACGGGAACCTGCTGTACATCGGCTTCCGC GGCCTGGACGGCGTGCACTGTGTCCCGACCCCCGACTCTGGGGTAGTGTGTGGCCGCATG GCCTGCTCCCCCACGCACGATGAGCACCTCCTGCACGGTGGGCAACCCCCCGAGGGGGAC CCGGACTTGGCCAAGATCCTGGAGGAGGTCCGCTACATTGCCAACCGCTTCCGCTGCCAG GACGAAAGCGAGGCGGTCTGCAGCGAGTGGAAGTTCGCCGCCTGTGTGGTGGACCGCCTG TGCCTCATGGCCTTCTCGGTCTTCACCATCATCTGCACCATCGGCATCCTGATGTCGGCT CCCAACTTCGTGGAGGCCGTGTCCAAAGACTTTGCGTAA PF02931 Neur_chan_LBD PF02932 Neur_chan_memb component cell component postsynaptic membrane component intrinsic to membrane component integral to membrane component membrane function receptor activity function transporter activity function ligand-gated ion channel activity function extracellular ligand-gated ion channel activity function neurotransmitter receptor activity function ion transporter activity function ion channel activity function signal transducer activity process cellular physiological process process transport process ion transport process physiological process "
drug:(2E)-1-[(6-chloropyridin-3-yl)methyl]-N-nitroimidazolidin-2-iminerdfs:label"(2E)-1-[(6-chloropyridin-3-yl)methyl]-N-nitroimidazolidin-2-imine"
drug:(2E)-1-[(6-chloropyridin-3-yl)methyl]-N-nitroimidazolidin-2-iminerdf:typedrugbank:drugs
drug:(2E)-1-[2-hydroxy-4-methoxy-5-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-onedrugbank:description" experimental This compound belongs to the chalcones and dihydrochalcones. These are organic compounds containing 1,3-Diphenylpropenone (benzylideneacetophenone), ArCH=CH(=O)Ar,or its derivatives formed by substitution. Chalcones and Dihydrochalcones Organic Compounds Phenylpropanoids and Polyketides Flavonoids Chalcones and Dihydrochalcones Hydroxycinnamic Acids and Derivatives Methoxyphenols and Derivatives Acetophenones Styrenes Benzoyl Derivatives Anisoles Alkyl Aryl Ethers Enones Acryloyl Compounds Polyols Enolates Polyamines Enols cinnamic acid or derivative hydroxycinnamic acid or derivative methoxyphenol acetophenone anisole styrene phenol ether benzoyl phenol derivative alkyl aryl ether benzene acryloyl-group enone polyol ketone ether enol polyamine enolate carbonyl group logP 4.49 ALOGPS logS -5 ALOGPS Water Solubility 3.22e-03 g/l ALOGPS logP 5.5 ChemAxon IUPAC Name (2E)-1-[2-hydroxy-4-methoxy-5-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-one ChemAxon Traditional IUPAC Name bavachalcone ChemAxon Molecular Weight 338.397 ChemAxon Monoisotopic Weight 338.151809192 ChemAxon SMILES COC1=CC(O)=C(C=C1CC=C(C)C)C(=O)\C=C\C1=CC=C(O)C=C1 ChemAxon Molecular Formula C21H22O4 ChemAxon InChI InChI=1S/C21H22O4/c1-14(2)4-8-16-12-18(20(24)13-21(16)25-3)19(23)11-7-15-5-9-17(22)10-6-15/h4-7,9-13,22,24H,8H2,1-3H3/b11-7+ ChemAxon InChIKey InChIKey=ZUGCRBMNFSAUOC-YRNVUSSQSA-N ChemAxon Polar Surface Area (PSA) 66.76 ChemAxon Refractivity 101.54 ChemAxon Polarizability 37.37 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 8.03 ChemAxon pKa (strongest basic) -4.9 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Ghose Filter true ChemAxon PubChem Compound 5321765 PubChem Substance 99443971 ChemSpider 4479431 PDB BVL BE0003768 Group IIE secretory phospholipase A2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Group IIE secretory phospholipase A2 Involved in calcium ion binding PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids PLA2G2E 1p36.13 Secreted None 8.28 15988.5 Human HUGO Gene Nomenclature Committee (HGNC) GNC:13414 GeneCards PLA2G2E GenBank Gene Database AF189279 GenBank Protein Database 7108923 UniProtKB Q9NZK7 UniProt Accession PA2GE_HUMAN GIIE sPLA2 Phosphatidylcholine 2-acylhydrolase GIIE sPLA(2)-IIE >Group IIE secretory phospholipase A2 MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL GTYNRKYAHYPNKLCTGPTPPC PF00068 Phospholip_A2_1 function lipase activity function catalytic activity function phospholipase activity function phospholipase A2 activity function hydrolase activity function ion binding function cation binding function calcium ion binding function hydrolase activity, acting on ester bonds function binding function carboxylic ester hydrolase activity process physiological process process metabolism process lipid catabolism process primary metabolism process lipid metabolism "
drug:(2E)-1-[2-hydroxy-4-methoxy-5-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-onerdfs:label"(2E)-1-[2-hydroxy-4-methoxy-5-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-one"
drug:(2E)-1-[2-hydroxy-4-methoxy-5-(3-methylbut-2-en-1-yl)phenyl]-3-(4-hydroxyphenyl)prop-2-en-1-onerdf:typedrugbank:drugs
drug:(2E)-2-({(2S)-2-CARBOXY-2-[(PHENOXYACETYL)AMINO]ETHOXY}IMINO)PENTANEDIOIC ACIDdrugbank:description" experimental This compound belongs to the n-acyl-alpha amino acids. These are compounds containing an alpha amino acid which bears an acyl group at his terminal nitrogen atom. N-acyl-alpha Amino Acids Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Tricarboxylic Acids and Derivatives Phenol Ethers Alkyl Aryl Ethers Oxime Ethers Secondary Carboxylic Acid Amides Polyols Polyamines Carboxylic Acids Enolates Imines tricarboxylic acid derivative phenol ether alkyl aryl ether benzene secondary carboxylic acid amide polyol carboxamide group oxime ether enolate polyamine carboxylic acid ether imine amine organonitrogen compound logP 0.1 ALOGPS logS -3.6 ALOGPS Water Solubility 9.79e-02 g/l ALOGPS logP 0.51 ChemAxon IUPAC Name (2E)-2-{[(2S)-2-carboxy-2-(2-phenoxyacetamido)ethoxy]imino}pentanedioic acid ChemAxon Traditional IUPAC Name (2E)-2-{[(2S)-2-carboxy-2-(2-phenoxyacetamido)ethoxy]imino}pentanedioic acid ChemAxon Molecular Weight 382.3221 ChemAxon Monoisotopic Weight 382.101230184 ChemAxon SMILES [H][C@@](CO\N=C(/CCC(O)=O)C(O)=O)(NC(=O)COC1=CC=CC=C1)C(O)=O ChemAxon Molecular Formula C16H18N2O9 ChemAxon InChI InChI=1S/C16H18N2O9/c19-13(9-26-10-4-2-1-3-5-10)17-12(16(24)25)8-27-18-11(15(22)23)6-7-14(20)21/h1-5,12H,6-9H2,(H,17,19)(H,20,21)(H,22,23)(H,24,25)/b18-11+/t12-/m0/s1 ChemAxon InChIKey InChIKey=LDNKNKRRFZRLIG-HWQJWEFDSA-N ChemAxon Polar Surface Area (PSA) 171.82 ChemAxon Refractivity 86.37 ChemAxon Polarizability 35.55 ChemAxon Rotatable Bond Count 12 ChemAxon H Bond Acceptor Count 10 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 2.83 ChemAxon pKa (strongest basic) -2.1 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 16741209 PubChem Substance 99444872 ChemSpider 20572517 PDB PL7 BE0004313 Penicillin-binding protein 1B Streptococcus pneumoniae # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Penicillin-binding protein 1B Cell wall/membrane/envelope biogenesis pbp1b None 8.82 89479.9 Streptococcus pneumoniae GeneCards pbp1b GenBank Gene Database AF101781 GenBank Protein Database 6165962 UniProtKB O70038 UniProt Accession O70038_STREE >Penicillin-binding protein 1b MQNQLNELKRKMLEFFQQKQKNKKSARPGKKGSSTKKSKTLDKSAIFPAILLSIKALFNL LFVLGFLGGMLGAGIALGYGVALFDKVRVPQTEELVNQVKDISSISEITYSDGTVIASIE SDLLRTSISSEQISENLKKAIIATEDEHFKEHKGVVPKAVIRATLGKFVGLGSSSGGSTL TQQLIKQQVVGDAPTLARKAAEIVDALALERAMNKDEILTTYLNVAPFGRNNKGQNIAGA RQAAEGIFGVDASQLTVPQAAFLAGLPQSPITYSPYENTGELKSDEDLEIGLRRAKAVLY SMYRTGALSKDEYSQYKDYDLKQDFLPSGTVTGISRDYLYFTTLAEAQERMYDYLAQRDN VSAKELKNEATQKFYRDLAAKEIENGGYKITTTIDQKIHSAMQSAVADYGYLLDDGTGRV EVGNVLMDNQTGAILGFVGGRNYQENQNNHAFDTKRSPASTTKPLLAYGIAIDQGLMGSE TILSNYPTNFANGNPIMYANSKGTGMMTLGEALNYSWNIPAYWTYRMLRENGVDVKGYME KMGYEIPEYGIESLPMGGGIEVTVAQHTNGYQTLANNGVYHQKHVISKIEAADGRVVYEY QDKPVQVYSKATATIMQGLLREVLSSRVTTTFKSNLTSLNPTLANADWIGKTGTTNQDEN MWLMLSTPRLTLGGWIGHDDNHSLSRRAGYSNNSNYMAHLVNAIQQASPSIWGNERFALD PSVVKSEVLKSTGQKPGKVSVEGKEVEVTGSTVTSYWANKSGAPATSYRFAIGGSDADYQ NAWSSIVGSLPTPSSSSSSSSSSSDSSNSSTTRPSSSRARR PF00905 Transpeptidase PF00912 Transgly component cell wall (sensu Bacteria) component external encapsulating structure component cell wall component cell function catalytic activity function binding function drug binding function penicillin binding process cell organization and biogenesis process peptidoglycan metabolism process external encapsulating structure organization and biogenesis process peptidoglycan biosynthesis process cell wall organization and biogenesis process cell wall organization and biogenesis (sensu Bacteria) process cell wall biosynthesis (sensu Bacteria) process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process process cellular physiological process process cellular carbohydrate metabolism "
drug:(2E)-2-({(2S)-2-CARBOXY-2-[(PHENOXYACETYL)AMINO]ETHOXY}IMINO)PENTANEDIOIC ACIDrdfs:label"(2E)-2-({(2S)-2-CARBOXY-2-[(PHENOXYACETYL)AMINO]ETHOXY}IMINO)PENTANEDIOIC ACID"
drug:(2E)-2-({(2S)-2-CARBOXY-2-[(PHENOXYACETYL)AMINO]ETHOXY}IMINO)PENTANEDIOIC ACIDrdf:typedrugbank:drugs
drug:(2E)-3-(2,4-DICHLOROPHENYL)-N-HYDROXYACRYLAMIDEdrugbank:description" experimental This compound belongs to the cinnamic acid amides. These are amides of cinnamic acids. Cinnamic Acid Amides Organic Compounds Phenylpropanoids and Polyketides Cinnamic Acids and Derivatives Cinnamic Acid Amides Phenylpropenes Dichlorobenzenes Styrenes Aryl Chlorides Enones Hydroxamic Acids Enolates Polyamines Organochlorides phenylpropene 1,3-dichlorobenzene styrene chlorobenzene benzene aryl chloride aryl halide enone carboxamide group hydroxamic acid enolate polyamine carboxylic acid derivative organohalogen organonitrogen compound amine organochloride logP 2.49 ALOGPS logS -3.6 ALOGPS Water Solubility 5.33e-02 g/l ALOGPS logP 2.53 ChemAxon IUPAC Name (2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide ChemAxon Traditional IUPAC Name (2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide ChemAxon Molecular Weight 232.063 ChemAxon Monoisotopic Weight 230.985383887 ChemAxon SMILES ONC(=O)\C=C\C1=CC=C(Cl)C=C1Cl ChemAxon Molecular Formula C9H7Cl2NO2 ChemAxon InChI InChI=1S/C9H7Cl2NO2/c10-7-3-1-6(8(11)5-7)2-4-9(13)12-14/h1-5,14H,(H,12,13)/b4-2+ ChemAxon InChIKey InChIKey=LHTLDFWBUPYUDR-DUXPYHPUSA-N ChemAxon Polar Surface Area (PSA) 49.33 ChemAxon Refractivity 56.26 ChemAxon Polarizability 21.34 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 9.55 ChemAxon pKa (strongest basic) -5.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11708451 PubChem Substance 99444289 ChemSpider 9883173 PDB GB4 BE0004101 Botulinum neurotoxin type A Clostridium botulinum # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Botulinum neurotoxin type A botA Clostridium botulinum UniProtKB P10845 UniProt Accession BXA1_CLOBO BE0004102 BoNT/A Clostridium botulinum # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown BoNT/A bont/a Clostridium botulinum UniProtKB Q7B8V4 UniProt Accession Q7B8V4_CLOBO "
drug:(2E)-3-(2,4-DICHLOROPHENYL)-N-HYDROXYACRYLAMIDErdfs:label"(2E)-3-(2,4-DICHLOROPHENYL)-N-HYDROXYACRYLAMIDE"
drug:(2E)-3-(2,4-DICHLOROPHENYL)-N-HYDROXYACRYLAMIDErdf:typedrugbank:drugs
drug:(2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACIDdrugbank:description" experimental This compound belongs to the cinnamic acids. These are organic aromatic compounds containing a benzene and a carboxylic acid group forming 3-phenylprop-2-enoic acid. Cinnamic Acids Organic Compounds Phenylpropanoids and Polyketides Cinnamic Acids and Derivatives Cinnamic Acids Phenylpropenes Styrenes Enones Polyamines Enolates Carboxylic Acids phenylpropene styrene benzene enone polyamine enolate carboxylic acid carboxylic acid derivative logP 5.09 ALOGPS logS -5.1 ALOGPS Water Solubility 1.87e-03 g/l ALOGPS logP 5.35 ChemAxon IUPAC Name (2E)-3-[2-(oct-1-yn-1-yl)phenyl]prop-2-enoic acid ChemAxon Traditional IUPAC Name (2E)-3-[2-(oct-1-yn-1-yl)phenyl]prop-2-enoic acid ChemAxon Molecular Weight 256.3395 ChemAxon Monoisotopic Weight 256.146329884 ChemAxon SMILES CCCCCCC#CC1=CC=CC=C1\C=C\C(O)=O ChemAxon Molecular Formula C17H20O2 ChemAxon InChI InChI=1S/C17H20O2/c1-2-3-4-5-6-7-10-15-11-8-9-12-16(15)13-14-17(18)19/h8-9,11-14H,2-6H2,1H3,(H,18,19)/b14-13+ ChemAxon InChIKey InChIKey=KRDSGPLHVQJFLM-BUHFOSPRSA-N ChemAxon Polar Surface Area (PSA) 37.3 ChemAxon Refractivity 76.74 ChemAxon Polarizability 30.78 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 4.07 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Ghose Filter true ChemAxon PubChem Compound 10308106 PubChem Substance 99444963 ChemSpider 8483572 PDB RS7 BE0000309 Arachidonate 15-lipoxygenase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Arachidonate 15-lipoxygenase Involved in oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Converts arachidonic acid to 15S- hydroperoxyeicosatetraenoic acid. Also acts on C-12 of arachidonate as well as on linoleic acid ALOX15 17p13.3 Cytoplasm None 6.56 74674.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:433 GenAtlas ALOX15 GeneCards ALOX15 GenBank Gene Database M23892 GenBank Protein Database 307135 UniProtKB P16050 UniProt Accession LOX15_HUMAN 15-LOX Arachidonate omega-6 lipoxygenase EC 1.13.11.33 >Arachidonate 15-lipoxygenase GLYRIRVSTGASLYAGSNNQVQLWLVGQHGEAALGKRLWPARGKETELKVEVPEYLGPLL FVKLRKRHLLKDDAWFCNWISVQGPGAGDEVRFPCYRWVEGNGVLSLPEGTGRTVGEDPQ GLFQKHREEELEERRKLYRWGNWKDGLILNMAGAKLYDLPVDERFLEDKRVDFEVSLAKG LADLAIKDSLNVLTCWKDLDDFNRIFWCGQSKLAERVRDSWKEDALFGYQFLNGANPVVL RRSAHLPARLVFPPGMEELQAQLEKELEGGTLFEADFSLLDGIKANVILCSQQHLAAPLV MLKLQPDGKLLPMVIQLQLPRTGSPPPPLFLPTDPPMAWLLAKCWVRSSDFQLHELQSHL LRGHLMAEVIVVATMRCLPSIHPIFKLIIPHLRYTLEINVRARTGLVSDMGIFDQIMSTG GGGHVQLLKQAGAFLTYSSFCPPDDLADRGLLGVKSSFYAQDALRLWEIIYRYVEGIVSL HYKTDVAVKDDPELQTWCREITEIGLQGAQDRGFPVSLQARDQVCHFVTMCIFTCTGQHA SVHLGQLDWYSWVPNAPCTMRLPPPTTKDATLETVMATLPNFHQASLQMSITWQLGRRQP VMVAVGQHEEEYFSGPEPKAVLKKFREELAALDKEIEIRNAKLDMPYEYLRPSVVENSVA I >1989 bp ATGGGTCTCTACCGCATCCGCGTGTCCACTGGGGCCTCGCTCTATGCCGGTTCCAACAAC CAGGTGCAGCTGTGGCTGGTCGGCCAGCACGGGGAGGCGGCGCTCGGGAAGCGACTGTGG CCCGCACGGGGCAAGGAGACAGAACTCAAGGTGGAAGTACCGGAGTATCTGGGGCCGCTG CTGTTTGTGAAACTGCGCAAACGGCACCTCCTTAAGGACGACGCCTGGTTCTGCAACTGG ATCTCTGTGCAGGGCCCCGGAGCCGGGGACGAGGTCAGGTTCCCTTGTTACCGCTGGGTG GAGGGCAACGGCGTCCTGAGCCTGCCTGAAGGCACCGGCCGCACTGTGGGCGAGGACCCT CAGGGCCTGTTCCAGAAACACCGGGAAGAAGAGCTGGAAGAGAGAAGGAAGTTGTACCGG TGGGGAAACTGGAAGGACGGGTTAATTCTGAATATGGCTGGGGCCAAACTATATGACCTC CCTGTGGATGAGCGATTTCTGGAAGACAAGAGAGTTGACTTTGAGGTTTCGCTGGCCAAG GGGCTGGCCGACCTCGCTATCAAAGACTCTCTAAATGTTCTGACTTGCTGGAAGGATCTA GATGACTTCAACCGGATTTTCTGGTGTGGTCAGAGCAAGCTGGCTGAGCGCGTGCGGGAC TCCTGGAAGGAAGATGCCTTATTTGGGTACCAGTTTCTTAATGGCGCCAACCCCGTGGTG CTGAGGCGCTCTGCTCACCTTCCTGCTCGCCTAGTGTTCCCTCCAGGCATGGAGGAACTG CAGGCCCAGCTGGAGAAGGAGCTGGAGGGAGGCACACTGTTCGAAGCTGACTTCTCCCTG CTGGATGGGATCAAGGCCAACGTCATTCTCTGTAGCCAGCAGCACCTGGCTGCCCCTCTA GTCATGCTGAAATTGCAGCCTGATGGGAAACTCTTGCCCATGGTCATCCAGCTCCAGCTG CCCCGCACAGGATCCCCACCACCTCCCCTTTTCTTGCCTACGGATCCCCCAATGGCCTGG CTTCTGGCCAAATGCTGGGTGCGCAGCTCTGACTTCCAGCTCCATGAGCTGCAGTCTCAT CTTCTGAGGGGACACTTGATGGCTGAGGTCATTGTTGTGGCCACCATGAGGTGCCTGCCG TCGATACATCCTATCTTCAAGCTTATAATTCCCCACCTGCGATACACCCTGGAAATTAAC GTCCGGGCCAGGACTGGGCTGGTCTCTGACATGGGAATTTTCGACCAGATAATGAGCACT GGTGGGGGAGGCCACGTGCAGCTGCTCAAGCAAGCTGGAGCCTTCCTAACCTACAGCTCC TTCTGTCCCCCTGATGACTTGGCCGACCGGGGGCTCCTGGGAGTGAAGTCTTCCTTCTAT GCCCAAGATGCGCTGCGGCTCTGGGAAATCATCTATCGGTATGTGGAAGGAATCGTGAGT CTCCACTATAAGACAGACGTGGCTGTGAAAGACGACCCAGAGCTGCAGACCTGGTGTCGA GAGATCACTGAAATCGGGCTGCAAGGGGCCCAGGACCGAGGGTTTCCTGTCTCTTTACAG GCTCGGGACCAGGTTTGCCACTTTGTCACCATGTGTATCTTCACCTGCACCGGCCAACAC GCCTCTGTGCACCTGGGCCAGCTGGACTGGTACTCTTGGGTGCCTAATGCACCCTGCACG ATGCGGCTGCCCCCGCCAACCACCAAGGATGCAACGCTGGAGACAGTGATGGCGACACTG CCCAACTTCCACCAGGCTTCTCTCCAGATGTCCATCACTTGGCAGCTGGGCAGACGCCAG CCCGTTATGGTGGCTGTGGGCCAGCATGAGGAGGAGTATTTTTCGGGCCCTGAGCCTAAG GCTGTGCTGAAGAAGTTCAGGGAGGAGCTGGCTGCCCTGGATAAGGAAATTGAGATCCGG AATGCAAAGCTGGACATGCCCTACGAGTACCTGCGGCCCAGCGTGGTGGAAAACAGTGTG GCCATCTAA PF01477 PLAT function ion binding function cation binding function transition metal ion binding function iron ion binding function binding function catalytic activity function oxidoreductase activity, acting on single donors with incorporation of molecular oxygen function oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen function oxidoreductase activity function lipoxygenase activity process fatty acid metabolism process icosanoid metabolism process leukotriene metabolism process generation of precursor metabolites and energy process electron transport process physiological process process organic acid metabolism process carboxylic acid metabolism process metabolism process cellular metabolism "
drug:(2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACIDrdfs:label"(2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID"
drug:(2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACIDrdf:typedrugbank:drugs
drug:(2E)-3-(3,4-DIHYDROXYPHENYL)-2-IMINOPROPANOIC ACIDdrugbank:description" experimental This compound belongs to the phenylpropanoic acids. These are compounds whose structure contain a benzene ring conjugated to a propanoic acid. Phenylpropanoic Acids Organic Compounds Phenylpropanoids and Polyketides Phenylpropanoic Acids Alpha Amino Acids and Derivatives Catechols Polyols Enols Enolates Carboxylic Acids Polyamines Imines 1,2-diphenol phenol derivative benzene polyol carboxylic acid derivative polyamine carboxylic acid enolate enol imine organonitrogen compound logP 0.69 ALOGPS logS -2.6 ALOGPS Water Solubility 5.33e-01 g/l ALOGPS logP 0.82 ChemAxon IUPAC Name 3-(3,4-dihydroxyphenyl)-2-iminopropanoic acid ChemAxon Traditional IUPAC Name 3-(3,4-dihydroxyphenyl)-2-iminopropanoic acid ChemAxon Molecular Weight 195.1721 ChemAxon Monoisotopic Weight 195.053157781 ChemAxon SMILES OC(=O)C(=N)CC1=CC(O)=C(O)C=C1 ChemAxon Molecular Formula C9H9NO4 ChemAxon InChI InChI=1S/C9H9NO4/c10-6(9(13)14)3-5-1-2-7(11)8(12)4-5/h1-2,4,10-12H,3H2,(H,13,14) ChemAxon InChIKey InChIKey=VFINRVRRNHRWEQ-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 101.61 ChemAxon Refractivity 59.15 ChemAxon Polarizability 18.15 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 3.62 ChemAxon pKa (strongest basic) 2.6 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937113 PubChem Substance 99444450 PDB IM3 BE0004141 D-amino-acid oxidase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown D-amino-acid oxidase Amino acid transport and metabolism Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D- amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids DAO 12q24 Peroxisome None 6.84 39473.7 Human HUGO Gene Nomenclature Committee (HGNC) GNC:2671 GeneCards DAO GenBank Gene Database X13227 GenBank Protein Database 30446 UniProtKB P14920 UniProt Accession OXDA_HUMAN DAAO DAMOX DAO >D-amino-acid oxidase MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPN NPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPR ELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGG IFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL >1044 bp ATGCGTGTGGTGGTGATTGGAGCAGGAGTCATCGGGCTGTCCACCGCCCTCTGCATCCAT GAGCGCTACCACTCAGTCCTGCAGCCACTGCACATAAAGGTCTACGCGGACCGCTTCACC CCACTCACCACCACCGACGTGGCTGCCGGCCTCTGGCAGCCCTACCTTTCTGACCCCAAC AACCCACAGGAGGCGGACTGGAGCCAACAGACCTTTGACTATCTCCTGAGCCATGTCCAT TCTCCCAACGCTGAAAACCTGGGCCTGTTCCTAATCTCGGGCTACAACCTCTTCCATGAA GCCATTCCGGACCCTTCCTGGAAGGACACAGTTCTGGGATTTCGGAAGCTGACCCCCAGA GAGCTGGATATGTTCCCAGATTACGGCTATGGCTGGTTCCACACAAGCCTAATTCTGGAG GGAAAGAACTATCTACAGTGGCTGACTGAAAGGTTAACTGAGAGGGGAGTGAAGTTCTTC CAGCGGAAAGTGGAGTCTTTTGAGGAGGTGGCAAGAGAAGGCGCAGACGTGATTGTCAAC TGCACTGGGGTATGGGCTGGGGCGCTACAACGAGACCCCCTGCTGCAGCCAGGCCGGGGG CAGATCATGAAGGTGGACGCCCCTTGGATGAAGCACTTCATTCTCACCCATGACCCAGAG AGAGGCATCTACAATTCCCCGTACATCATCCCAGGGACCCAGACAGTTACTCTTGGAGGC ATCTTCCAGTTGGGAAACTGGAGTGAACTAAACAATATCCAGGACCACAACACCATTTGG GAAGGCTGCTGCAGACTGGAGCCCACACTGAAGAATGCAAGAATTATTGGTGAAGCAACT GGCTTCCGGCCAGTACGCCCCCAGATTCGGCTAGAAAGAGAACAGCTTCGCACTGGACCT TCAAACACAGAGGTCATCCACAACTATGGCCATGGAGGCTACGGGCTCACCATCCACTGG GGATGTGCCCTGGAGGCAGCCAAGCTCTTTGGGAGAATCCTGGAAGAAAAGAAATTGTCC AGAATGCCACCATCCCACCTCTGA PF01266 DAO function catalytic activity function oxidoreductase activity function oxidoreductase activity, acting on the CH-NH2 group of donors function oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor function D-amino-acid oxidase activity process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process "
drug:(2E)-3-(3,4-DIHYDROXYPHENYL)-2-IMINOPROPANOIC ACIDrdfs:label"(2E)-3-(3,4-DIHYDROXYPHENYL)-2-IMINOPROPANOIC ACID"
drug:(2E)-3-(3,4-DIHYDROXYPHENYL)-2-IMINOPROPANOIC ACIDrdf:typedrugbank:drugs
drug:(2E)-3-(3,4-DIHYDROXYPHENYL)-N-[2-(4-HYDROXYPHENYL)ETHYL]ACRYLAMIDEdrugbank:description" experimental This compound belongs to the cinnamic acid amides. These are amides of cinnamic acids. Cinnamic Acid Amides Organic Compounds Phenylpropanoids and Polyketides Cinnamic Acids and Derivatives Cinnamic Acid Amides Hydroxycinnamic Acids and Derivatives Phenethylamines Phenylpropenes Styrenes Catechols Enones Polyols Secondary Carboxylic Acid Amides Enolates Enols Polyamines Carboxylic Acids phenylpropene phenethylamine styrene 1,2-diphenol phenol derivative benzene enone secondary carboxylic acid amide carboxamide group polyol carboxylic acid derivative carboxylic acid enolate enol polyamine amine organonitrogen compound logP 2.26 ALOGPS logS -3.9 ALOGPS Water Solubility 3.80e-02 g/l ALOGPS logP 2.66 ChemAxon IUPAC Name (2E)-3-(3,4-dihydroxyphenyl)-N-[2-(4-hydroxyphenyl)ethyl]prop-2-enamide ChemAxon Traditional IUPAC Name (2E)-3-(3,4-dihydroxyphenyl)-N-[2-(4-hydroxyphenyl)ethyl]prop-2-enamide ChemAxon Molecular Weight 299.3212 ChemAxon Monoisotopic Weight 299.115758037 ChemAxon SMILES OC1=CC=C(CCNC(=O)\C=C\C2=CC=C(O)C(O)=C2)C=C1 ChemAxon Molecular Formula C17H17NO4 ChemAxon InChI InChI=1S/C17H17NO4/c19-14-5-1-12(2-6-14)9-10-18-17(22)8-4-13-3-7-15(20)16(21)11-13/h1-8,11,19-21H,9-10H2,(H,18,22)/b8-4+ ChemAxon InChIKey InChIKey=VSHUQLRHTJOKTA-XBXARRHUSA-N ChemAxon Polar Surface Area (PSA) 89.79 ChemAxon Refractivity 85.09 ChemAxon Polarizability 31.99 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 9.04 ChemAxon pKa (strongest basic) 1.21 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon ChemSpider 8170478 PDB Y13 BE0004391 Peptide deformylase Helicobacter pylori # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Peptide deformylase Translation, ribosomal structure and biogenesis def Cytoplasmic None 6.25 20038.3 Helicobacter pylori GeneCards def GenBank Gene Database AY559449 GenBank Protein Database 49089809 UniProtKB Q672W7 UniProt Accession Q672W7_HELPX >Peptide deformylase MALLEIIHYPSKILRTISKEVVSFDAKLHQQLDDMYETMIASEGIGLAAIQVGLPLRMLI INLPQEDGVQHKEDCLEIINPKFIETGGSMMYKEGCLSVPGFYEEVERFEKVKIEYQNRF AEVKVLEASELLAVAIQHEIDHLNGVLFVDKLSILKRKKFEKELKELQKKQKHK PF01327 Pep_deformylase function ion binding function cation binding function transition metal ion binding function binding function iron ion binding function catalytic activity function peptide deformylase activity function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides process physiological process process macromolecule biosynthesis process protein biosynthesis process metabolism process macromolecule metabolism "
drug:(2E)-3-(3,4-DIHYDROXYPHENYL)-N-[2-(4-HYDROXYPHENYL)ETHYL]ACRYLAMIDErdfs:label"(2E)-3-(3,4-DIHYDROXYPHENYL)-N-[2-(4-HYDROXYPHENYL)ETHYL]ACRYLAMIDE"
drug:(2E)-3-(3,4-DIHYDROXYPHENYL)-N-[2-(4-HYDROXYPHENYL)ETHYL]ACRYLAMIDErdf:typedrugbank:drugs
drug:(2E)-3-(3-hydroxy-4-methoxyphenyl)prop-2-enoic aciddrugbank:description" experimental This compound belongs to the cinnamic acids. These are organic aromatic compounds containing a benzene and a carboxylic acid group forming 3-phenylprop-2-enoic acid. Cinnamic Acids Organic Compounds Phenylpropanoids and Polyketides Cinnamic Acids and Derivatives Cinnamic Acids Hydroxycinnamic Acids Coumaric Acids and Derivatives Methoxyphenols and Derivatives Phenylpropenes Anisoles Styrenes Alkyl Aryl Ethers Enones Polyols Polyamines Carboxylic Acids Enolates Enols methoxyphenol phenylpropene anisole phenol ether styrene alkyl aryl ether phenol derivative benzene enone polyol enol ether carboxylic acid carboxylic acid derivative polyamine enolate logP 1.56 ALOGPS logS -2.4 ALOGPS Water Solubility 8.71e-01 g/l ALOGPS logP 1.67 ChemAxon IUPAC Name (2E)-3-(3-hydroxy-4-methoxyphenyl)prop-2-enoic acid ChemAxon Traditional IUPAC Name isoferulic acid ChemAxon Molecular Weight 194.184 ChemAxon Monoisotopic Weight 194.057908808 ChemAxon SMILES COC1=C(O)C=C(\C=C\C(O)=O)C=C1 ChemAxon Molecular Formula C10H10O4 ChemAxon InChI InChI=1S/C10H10O4/c1-14-9-4-2-7(6-8(9)11)3-5-10(12)13/h2-6,11H,1H3,(H,12,13)/b5-3+ ChemAxon InChIKey InChIKey=QURCVMIEKCOAJU-HWKANZROSA-N ChemAxon Polar Surface Area (PSA) 66.76 ChemAxon Refractivity 51.5 ChemAxon Polarizability 19.36 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 3.77 ChemAxon pKa (strongest basic) -4.9 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 736186 PubChem Substance 99443580 ChemSpider 643318 PDB 4FE BE0003784 O-methyltransferase Synechocystis sp. (strain PCC 6803 / Kazusa) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown O-methyltransferase Involved in O-methyltransferase activity slr0095 None 5.83 24312.8 Synechocystis sp. (strain PCC 6803 / Kazusa) GenBank Gene Database BA000022 GenBank Protein Database 14595182 UniProtKB Q55813 UniProt Accession Q55813_SYNY3 >O-methyltransferase MGKGITGFDPSLYSYLQSISADDSFYLAQLRRETAHLPGAPMQISPEQAQFLGLLISLTG AKQVLEIGVFRGYSALAMALQLPPDGQIIACDQDPNATAIAKKYWQKAGVAEKISLRLGP ALATLEQLTQGKPLPEFDLIFIDADKRNYPRYYEIGLNLLRRGGLMVIDNVLWHGKVTEV DPQEAQTQVLQQFNRDLAQDERVRISVIPLGDGMTLALKK >558 bp GTGGGGCGTTTGGATCAAGATAGCGAAGGACTATTGCTGCTCACCAGCAACGGTAAACTT CAGCATCGTTTGGCCCACCGGGAGTTTGCCCACCAACGTACTTATTTTGCCCAAGTAGAA GGCTCTCCAACGGACGAAGACCTAGAACCCCTGCGGCGGGGCATAACTTTCGCGGATTAC CCTACCAGACCGGCGATCGCCAAAATTATCACTGAACCAGATTTTCCCCCCAGAAATCCT CCCATTCGTTATCGAGCCTCCATTCCCACCAGTTGGTTAAGCATTACCCTAACGGAGGGG CGCAATCGTCAGGTACGTCGAATGACAGCGGCAGTGGGCTTCCCTACCCTACGATTGGTG CGGGTGCAAATACAGGTTACTGGTCGCTCTCCCCAACAGGGCAAAGGTAAGTCAGCAGCA ACTTGGTGCTTAACCCTAGAAGGTTTGAGTCCGGGGCAATGGCGACCCCTGACCCCTTGG GAAGAAAATTTTTGCCAGCAACTCTTAACGGGAAATCCCAATGGTCCCTGGCAGAAAAAA TTTGGCGATCGCCGTTGA PF01596 Methyltransf_3 function catalytic activity function transferase activity function transferase activity, transferring one-carbon groups function methyltransferase activity function O-methyltransferase activity "
drug:(2E)-3-(3-hydroxy-4-methoxyphenyl)prop-2-enoic acidrdfs:label"(2E)-3-(3-hydroxy-4-methoxyphenyl)prop-2-enoic acid"
drug:(2E)-3-(3-hydroxy-4-methoxyphenyl)prop-2-enoic acidrdf:typedrugbank:drugs
drug:(2E)-3-(4-CHLOROPHENYL)-N-HYDROXYACRYLAMIDEdrugbank:description" experimental This compound belongs to the cinnamic acid amides. These are amides of cinnamic acids. Cinnamic Acid Amides Organic Compounds Phenylpropanoids and Polyketides Cinnamic Acids and Derivatives Cinnamic Acid Amides Phenylpropenes Styrenes Chlorobenzenes Aryl Chlorides Enones Hydroxamic Acids Enolates Polyamines Organochlorides phenylpropene styrene chlorobenzene aryl chloride benzene aryl halide enone carboxamide group hydroxamic acid enolate carboxylic acid derivative polyamine organohalogen organochloride amine organonitrogen compound logP 1.65 ALOGPS logS -3 ALOGPS Water Solubility 1.95e-01 g/l ALOGPS logP 1.93 ChemAxon IUPAC Name (2E)-3-(4-chlorophenyl)-N-hydroxyprop-2-enamide ChemAxon Traditional IUPAC Name (2E)-3-(4-chlorophenyl)-N-hydroxyprop-2-enamide ChemAxon Molecular Weight 197.618 ChemAxon Monoisotopic Weight 197.024356212 ChemAxon SMILES ONC(=O)\C=C\C1=CC=C(Cl)C=C1 ChemAxon Molecular Formula C9H8ClNO2 ChemAxon InChI InChI=1S/C9H8ClNO2/c10-8-4-1-7(2-5-8)3-6-9(12)11-13/h1-6,13H,(H,11,12)/b6-3+ ChemAxon InChIKey InChIKey=YPYUWBDOEMPXSK-ZZXKWVIFSA-N ChemAxon Polar Surface Area (PSA) 49.33 ChemAxon Refractivity 51.45 ChemAxon Polarizability 19.23 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 9.56 ChemAxon pKa (strongest basic) -5.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11694089 PubChem Substance 99444290 ChemSpider 9868814 PDB GB5 BE0004101 Botulinum neurotoxin type A Clostridium botulinum # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Botulinum neurotoxin type A botA Clostridium botulinum UniProtKB P10845 UniProt Accession BXA1_CLOBO BE0004102 BoNT/A Clostridium botulinum # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown BoNT/A bont/a Clostridium botulinum UniProtKB Q7B8V4 UniProt Accession Q7B8V4_CLOBO "
drug:(2E)-3-(4-CHLOROPHENYL)-N-HYDROXYACRYLAMIDErdfs:label"(2E)-3-(4-CHLOROPHENYL)-N-HYDROXYACRYLAMIDE"
drug:(2E)-3-(4-CHLOROPHENYL)-N-HYDROXYACRYLAMIDErdf:typedrugbank:drugs
drug:(2E)-3-{3-[(5-ETHYL-3-IODO-6-METHYL-2-OXO-1,2-DIHYDROPYRIDIN-4-YL)OXY]PHENYL}ACRYLONITRILEdrugbank:description" experimental This compound belongs to the diarylethers. These are organic compounds containing the dialkyl ether functional group, with the formula ROR', where R and R' are aryl groups. Diarylethers Organic Compounds Organooxygen Compounds Ethers Diarylethers Styrenes Phenol Ethers Dihydropyridines Pyridinones Aryl Iodides Polyamines Nitriles Organoiodides styrene phenol ether dihydropyridine pyridinone hydropyridine benzene pyridine aryl iodide aryl halide polyamine carbonitrile nitrile organoiodide organohalogen organonitrogen compound logP 3.97 ALOGPS logS -4.4 ALOGPS Water Solubility 1.74e-02 g/l ALOGPS logP 3.68 ChemAxon IUPAC Name (2E)-3-{3-[(5-ethyl-3-iodo-6-methyl-2-oxo-1,2-dihydropyridin-4-yl)oxy]phenyl}prop-2-enenitrile ChemAxon Traditional IUPAC Name (2E)-3-{3-[(3-ethyl-5-iodo-2-methyl-6-oxo-1H-pyridin-4-yl)oxy]phenyl}prop-2-enenitrile ChemAxon Molecular Weight 406.2177 ChemAxon Monoisotopic Weight 406.017821154 ChemAxon SMILES CCC1=C(C)NC(=O)C(I)=C1OC1=CC=CC(\C=C\C#N)=C1 ChemAxon Molecular Formula C17H15IN2O2 ChemAxon InChI InChI=1S/C17H15IN2O2/c1-3-14-11(2)20-17(21)15(18)16(14)22-13-8-4-6-12(10-13)7-5-9-19/h4-8,10H,3H2,1-2H3,(H,20,21)/b7-5+ ChemAxon InChIKey InChIKey=XMFUXIRAVPMVRS-FNORWQNLSA-N ChemAxon Polar Surface Area (PSA) 62.12 ChemAxon Refractivity 98.23 ChemAxon Polarizability 35.5 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 10.34 ChemAxon pKa (strongest basic) -4.7 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5459348 PubChem Substance 99443506 ChemSpider 4573144 PDB 3AC BE0002050 Gag-Pol polyprotein HIV-1 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Gag-Pol polyprotein Integrase performs the integration of the newly synthesized dsDNA copy of the viral genome into the host chromosome. The integrated DNA is called provirus gag-pol Nucleus. Cytoplasm (By similarity). Note=Following virus entry, the nuclear localization signal (NLS None 9.11 163290.0 HIV-1 GenBank Gene Database M15654 GenBank Protein Database 326388 UniProtKB P03366 UniProt Accession POL_HV1B1 CA Capsid protein p24 EC 2.7.7.49 EC 2.7.7.7 EC 3.1.26.4 EC 3.4.23.16 IN] Integrase MA NC Nucleocapsid protein p7 p15 p51 RT p6-pol p6* p66 RT PR Pr160Gag-Pol[Contains: Matrix protein p17 Protease Retropepsin Reverse transcriptase/ribonuclease H Spacer peptide p2 TF Transframe peptide >Gag-Pol polyprotein MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQI LGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAA DTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGAT PQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTT STLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRF YKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKA RVLAEAMSQVTNTATIMMQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEG HQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTISSEQTRANSPTRRELQVWGR DNNSPSEAGADRQGTVSFNFPQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPG RWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFP ISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVF AIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLD EDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIY QYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTV QPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAEL ELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAH TNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPP LVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQA IYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKG IGGNEQVDKLVSAGIRKILFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCD KCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFL LKLAGRWPVKTIHTDNGSNFTSATVKAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKI IGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQ NFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCV ASRQDED >1539 bp ATGGGTGCGAGAGCGTCAGTATTAAGCGGGGGAGAATTAGATCGATGGGAAAAAATTCGG TTAAGGCCAGGGGGAAAGAAAAAATATAAATTAAAACATATAGTATGGGCAAGCAGGGAG CTAGAACGATTCGCAGTTAATCCTGGCCTGTTAGAAACATCAGAAGGCTGTAGACAAATA CTGGGACAGCTACAACCATCCCTTCAGACAGGATCAGAAGAACTTAGATCATTATATAAT ACAGTAGCAACCCTCTATTGTGTGCATCAAAGGATAGAGATAAAAGACACCAAGGAAGCT TTAGACAAGATAGAGGAAGAGCAAAACAAAAGTAAGAAAAAAGCACAGCAAGCAGCAGCT GACACAGGACACAGCAGTCAGGTCAGCCAAAATTACCCTATAGTGCAGAACATCCAGGGG CAAATGGTACATCAGGCCATATCACCTAGAACTTTAAATGCATGGGTAAAAGTAGTAGAA GAGAAGGCTTTCAGCCCAGAAGTAATACCCATGTTTTCAGCATTATCAGAAGGAGCCACC CCACAAGATTTAAACACCATGCTAAACACAGTGGGGGGACATCAAGCAGCCATGCAAATG TTAAAAGAGACCATCAATGAGGAAGCTGCAGAATGGGATAGAGTACATCCAGTGCATGCA GGGCCTATTGCACCAGGCCAGATGAGAGAACCAAGGGGAAGTGACATAGCAGGAACTACT AGTACCCTTCAGGAACAAATAGGATGGATGACAAATAATCCACCTATCCCAGTAGGAGAA ATTTATAAAAGATGGATAATCCTGGGATTAAATAAAATAGTAAGAATGTATAGCCCTACC AGCATTCTGGACATAAGACAAGGACCAAAAGAACCTTTTAGAGACTATGTAGACCGGTTC TATAAAACTCTAAGAGCCGAGCAAGCTTCACAGGAGGTAAAAAATTGGATGACAGAAACC TTGTTGGTCCAAAATGCGAACCCAGATTGTAAGACTATTTTAAAAGCATTGGGACCAGCG GCTACACTAGAAGAAATGATGACAGCATGTCAGGGAGTAGGAGGACCCGGCCATAAGGCA AGAGTTTTGGCTGAAGCAATGAGCCAAGTAACAAATACAGCTACCATAATGATGCAGAGA GGCAATTTTAGGAACCAAAGAAAGATGGTTAAGTGTTTCAATTGTGGCAAAGAAGGGCAC ACAGCCAGAAATTGCAGGGCCCCTAGGAAAAAGGGCTGTTGGAAATGTGGAAAGGAAGGA CACCAAATGAAAGATTGTACTGAGAGACAGGCTAATTTTTTAGGGAAGATCTGGCCTTCC TACAAGGGAAGGCCAGGGAATTTTCTTCAGAGCAGACCAGAGCCAACAGCCCCACCATTT CTTCAGAGCAGACCAGAGCCAACAGCCCCACCAGAAGAGAGCTTCAGGTCTGGGGTAGAG ACAACAACTCCCCCTCAGAAGCAGGAGCCGATAGACAAGGAACTGTATCCTTTAACTTCC CTCAGATCACTCTTTGGCAACGACCCCTCGTCACAATAA PF00078 RVT_1 PF00540 Gag_p17 PF00607 Gag_p24 PF00552 Integrase PF02022 Integrase_Zn PF00075 RnaseH PF00665 rve PF00077 RVP PF06815 RVT_connect PF06817 RVT_thumb PF00098 zf-CCHC function nucleotidyltransferase activity function hydrolase activity function integrase activity function aspartic-type endopeptidase activity function ion binding function cation binding function peptidase activity function nuclease activity function transition metal ion binding function endopeptidase activity function RNA-directed DNA polymerase activity function transferase activity function binding function endonuclease activity function zinc ion binding function hydrolase activity, acting on ester bonds function endoribonuclease activity function transferase activity, transferring phosphorus-containing groups function DNA binding function catalytic activity function endoribonuclease activity, producing 5'-phosphomonoesters function nucleic acid binding function ribonuclease H activity function RNA binding function structural molecule activity process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA recombination process macromolecule metabolism process DNA integration process protein metabolism process cellular protein metabolism process viral life cycle process proteolysis process physiological process process DNA replication process metabolism process DNA metabolism process cellular metabolism process RNA-dependent DNA replication "
drug:(2E)-3-{3-[(5-ETHYL-3-IODO-6-METHYL-2-OXO-1,2-DIHYDROPYRIDIN-4-YL)OXY]PHENYL}ACRYLONITRILErdfs:label"(2E)-3-{3-[(5-ETHYL-3-IODO-6-METHYL-2-OXO-1,2-DIHYDROPYRIDIN-4-YL)OXY]PHENYL}ACRYLONITRILE"
drug:(2E)-3-{3-[(5-ETHYL-3-IODO-6-METHYL-2-OXO-1,2-DIHYDROPYRIDIN-4-YL)OXY]PHENYL}ACRYLONITRILErdf:typedrugbank:drugs
drug:(2E)-N-hydroxy-3-[1-methyl-4-(phenylacetyl)-1H-pyrrol-2-yl]prop-2-enamidedrugbank:description" experimental This compound belongs to the benzene and substituted derivatives. These are aromatic compounds containing at least one benzene ring. Benzene and Substituted Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives N-methylpyrroles Enones Hydroxamic Acids Polyamines Enolates pyrrole enone ketone hydroxamic acid carboxamide group carboxylic acid derivative enolate polyamine organonitrogen compound amine carbonyl group logP 1.89 ALOGPS logS -3.7 ALOGPS Water Solubility 5.39e-02 g/l ALOGPS logP 1.94 ChemAxon IUPAC Name (2E)-N-hydroxy-3-[1-methyl-4-(2-phenylacetyl)-1H-pyrrol-2-yl]prop-2-enamide ChemAxon Traditional IUPAC Name (2E)-N-hydroxy-3-[1-methyl-4-(2-phenylacetyl)pyrrol-2-yl]prop-2-enamide ChemAxon Molecular Weight 284.3098 ChemAxon Monoisotopic Weight 284.116092388 ChemAxon SMILES CN1C=C(C=C1\C=C\C(=O)NO)C(=O)CC1=CC=CC=C1 ChemAxon Molecular Formula C16H16N2O3 ChemAxon InChI InChI=1S/C16H16N2O3/c1-18-11-13(10-14(18)7-8-16(20)17-21)15(19)9-12-5-3-2-4-6-12/h2-8,10-11,21H,9H2,1H3,(H,17,20)/b8-7+ ChemAxon InChIKey InChIKey=UFQOXIMRSMFQRI-BQYQJAHWSA-N ChemAxon Polar Surface Area (PSA) 71.33 ChemAxon Refractivity 81.3 ChemAxon Polarizability 30.18 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 9.52 ChemAxon pKa (strongest basic) -5.2 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 10379137 PubChem Substance 99443821 ChemSpider 8554580 PDB AGE BE0001608 Histone deacetylase 8 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Histone deacetylase 8 Chromatin structure and dynamics Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes HDAC8 Xq13 Nucleus. Note=Excluded from the nucleoli None 5.37 41758.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:13315 GenAtlas HDAC8 GeneCards HDAC8 GenBank Gene Database AF230097 GenBank Protein Database 8118721 UniProtKB Q9BY41 UniProt Accession HDAC8_HUMAN HD8 >Histone deacetylase 8 MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPK VASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATI TAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLH HGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKY YQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLI LGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPH RIQQILNYIKGNLKHVV >1134 bp ATGGAGGAGCCGGAGGAACCGGCGGACAGTGGGCAGTCGCTGGTCCCGGTTTATATCTAT AGTCCCGAGTATGTCAGTATGTGTGACTCCCTGGCCAAGATCCCCAAACGGGCCAGTATG GTGCATTCTTTGATTGAAGCATATGCACTGCATAAGCAAATGAGGATAGTTAAGCCTAAA GTGGCCTCCATGGAGGAGATGGCCACCTTCCACACTGATGCTTATCTGCAGCATCTCCAG AAGGTCAGCCAAGAGGGCGATGATGATCATCCGGACTCCATAGAATATGGGCTAGGTTAT GACTGCCCAGCCACTGAAGGGATATTTGACTATGCAGCAGCTATAGGAGGGGCTACGATC ACAGCTGCCCAATGCCTGATTGACGGAATGTGCAAAGTAGCAATTAACTGGTCTGGAGGG TGGCATCATGCAAAGAAAGATGAAGCATCTGGTTTTTGTTATCTCAATGATGCTGTCCTG GGAATATTACGATTGCGACGGAAATTTGAGCGTATTCTCTACGTGGATTTGGATCTGCAC CATGGAGATGGTGTAGAAGACGCATTCAGTTTCACCTCCAAAGTCATGACCGTGTCCCTG CACAAATTCTCCCCAGGATTTTTCCCAGGAACAGGTGACGTGTCTGATGTTGGCCTAGGG AAGGGACGGTACTACAGTGTAAATGTGCCCATTCAGGATGGCATACAAGATGAAAAATAT TACCAGATCTGTGAAAGTGTACTAAAGGAAGTATACCAAGCCTTTAATCCCAAAGCAGTG GTCTTACAGCTGGGAGCTGACACAATAGCTGGGGATCCCATGTGCTCCTTTAACATGACT CCAGTGGGAATTGGCAAGTGTCTTAAGTACATCCTTCAATGGCAGTTGGCAACACTCATT TTGGGAGGAGGAGGCTATAACCTTGCCAACACGGCTCGATGCTGGACATACTTGACCGGG GTCATCCTAGGGAAAACACTATCCTCTGAGATCCCAGATCATGAGTTTTTCACAGCATAT GGTCCTGATTATGTGCTGGAAATCACGCCAAGCTGCCGGCCAGACCGCAATGAGCCCCAC CGAATCCAACAAATCCTCAACTACATCAAAGGGAATCTGAAGCATGTGGTCTAG PF00850 Hist_deacetyl component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function hydrolase activity function histone deacetylase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides function catalytic activity process metabolism process protein amino acid deacetylation process histone deacetylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification process physiological process "
drug:(2E)-N-hydroxy-3-[1-methyl-4-(phenylacetyl)-1H-pyrrol-2-yl]prop-2-enamiderdfs:label"(2E)-N-hydroxy-3-[1-methyl-4-(phenylacetyl)-1H-pyrrol-2-yl]prop-2-enamide"
drug:(2E)-N-hydroxy-3-[1-methyl-4-(phenylacetyl)-1H-pyrrol-2-yl]prop-2-enamiderdf:typedrugbank:drugs
drug:(2E)-N-{4-[(3-bromophenyl)amino]quinazolin-6-yl}-4-(dimethylamino)but-2-enamidedrugbank:description" experimental This compound belongs to the quinazolinamines. These are heterocyclic aromatic compounds containing a quianazoline moiety substituted by one or more amine groups. Quinazolinamines Organic Compounds Heterocyclic Compounds Naphthyridines Quinazolines Anilides Aminopyrimidines and Derivatives Bromobenzenes Aryl Bromides Enones Tertiary Amines Secondary Carboxylic Acid Amides Polyamines Carboxylic Acids Secondary Amines Enolates Organobromides aminopyrimidine bromobenzene benzene aryl halide aryl bromide pyrimidine enone secondary carboxylic acid amide carboxamide group tertiary amine polyamine carboxylic acid derivative enolate carboxylic acid secondary amine organohalogen amine organobromide organonitrogen compound logP 3.81 ALOGPS logS -4.6 ALOGPS Water Solubility 1.17e-02 g/l ALOGPS logP 4.04 ChemAxon IUPAC Name (2E)-N-{4-[(3-bromophenyl)amino]quinazolin-6-yl}-4-(dimethylamino)but-2-enamide ChemAxon Traditional IUPAC Name (2E)-N-{4-[(3-bromophenyl)amino]quinazolin-6-yl}-4-(dimethylamino)but-2-enamide ChemAxon Molecular Weight 426.31 ChemAxon Monoisotopic Weight 425.085122934 ChemAxon SMILES CN(C)C\C=C\C(=O)NC1=CC=C2N=CN=C(NC3=CC(Br)=CC=C3)C2=C1 ChemAxon Molecular Formula C20H20BrN5O ChemAxon InChI InChI=1S/C20H20BrN5O/c1-26(2)10-4-7-19(27)24-16-8-9-18-17(12-16)20(23-13-22-18)25-15-6-3-5-14(21)11-15/h3-9,11-13H,10H2,1-2H3,(H,24,27)(H,22,23,25)/b7-4+ ChemAxon InChIKey InChIKey=ZCIXBBSRVLSRJQ-QPJJXVBHSA-N ChemAxon Polar Surface Area (PSA) 70.15 ChemAxon Refractivity 113.91 ChemAxon Polarizability 42.29 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 14.36 ChemAxon pKa (strongest basic) 8.81 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 5328969 PubChem Substance 99445035 ChemSpider 4486131 PDB SR2 BE0000838 Proto-oncogene tyrosine-protein kinase Src Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Proto-oncogene tyrosine-protein kinase Src Involved in protein kinase activity SRC 20q12-q13 None 7.47 59704.0 Human HUGO Gene Nomenclature Committee (HGNC) 11283 GenAtlas SRC GeneCards SRC GenBank Gene Database AL133293 GenBank Protein Database 10635153 UniProtKB P12931 UniProt Accession SRC_HUMAN c- Src EC 2.7.10.2 p60-Src pp60c-src >Proto-oncogene tyrosine-protein kinase Src GSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEP KLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDW WLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESE TTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLC HRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLK PGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYL RLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTA RQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERG YRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL >1611 bp ATGGGTAGCAACAAGAGCAAGCCCAAGGATGCCAGCCAGCGGCGCCGCAGCCTGGAGCCC GCCGAGAACGTGCACGGCGCTGGCGGGGGCGCTTTCCCCGCCTCGCAGACCCCCAGCAAG CCAGCCTCGGCCGACGGCCACCGCGGCCCCAGCGCGGCCTTCGCCCCCGCGGCCGCCGAG CCCAAGCTGTTCGGAGGCTTCAACTCCTCGGACACCGTCACCTCCCCGCAGAGGGCGGGC CCGCTGGCCGGTGGAGTGACCACCTTTGTGGCCCTCTATGACTATGAGTCTAGGACGGAG ACAGACCTGTCCTTCAAGAAAGGCGAGCGGCTCCAGATTGTCAACAACACAGAGGGAGAC TGGTGGCTGGCCCACTCGCTCAGCACAGGACAGACAGGCTACATCCCCAGCAACTACGTG GCGCCCTCCGACTCCATCCAGGCTGAGGAGTGGTATTTTGGCAAGATCACCAGACGGGAG TCAGAGCGGTTACTGCTCAATGCAGAGAACCCGAGAGGGACCTTCCTCGTGCGAGAAAGT GAGACCACGAAAGGTGCCTACTGCCTCTCAGTGTCTGACTTCGACAACGCCAAGGGCCTC AACGTGAAGCACTACAAGATCCGCAAGCTGGACAGCGGCGGCTTCTACATCACCTCCCGC ACCCAGTTCAACAGCCTGCAGCAGCTGGTGGCCTACTACTCCAAACACGCCGATGGCCTG TGCCACCGCCTCACCACCGTGTGCCCCACGTCCAAGCCGCAGACTCAGGGCCTGGCCAAG GATGCCTGGGAGATCCCTCGGGAGTCGCTGCGGCTGGAGGTCAAGCTGGGCCAGGGCTGC TTTGGCGAGGTGTGGATGGGGACCTGGAACGGTACCACCAGGGTGGCCATCAAAACCCTG AAGCCTGGCACGATGTCTCCAGAGGCCTTCCTGCAGGAGGCCCAGGTCATGAAGAAGCTG AGGCATGAGAAGCTGGTGCAGTTGTATGCTGTGGTTTCAGAGGAGCCCATTTACATCGTC ACGGAGTACATGAGCAAGGGGAGTTTGCTGGACTTTCTCAAGGGGGAGACAGGCAAGTAC CTGCGGCTGCCTCAGCTGGTGGACATGGCTGCTCAGATCGCCTCAGGCATGGCGTACGTG GAGCGGATGAACTACGTCCACCGGGACCTTCGTGCAGCCAACATCCTGGTGGGAGAGAAC CTGGTGTGCAAAGTGGCGGACTTTGGGCTGGCTCGGCTCATTGAAGACAATGAGTACACG GCGCGGCAAGGTGCCAAATTCCCCATCAAGTGGACGGCTCCAGAAGCTGCCCTCTATGGC CGCTTCACCATCAAGTCGGACGTGTGGTCCTTCGGGATCCTGCTGACTGAGCTCACCACA AAGGGACGGGTGCCCTACCCTGGGATGGTGAACCGCGAGGTGCTGGACCAGGTGGAGCGG GGCTACCGGATGCCCTGCCCGCCGGAGTGTCCCGAGTCCCTGCACGACCTCATGTGCCAG TGCTGGCGGAAGGAGCCTGAGGAGCGGCCCACCTTCGAGTACCTGCAGGCCTTCCTGGAG GACTACTTCACGTCCACCGAGCCCCAGTACCAGCCCGGGGAGAACCTCTAG PF07714 Pkinase_Tyr PF00017 SH2 PF00018 SH3_1 function ATP binding function transferase activity, transferring phosphorus-containing groups function kinase activity function nucleotide binding function protein kinase activity function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function catalytic activity function protein-tyrosine kinase activity process biopolymer metabolism process biopolymer modification process protein modification process intracellular signaling cascade process protein amino acid phosphorylation process physiological process process cellular process process cell communication process metabolism process signal transduction process macromolecule metabolism "
drug:(2E)-N-{4-[(3-bromophenyl)amino]quinazolin-6-yl}-4-(dimethylamino)but-2-enamiderdfs:label"(2E)-N-{4-[(3-bromophenyl)amino]quinazolin-6-yl}-4-(dimethylamino)but-2-enamide"
drug:(2E)-N-{4-[(3-bromophenyl)amino]quinazolin-6-yl}-4-(dimethylamino)but-2-enamiderdf:typedrugbank:drugs
drug:(2E,4E)-11-METHOXY-3,7,11-TRIMETHYLDODECA-2,4-DIENOIC ACIDdrugbank:description" experimental This compound belongs to the sesquiterpenes. These are terpenes with three consecutive isoprene units. Sesquiterpenes Organic Compounds Lipids Prenol Lipids Sesquiterpenes Methoxy Fatty Acids Branched Fatty Acids Unsaturated Fatty Acids Enones Enolates Polyamines Carboxylic Acids Ethers enone ether polyamine enolate carboxylic acid carboxylic acid derivative logP 5.18 ALOGPS logS -4.5 ALOGPS Water Solubility 8.68e-03 g/l ALOGPS logP 4.1 ChemAxon IUPAC Name (2E,4E,7S)-11-methoxy-3,7,11-trimethyldodeca-2,4-dienoic acid ChemAxon Traditional IUPAC Name (2E,4E,7S)-11-methoxy-3,7,11-trimethyldodeca-2,4-dienoic acid ChemAxon Molecular Weight 268.3917 ChemAxon Monoisotopic Weight 268.203844762 ChemAxon SMILES COC(C)(C)CCC[C@@](C)([H])C\C=C\C(\C)=C\C(O)=O ChemAxon Molecular Formula C16H28O3 ChemAxon InChI InChI=1S/C16H28O3/c1-13(10-7-11-16(3,4)19-5)8-6-9-14(2)12-15(17)18/h6,9,12-13H,7-8,10-11H2,1-5H3,(H,17,18)/b9-6+,14-12+/t13-/m1/s1 ChemAxon InChIKey InChIKey=MNYBEULOKRVZKY-ATCPXPEISA-N ChemAxon Polar Surface Area (PSA) 46.53 ChemAxon Refractivity 80.86 ChemAxon Polarizability 32.11 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 5.05 ChemAxon pKa (strongest basic) -4.1 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5288795 PubChem Substance 99444646 ChemSpider 4450887 PDB MEI BE0003740 Nuclear receptor coactivator 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Nuclear receptor coactivator 2 Involved in nuclear hormone receptor binding Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF- 2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues NCOA2 8q13.3 Nucleus None 6.62 159155.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:7669 GeneCards NCOA2 GenBank Gene Database X97674 GenBank Protein Database 1877215 UniProtKB Q15596 UniProt Accession NCOA2_HUMAN hTIF2 NCoA-2 Transcriptional intermediary factor 2 >Nuclear receptor coactivator 2 MSGMGENTSDPSRAETRKRKECPDQLGPSPKRNTEKRNREQENKYIEELAELIFANFNDI DNFNFKPDKCAILKETVKQIRQIKEQEKAAAANIDEVQKSDVSSTGQGVIDKDALGPMML EALDGFFFVVNLEGNVVFVSENVTQYLRYNQEELMNKSVYSILHVGDHTEFVKNLLPKSI VNGGSWSGEPPRRNSHTFNCRMLVKPLPDSEEEGHDNQEAHQKYETMQCFAVSQPKSIKE EGEDLQSCLICVARRVPMKERPVLPSSESFTTRQDLQGKITSLDTSTMRAAMKPGWEDLV RRCIQKFHAQHEGESVSYAKRHHHEVLRQGLAFSQIYRFSLSDGTLVAAQTKSKLIRSQT TNEPQLVISLHMLHREQNVCVMNPDLTGQTMGKPLNPISSNSPAHQALCSGNPGQDMTLS SNINFPINGPKEQMGMPMGRFGGSGGMNHVSGMQATTPQGSNYALKMNSPSQSSPGMNPG QPTSMLSPRHRMSPGVAGSPRIPPSQFSPAGSLHSPVGVCSSTGNSHSYTNSSLNALQAL SEGHGVSLGSSLASPDLKMGNLQNSPVNMNPPPLSKMGSLDSKDCFGLYGEPSEGTTGQA ESSCHPGEQKETNDPNLPPAVSSERADGQSRLHDSKGQTKLLQLLTTKSDQMEPSPLASS LSDTNKDSTGSLPGSGSTHGTSLKEKHKILHRLLQDSSSPVDLAKLTAEATGKDLSQESS STAPGSEVTIKQEPVSPKKKENALLRYLLDKDDTKDIGLPEITPKLERLDSKTDPASNTK LIAMKTEKEEMSFEPGDQPGSELDNLEEILDDLQNSQLPQLFPDTRPGAPAGSVDKQAII NDLMQLTAENSPVTPVGAQKTALRISQSTFNNPRPGQLGRLLPNQNLPLDITLQSPTGAG PFPPIRNSSPYSVIPQPGMMGNQGMIGNQGNLGNSSTGMIGNSASRPTMPSGEWAPQSSA VRVTCAATTSAMNRPVQGGMIRNPAASIPMRPSSQPGQRQTLQSQVMNIGPSELEMNMGG PQYSQQQAPPNQTAPWPESILPIDQASFASQNRQPFGSSPDDLLCPHPAAESPSDEGALL DQLYLALRNFDGLEEIDRALGIPELVSQSQAVDPEQFSSQDSNIMLEQKAPVFPQQYASQ AQMAQGSYSPMQDPNFHTMGQRPSYATLRMQPRPGLRPTGLVQNQPNQLRLQLQHRLQAQ QNRQPLMNQISNVSNVNLTLRPGVPTQAPINAQMLAQRQREILNQHLRQRQMHQQQQVQQ RTLMMRGQGLNMTPSMVAPSGMPATMSNPRIPQANAQQFPFPPNYGISQQPDPGFTGATT PQSPLMSPRMAHTQSPMMQQSQANPAYQAPSDINGWAQGNMGGNSMFSQQSPPHFGQQAN TSMYSNNMNINVSMATNTGGMSSMNQMTGQISMTSVTSVPTSGLSSMGPEQVNDPALRGG NLFPNQLPGMDMIKQEGDTTRKYC >4395 bp ATGAGTGGGATGGGAGAAAATACCTCTGACCCCTCCAGGGCAGAGACAAGAAAGCGCAAG GAATGTCCTGACCAACTTGGACCCAGCCCCAAAAGGAACACTGAAAAACGTAATCGTGAA CAGGAAAATAAATATATAGAAGAACTTGCAGAGTTGATTTTTGCAAATTTTAATGATATA GACAACTTTAACTTCAAACCTGACAAATGTGCAATCTTAAAAGAAACTGTGAAGCAAATT CGTCAGATCAAAGAACAAGAGAAAGCAGCAGCTGCCAACATAGATGAAGTGCAGAAGTCA GATGTATCCTCTACAGGGCAGGGTGTCATCGACAAGGATGCGCTGGGGCCTATGATGCTT GAGGCCCTTGATGGGTTCTTCTTTGTAGTGAACCTGGAAGGCAACGTTGTGTTTGTGTCA GAGAATGTGACACAGTATCTAAGGTATAACCAAGAAGAGCTGATGAACAAAAGTGTATAT AGCATCTTGCATGTTGGGGACCACACGGAATTTGTCAAAAACCTGCTGCCAAAGTCTATA GTAAATGGGGGATCTTGGTCTGGCGAACCTCCGAGGCGGAACAGCCATACCTTCAATTGT CGGATGCTGGTAAAACCTTTACCTGATTCAGAAGAGGAGGGTCATGATAACCAGGAAGCT CATCAGAAATATGAAACTATGCAGTGCTTCGCTGTCTCTCAACCAAAGTCCATCAAAGAA GAAGGAGAAGATTTGCAGTCCTGCTTGATTTGCGTGGCAAGAAGAGTTCCCATGAAGGAA AGACCAGTTCTTCCCTCATCAGAAAGTTTTACTACTCGCCAGGATCTCCAAGGCAAGATC ACGTCTCTGGATACCAGCACCATGAGAGCAGCCATGAAACCAGGCTGGGAGGACCTGGTA AGAAGGTGTATTCAGAAGTTCCATGCGCAGCATGAAGGAGAATCTGTGTCCTATGCTAAG AGGCATCATCATGAAGTACTGAGACAAGGATTGGCATTCAGTCAAATCTATCGTTTTTCC TTGTCTGATGGCACTCTTGTTGCTGCACAAACGAAGAGCAAACTCATCCGTTCTCAGACT ACTAATGAACCTCAACTTGTAATATCTTTACATATGCTTCACAGAGAGCAGAATGTGTGT GTGATGAATCCGGATCTGACTGGACAAACGATGGGGAAGCCACTGAATCCAATTAGCTCT AACAGCCCTGCCCATCAGGCCCTGTGCAGTGGGAACCCAGGTCAGGACATGACCCTCAGT AGCAATATAAATTTTCCCATAAATGGCCCAAAGGAACAAATGGGCATGCCCATGGGCAGG TTTGGTGGTTCTGGGGGAATGAACCATGTGTCAGGCATGCAAGCAACCACTCCTCAGGGT AGTAACTATGCACTCAAAATGAACAGCCCCTCACAAAGCAGCCCTGGCATGAATCCAGGA CAGCCCACCTCCATGCTTTCACCAAGGCATCGCATGAGCCCTGGAGTGGCTGGCAGCCCT CGAATCCCACCCAGTCAGTTTTCCCCTGCAGGAAGCTTGCATTCCCCTGTGGGAGTTTGC AGCAGCACAGGAAATAGCCATAGTTATACCAACAGCTCCCTCAATGCACTTCAGGCCCTC AGCGAGGGGCACGGGGTCTCATTAGGGTCATCGTTGGCTTCACCAGACCTAAAAATGGGC AATTTGCAAAACTCCCCAGTTAATATGAATCCTCCCCCACTCAGCAAGATGGGAAGCTTG GACTCAAAAGACTGTTTTGGACTATATGGGGAGCCCTCTGAAGGTACAACTGGACAAGCA GAGAGCAGCTGCCATCCTGGAGAGCAAAAGGAAACAAATGACCCCAACCTGCCCCCGGCC GTGAGCAGTGAGAGAGCTGACGGGCAGAGCAGACTGCATGACAGCAAAGGGCAGACCAAA CTCCTGCAGCTGCTGACCACCAAATCTGATCAGATGGAGCCCTCGCCCTTAGCCAGCTCT TTGTCGGATACAAACAAAGACTCCACAGGTAGCTTGCCTGGTTCTGGGTCTACACATGGA ACCTCGCTCAAGGAGAAGCATAAAATTTTGCACAGACTCTTGCAGGACAGCAGTTCCCCT GTGGACTTGGCCAAGTTAACAGCAGAAGCCACAGGCAAAGACCTGAGCCAGGAGTCCAGC AGCACAGCTCCTGGATCAGAAGTGACTATTAAACAAGAGCCGGTGAGCCCCAAGAAGAAA GAGAATGCACTACTTCGCTATTTGCTAGATAAAGATGATACTAAAGATATTGGTTTACCA GAAATAACCCCCAAACTTGAGAGACTGGACAGTAAGACAGATCCTGCCAGTAACACAAAA TTAATAGCAATGAAAACTGAGAAGGAGGAGATGAGCTTTGAGCCTGGTGACCAGCCTGGC AGTGAGCTGGACAACTTGGAGGAGATTTTGGATGATTTGCAGAATAGTCAATTACCACAG CTTTTCCCAGACACGAGGCCAGGCGCCCCTGCTGGATCAGTTGACAAGCAAGCCATCATC AATGACCTCATGCAACTCACAGCTGAAAACAGCCCTGTCACACCTGTTGGAGCCCAGAAA ACAGCACTGCGAATTTCACAGAGCACTTTTAATAACCCACGACCAGGGCAACTGGGCAGG TTATTGCCAAACCAGAATTTACCACTTGACATCACATTGCAAAGCCCAACTGGTGCTGGA CCTTTCCCACCAATCAGAAACAGTAGTCCCTACTCAGTGATACCTCAGCCAGGAATGATG GGTAATCAAGGGATGATAGGAAACCAAGGAAATTTAGGGAACAGTAGCACAGGAATGATT GGTAACAGTGCTTCTCGGCCTACTATGCCATCTGGAGAATGGGCACCGCAGAGTTCGGCT GTGAGAGTCACCTGTGCTGCTACCACCAGTGCCATGAACCGGCCAGTCCAAGGAGGTATG ATTCGGAACCCAGCAGCCAGCATCCCCATGAGGCCCAGCAGCCAGCCTGGCCAAAGACAG ACGCTTCAGTCTCAGGTCATGAATATAGGGCCATCTGAATTAGAGATGAACATGGGGGGA CCTCAGTATAGCCAACAACAAGCTCCTCCAAATCAGACTGCCCCATGGCCTGAAAGCATC CTGCCTATAGACCAGGCGTCTTTTGCCAGCCAAAACAGGCAGCCATTTGGCAGTTCTCCA GATGACTTGCTATGTCCACATCCTGCAGCTGAGTCTCCGAGTGATGAGGGAGCTCTCCTG GACCAGCTGTATCTGGCCTTGCGGAATTTTGATGGCCTGGAGGAGATTGATAGAGCCTTA GGAATACCCGAACTGGTCAGCCAGAGCCAAGCAGTAGATCCAGAACAGTTCTCAAGTCAG GATTCCAACATCATGCTGGAGCAGAAGGCGCCCGTTTTCCCACAGCAGTATGCATCTCAG GCACAAATGGCCCAGGGTAGCTATTCTCCCATGCAAGATCCAAACTTTCACACCATGGGA CAGCGGCCTAGTTATGCCACACTCCGTATGCAGCCCAGACCGGGCCTCAGGCCCACGGGC CTAGTGCAGAACCAGCCAAATCAACTAAGACTTCAACTTCAGCATCGCCTCCAAGCACAG CAGAATCGCCAGCCACTTATGAATCAAATCAGCAATGTTTCCAATGTGAACTTGACTCTG AGGCCTGGAGTACCAACACAGGCACCTATTAATGCACAGATGCTGGCCCAGAGACAGAGG GAAATCCTGAACCAGCATCTTCGACAGAGACAAATGCATCAGCAACAGCAAGTTCAGCAA CGAACTTTGATGATGAGAGGACAAGGGTTGAATATGACACCAAGCATGGTGGCTCCTAGT GGTATGCCAGCAACTATGAGCAACCCTCGGATTCCCCAGGCAAATGCACAGCAGTTTCCA TTTCCTCCAAACTACGGAATAAGTCAGCAACCTGATCCAGGCTTTACTGGGGCTACGACT CCCCAGAGCCCACTTATGTCACCCCGAATGGCACATACACAGAGTCCCATGATGCAACAG TCTCAGGCCAACCCAGCCTATCAGGCCCCCTCCGACATAAATGGATGGGCGCAGGGGAAC ATGGGCGGAAACAGCATGTTTTCCCAGCAGTCCCCACCACACTTTGGGCAGCAAGCAAAC ACCAGCATGTACAGTAACAACATGAACATCAATGTGTCCATGGCGACCAACACAGGTGGC ATGAGCAGCATGAACCAGATGACAGGACAGATCAGCATGACCTCAGTGACCTCCGTGCCT ACGTCAGGGCTGTCCTCCATGGGTCCCGAGCAGGTTAATGATCCTGCTCTGAGGGGAGGC AACCTGTTCCCAAACCAGCTGCCTGGAATGGATATGATTAAGCAGGAGGGAGACACAACA CGGAAATATTGCTGA PF00989 PAS PF07469 DUF1518 PF08815 Nuc_rec_co-act PF08832 SRC-1 component organelle component membrane-bound organelle component intracellular membrane-bound organelle component nucleus function protein binding function signal transducer activity function transcription factor binding function transcription regulator activity function transcription cofactor activity function transcription coactivator activity function binding process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent process cellular process process cell communication process signal transduction process regulation of biological process process regulation of physiological process process regulation of metabolism BE0000078 Retinoic acid receptor RXR-beta Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Retinoic acid receptor RXR-beta Cell cycle control, cell division, chromosome partitioning Nuclear hormone receptor. Involved in the retinoic acid response pathway. Binds 9-cis retinoic acid (9C-RA) RXRB 6p21.3 Nucleus None 8.24 56922.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:10478 GenAtlas RXRB GeneCards RXRB GenBank Gene Database X63522 GenBank Protein Database 30448 IUPHAR 611 Guide to Pharmacology 108 UniProtKB P28702 UniProt Accession RXRB_HUMAN Retinoid X receptor beta >Retinoic acid receptor RXR-beta MSWAARPPFLPQRHAAGQCGPVGVRKEMHCGVASRWRRRRPWLDPAAAAAAAVAGGEQQT PEPEPGEAGRDGMGDSGRDSRSPDSSSPNPLPQGVPPPSPPGPPLPPSTAPSLGGSGAPP PPPMPPPPLGSPFPVISSSMGSPGLPPPAPPGFSGPVSSPQINSTVSLPGGGSGPPEDVK PPVLGVRGLHCPPPPGGPGAGKRLCAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLTYS CRDNKDCTVDKRQRNRCQYCRYQKCLATGMKREAVQEERQRGKDKDGDGEGAGGAPEEMP VDRILEAELAVEQKSDQGVEGPGGTGGSGSSPNDPVTNICQAADKQLFTLVEWAKRIPHF SSLPLDDQVILLRAGWNELLIASFSHRSIDVRDGILLATGLHVHRNSAHSAGVGAIFDRV LTELVSKMRDMRMDKTELGCLRAIILFNPDAKGLSNPSEVEVLREKVYASLETYCKQKYP EQQGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQLA >1602 bp ATGTCTTGGGCCGCTCGCCCGCCCTTCCTCCCTCAGCGGCATGCCGCAGGGCAGTGTGGG CCGGTGGGGGTGCGAAAAGAAATGCATTGTGGGGTCGCGTCCCGGTGGCGGCGGCGACGG CCCTGGCTGGATCCCGCAGCGGCGGCGGCGGCGGCGGTGGCAGGCGGAGAACAACAAACC CCGGAGCCGGAGCCAGGGGAGGCTGGACGGGACGGGATGGGCGACAGCGGGCGGGACTCC CGAAGCCCAGACAGCTCCTCCCCAAATCCCCTTCCCCAGGGAGTCCCTCCCCCTTCTCCT CCTGGGCCACCCCTACCCCCTTCAACAGCTCCATCCCTTGGAGGCTCTGGGGCCCCACCC CCACCCCCGATGCCACCACCCCCACTGGGCTCTCCCTTTCCAGTCATCAGTTCTTCCATG GGGTCCCCTGGTCTGCCCCCTCCAGCTCCCCCAGGATTCTCCGGGCCTGTCAGCAGCCCC CAGATTAACTCAACAGTGTCACTCCCTGGGGGTGGGTCTGGCCCCCCTGAAGATGTGAAG CCACCAGTCTTAGGGGTCCGGGGCCTGCACTGTCCACCCCCTCCAGGTGGCCCTGGGGCT GGCAAACGGCTATGTGCAATCTGCGGGGACAGAAGCTCAGGCAAACACTACGGGGTTTAC AGCTGTGAGGGTTGCAAGGGCTTCTTCAAACGCACCATCCGCAAAGACCTTACATACTCT TGCCGGGACAACAAAGACTGCACAGTGGACAAGCGCCAGCGGAACCGCTGTCAGTACTGC CGCTATCAGAAGTGCCTGGCCACTGGCATGAAGAGGGAGGCGGTACAGGAGGAGCGTCAG CGGGGAAAGGACAAGGATGGGGATGGGGAGGGGGCTGGGGGAGCCCCCGAGGAGATGCCT GTGGACAGGATCCTGGAGGCAGAGCTTGCTGTGGAACAGAAGAGTGACCAGGGCGTTGAG GGTCCTGGGGGAACCGGGGGTAGCGGCAGCAGCCCAAATGACCCTGTGACTAACATCTGT CAGGCAGCTGACAAACAGCTATTCACGCTTGTTGAGTGGGCGAAGAGGATCCCACACTTT TCCTCCTTGCCTCTGGATGATCAGGTCATATTGCTGCGGGCAGGCTGGAATGAACTCCTC ATTGCCTCCTTTTCACACCGATCCATTGATGTTCGAGATGGCATCCTCCTTGCCACAGGT CTTCACGTGCACCGCAACTCAGCCCATTCAGCAGGAGTAGGAGCCATCTTTGATCGGGTG CTGACAGAGCTAGTGTCCAAAATGCGTGACATGAGGATGGACAAGACAGAGCTTGGCTGC CTGAGGGCAATCATTCTGTTTAATCCAGATGCCAAGGGCCTCTCCAACCCTAGTGAGGTG GAGGTCCTGCGGGAGAAAGTGTATGCATCACTGGAGACCTACTGCAAACAGAAGTACCCT GAGCAGCAGGGACGGTTTGCCAAGCTGCTGCTACGTCTTCCTGCCCTCCGGTCCATTGGC CTTAAGTGTCTAGAGCATCTGTTTTTCTTCAAGCTCATTGGTGACACCCCCATCGACACC TTCCTCATGGAGATGCTTGAGGCTCCCCATCAACTGGCCTGA PF00104 Hormone_recep PF00105 zf-C4 component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function transcription factor activity function steroid binding function ligand-dependent nuclear receptor activity function DNA binding function binding function signal transducer activity function receptor activity function nucleic acid binding function steroid hormone receptor activity process regulation of biological process process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent BE0003781 Oxysterols receptor LXR-alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Oxysterols receptor LXR-alpha Involved in sequence-specific DNA binding Orphan receptor. Interaction with RXR shifts RXR from its role as a silent DNA-binding partner to an active ligand- binding subunit in mediating retinoid responses through target genes defined by LXRES. LXRES are DR4-type response elements characterized by direct repeats of two similar hexanuclotide half- sites spaced by four nucleotides. Plays an important role in the regulation of cholesterol homeostasis NR1H3 11p11.2 Nucleus (Potential) None 7.72 50395.3 Human HUGO Gene Nomenclature Committee (HGNC) GNC:7966 GeneCards NR1H3 GenBank Gene Database U22662 GenBank Protein Database 726513 UniProtKB Q13133 UniProt Accession NR1H3_HUMAN Liver X receptor alpha Nuclear orphan receptor LXR-alpha Nuclear receptor subfamily 1 group H member 3 >Oxysterols receptor LXR-alpha MSLWLGAPVPDIPPDSAVELWKPGAQDASSQAQGGSSCILREEARMPHSAGGTAGVGLEA AEPTALLTRAEPPSEPTEIRPQKRKKGPAPKMLGNELCSVCGDKASGFHYNVLSCEGCKG FFRRSVIKGAHYICHSGGHCPMDTYMRRKCQECRLRKCRQAGMREECVLSEEQIRLKKLK RQEEEQAHATSLPPRASSPPQILPQLSPEQLGMIEKLVAAQQQCNRRSFSDRLRVTPWPM APDPHSREARQQRFAHFTELAIVSVQEIVDFAKQLPGFLQLSREDQIALLKTSAIEVMLL ETSRRYNPGSESITFLKDFSYNREDFAKAGLQVEFINPIFEFSRAMNELQLNDAEFALLI AISIFSADRPNVQDQLQVERLQHTYVEALHAYVSIHHPHDRLMFPRMLMKLVSLRTLSSV HSEQVFALRLQDKKLPPLLSEIWDVHE >1344 bp ATGTCCTTGTGGCTGGGGGCCCCTGTGCCTGACATTCCTCCTGACTCTGCGGTGGAGCTG TGGAAGCCAGGCGCACAGGATGCAAGCAGCCAGGCCCAGGGAGGCAGCAGCTGCATCCTC AGAGAGGAAGCCAGGATGCCCCACTCTGCTGGGGGTACTGCAGGGGTGGGGCTGGAGGCT GCAGAGCCCACAGCCCTGCTCACCAGGGCAGAGCCCCCTTCAGAACCCACAGAGATCCGT CCACAAAAGCGGAAAAAGGGGCCAGCCCCCAAAATGCTGGGGAACGAGCTATGCAGCGTG TGTGGGGACAAGGCCTCGGGCTTCCACTACAATGTTCTGAGCTGCGAGGGCTGCAAGGGA TTCTTCCGCCGCAGCGTCATCAAGGGAGCGCACTACATCTGCCACAGTGGCGGCCACTGC CCCATGGACACCTACATGCGTCGCAAGTGCCAGGAGTGTCGGCTTCGCAAATGCCGTCAG GCTGGCATGCGGGAGGAGTGTGTCCTGTCAGAAGAACAGATCCGCCTGAAGAAACTGAAG CGGCAAGAGGAGGAACAGGCTCATGCCACATCCTTGCCCCCCAGGCGTTCCTCACCCCCC CAAATCCTGCCCCAGCTCAGCCCGGAACAACTGGGCATGATCGAGAAGCTCGTCGCTGCC CAGCAACAGTGTAACCGGCGCTCCTTTTCTGACCGGCTTCGAGTCACGCCTTGGCCCATG GCACCAGATCCCCATAGCCGGGAGGCCCGTCAGCAGCGCTTTGCCCACTTCACTGAGCTG GCCATCGTCTCTGTGCAGGAGATAGTTGACTTTGCTAAACAGCTACCCGGCTTCCTGCAG CTCAGCCGGGAGGACCAGATTGCCCTGCTGAAGACCTCTGCGATCGAGGTGATGCTTCTG GAGACATCTCGGAGGTACAACCCTGGGAGTGAGAGTATCACCTTCCTCAAGGATTTCAGT TATAACCGGGAAGACTTTGCCAAAGCAGGGCTGCAAGTGGAATTCATCAACCCCATCTTC GAGTTCTCCAGGGCCATGAATGAGCTGCAACTCAATGATGCCGAGTTTGCCTTGCTCATT GCTATCAGCATCTTCTCTGCAGACCGGCCCAACGTGCAGGACCAGCTCCAGGTGGAGAGG CTGCAGCACACATATGTGGAAGCCCTGCATGCCTACGTCTCCATCCACCATCCCCATGAC CGACTGATGTTCCCACGGATGCTAATGAAACTGGTGAGCCTCCGGACCCTGAGCAGCGTC CACTCAGAGCAAGTGTTTGCACTGCGTCTGCAGGACAAAAAGCTCCCACCGCTGCTCTCT GAGATCTGGGATGTGCACGAATGA PF00104 Hormone_recep PF00105 zf-C4 component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function receptor activity function nucleic acid binding function steroid hormone receptor activity function transcription factor activity function thyroid hormone receptor activity function ligand-dependent nuclear receptor activity function DNA binding function binding function signal transducer activity process regulation of transcription process regulation of transcription, DNA-dependent process regulation of biological process process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism "
drug:(2E,4E)-11-METHOXY-3,7,11-TRIMETHYLDODECA-2,4-DIENOIC ACIDrdfs:label"(2E,4E)-11-METHOXY-3,7,11-TRIMETHYLDODECA-2,4-DIENOIC ACID"
drug:(2E,4E)-11-METHOXY-3,7,11-TRIMETHYLDODECA-2,4-DIENOIC ACIDrdf:typedrugbank:drugs
drug:(2E,4E)-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC ACIDdrugbank:description" experimental This compound belongs to the acetophenones. These are organic compounds containing the acetophenone structure. Acetophenones Organic Compounds Benzenoids Benzene and Substituted Derivatives Acetophenones Carbocyclic Fatty Acids Medium-chain Keto Acids and Derivatives Benzoyl Derivatives Unsaturated Fatty Acids Enones Acryloyl Compounds Carboxylic Acids Enolates Polyamines Enols benzoyl acryloyl-group enone ketone enol carboxylic acid carboxylic acid derivative polyamine enolate carbonyl group logP 1.63 ALOGPS logS -2.8 ALOGPS Water Solubility 3.59e-01 g/l ALOGPS logP 1.72 ChemAxon IUPAC Name (2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid ChemAxon Traditional IUPAC Name (2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid ChemAxon Molecular Weight 218.2054 ChemAxon Monoisotopic Weight 218.057908808 ChemAxon SMILES OC(=O)C(\O)=C/C=C/C(=O)C1=CC=CC=C1 ChemAxon Molecular Formula C12H10O4 ChemAxon InChI InChI=1S/C12H10O4/c13-10(9-5-2-1-3-6-9)7-4-8-11(14)12(15)16/h1-8,14H,(H,15,16)/b7-4+,11-8+ ChemAxon InChIKey InChIKey=RDRDHXDYMGUCKE-VCABWLAWSA-N ChemAxon Polar Surface Area (PSA) 74.6 ChemAxon Refractivity 60.71 ChemAxon Polarizability 21.71 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 3.48 ChemAxon pKa (strongest basic) -6.1 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5462192 PubChem Substance 99444386 ChemSpider 16188846 PDB HPZ BE0003969 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase Burkholderia xenovorans (strain LB400) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase Involved in 2,6-dioxo-6-phenylhexa-3-enoate hydrolase a Catalyzes an unusual C-C bond hydrolysis of 2-hydroxy-6- oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) to produce benzoic acid and 2-hydroxy-2,4-pentadienoic acid (HPD) bphD None 6.61 32029.4 Burkholderia xenovorans (strain LB400) GeneCards bphD GenBank Gene Database X66123 GenBank Protein Database 397886 UniProtKB P47229 UniProt Accession BPHD_BURXL 2,6-dioxo-6-phenylhexa-3-enoate hydrolase HOPDA hydrolase >2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase MTALTESSTSKFVKINEKGFSDFNIHYNEAGNGETVIMLHGGGPGAGGWSNYYRNVGPFV DAGYRVILKDSPGFNKSDAVVMDEQRGLVNARAVKGLMDALDIDRAHLVGNSMGGATALN FALEYPDRIGKLILMGPGGLGPSMFAPMPMEGIKLLFKLYAEPSYETLKQMLQVFLYDQS LITEELLQGRWEAIQRQPEHLKNFLISAQKAPLSTWDVTARLGEIKAKTFITWGRDDRFV PLDHGLKLLWNIDDARLHVFSKCGHWAQWEHADEFNRLVIDFLRHA >861 bp ATGACCGCACTCACCGAAAGTTCTACCAGCAAGTTCGTGAAAATAAATGAAAAAGGTTTT TCCGATTTCAATATTCACTACAACGAGGCGGGTAACGGCGAAACCGTCATCATGCTGCAT GGCGGGGGCCCCGGCGCTGGCGGCTGGAGTAACTACTACCGCAACGTCGGACCGTTTGTC GACGCCGGTTACCGGGTGATCCTGAAGGATTCGCCCGGCTTCAACAAGTCGGACGCGGTG GTGATGGACGAGCAGCGCGGCCTGGTCAACGCCCGTGCCGTCAAAGGGCTGATGGATGCG CTGGACATCGACCGGGCGCACCTGGTCGGCAACTCGATGGGGGGCGCCACGGCGCTGAAC TTCGCGCTCGAATACCCCGACCGCATCGGCAAACTGATCCTCATGGGGCCCGGCGGCCTG GGCCCCAGCATGTTCGCGCCGATGCCGATGGAAGGCATCAAGCTGCTGTTCAAGCTGTAT GCCGAGCCGTCCTACGAGACGCTGAAACAGATGCTTCAGGTGTTTTTGTACGACCAGTCC CTTATCACCGAGGAGTTGCTGCAGGGCCGCTGGGAAGCCATTCAGCGCCAACCGGAACAC CTGAAGAACTTCCTCATCAGCGCACAAAAGGCGCCGCTTTCAACCTGGGATGTGACTGCC AGACTTGGAGAAATCAAGGCCAAGACATTCATTACCTGGGGGCGCGATGATCGCTTCGTT CCCCTTGACCACGGTTTGAAGCTGCTCTGGAACATCGACGACGCGCGTTTGCACGTTTTC TCCAAGTGCGGCCATTGGGCGCAATGGGAGCATGCCGATGAATTCAACCGCCTGGTGATT GACTTCCTGCGGCACGCGTAA PF00561 Abhydrolase_1 function catalytic activity "
drug:(2E,4E)-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC ACIDrdfs:label"(2E,4E)-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC ACID"
drug:(2E,4E)-2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOIC ACIDrdf:typedrugbank:drugs
drug:(2E,4R,5S)-2,3,4,5-TETRAHYDROXY-6-(PALMITOYLOXY)HEX-2-ENOIC ACIDdrugbank:description" experimental This compound belongs to the fatty acid esters. These are carboxylic ester derivatives of a fatty acid. Fatty Acid Esters Organic Compounds Lipids Fatty Acid Esters Dicarboxylic Acids and Derivatives Enones Secondary Alcohols Carboxylic Acid Esters Enediols 1,2-Diols Ethers Carboxylic Acids Polyamines Enolates dicarboxylic acid derivative enone polyol carboxylic acid ester secondary alcohol enediol 1,2-diol ether polyamine enolate carboxylic acid derivative carboxylic acid alcohol logP 4.39 ALOGPS logS -4.6 ALOGPS Water Solubility 1.18e-02 g/l ALOGPS logP 4.11 ChemAxon IUPAC Name (2Z,4R,5S)-6-(hexadecanoyloxy)-2,3,4,5-tetrahydroxyhex-2-enoic acid ChemAxon Traditional IUPAC Name (2Z,4R,5S)-6-(hexadecanoyloxy)-2,3,4,5-tetrahydroxyhex-2-enoic acid ChemAxon Molecular Weight 432.5482 ChemAxon Monoisotopic Weight 432.272318256 ChemAxon SMILES [H][C@](O)(COC(=O)CCCCCCCCCCCCCCC)[C@@]([H])(O)C(\O)=C(\O)C(O)=O ChemAxon Molecular Formula C22H40O8 ChemAxon InChI InChI=1S/C22H40O8/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-18(24)30-16-17(23)19(25)20(26)21(27)22(28)29/h17,19,23,25-27H,2-16H2,1H3,(H,28,29)/b21-20-/t17-,19+/m0/s1 ChemAxon InChIKey InChIKey=XWTWKBKNEMLBKW-KCWNHAIFSA-N ChemAxon Polar Surface Area (PSA) 144.52 ChemAxon Refractivity 114.12 ChemAxon Polarizability 49.75 ChemAxon Rotatable Bond Count 20 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 3.03 ChemAxon pKa (strongest basic) -3.6 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937151 PubChem Substance 99444909 PDB PVC BE0001361 Hyaluronate lyase Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Hyaluronate lyase Involved in hyaluronidase activity Cleaves hyaluronate chains at a beta-D-GalNAc- (1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D- glucosamine SP_0314 Cell wall; peptidoglycan-anchor (Potential) None 5.97 120772.0 Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) GenBank Gene Database AE005672 GenBank Protein Database 14971788 UniProtKB Q54873 UniProt Accession HYSA_STRPN EC 4.2.2.1 Hyaluronate lyase precursor Hyaluronidase HYase >Hyaluronate lyase precursor MQTKTKKLIVSLSSLVLSGFLLNHYMTIGAEETTTNTIQQSQKEVQYQQRDTKNLVENGD FGQTEDGSSPWTGSKAQGWSAWVDQKNSADASTRVIEAKDGAITISSHEKLRAALHRMVP IEAKKKYKLRFKIKTDNKIGIAKVRIIEESGKDKRLWNSATTSGTKDWQTIEADYSPTLD VDKIKLELFYETGTGTVSFKDIELVEVADQLSEDSQTDKQLEEKIDLPIGKKHVFSLADY TYKVENPDVASVKNGILEPLKEGTTNVIVSKDGKEVKKIPLKILASVKDAYTDRLDDWNG IIAGNQYYDSKNEQMAKLNQELEGKVADSLSSISSQADRTYLWEKFSNYKTSANLTATYR KLEEMAKQVTNPSSRYYQDETVVRTVRDSMEWMHKHVYNSEKSIVGNWWDYEIGTPRAIN NTLSLMKEYFSDEEIKKYTDVIEKFVPDPEHFRKTTDNPFKALGGNLVDMGRVKVIAGLL RKDDQEISSTIRSIEQVFKLVDQGEGFYQDGSYIDHTNVAYTGAYGNVLIDGLSQLLPVI QKTKNPIDKDKMQTMYHWIDKSFAPLLVNGELMDMSRGRSISRANSEGHVAAVEVLRGIH RIADMSEGETKQCLQSLVKTIVQSDSYYDVFKNLKTYKDISLMQSLLSDAGVASVPRPSY LSAFNKMDKTAMYNAEKGFGFGLSLFSSRTLNYEHMNKENKRGWYTSDGMFYLYNGDLSH YSDGYWPTVNPYKMPGTTETDAKRADSDTGKVLPSAFVGTSKLDDANATATMDFTNWNQT LTAHKSWFMLKDKIAFLGSNIQNTSTDTAATTIDQRKLESGNPYKVYVNDKEASLTEQEK DYPETQSVFLESFDSKKNIGYFFFKKSSISMSKALQKGAWKDINEGQSDKEVENEFLTIS QAHKQNRDSYGYMLIPNVDRATFNQMIKELESSLIENNETLQSVYDAKQGVWGIVKYDDS VSTISNQFQVLKRGVYTIRKEGDEYKIAYYNPETQESAPDQEVFKKLEQAAQPQVQNSKE KEKSEEEKNHSDQKNLPQTGEGQSILASLGFLLLGAFYLFRRGKNN >3201 bp ATGCAAACAAAAACAAAGAAGCTCATTGTGAGTTTGTCTTCACTTGTTTTATCAGGATTT TTATTAAACCATTATATGACAATTGGAGCGGAAGAAACGACTACGAATACCATTCAGCAA AGCCAGAAGGAAGTTCAGTATCAGCAAAGGGATACAAAAAATTTAGTTGAAAATGGTGAT TTTGGTCAGACGGAGGACGGAAGCAGTCCGTGGACAGGAAGCAAAGCTCAGGGGTGGTCA GCTTGGGTAGACCAGAAGAATAGTGCAGATGCCTCAACTCGAGTCATTGAGGCTAAGGAT GGGGCTATCACTATCTCAAGCCATGAGAAATTAAGGGCAGCGCTTCACCGTATGGTTCCT ATTGAAGCTAAGAAAAAGTATAAACTGCGTTTCAAGATTAAAACAGATAATAAAATCGGG ATTGCCAAAGTTCGTATCATTGAGGAAAGTGGTAAGGACAAGCGATTGTGGAATTCTGCA ACGACGTCAGGAACAAAGGACTGGCAGACCATTGAAGCAGACTATAGCCCGACTTTAGAT GTTGATAAAATCAAGCTGGAGTTATTCTATGAAACAGGAACTGGGACTGTTTCCTTTAAG GATATTGAGCTGGTAGAGGTAGCAGACCAGCTTTCTGAGGATTCTCAAACAGATAAACAG CTTGAGGAAAAGATTGATTTACCAATTGGAAAAAAACATGTTTTTTCTCTTGCGGACTAT ACTTATAAGGTAGAAAATCCTGACGTTGCTTCAGTCAAAAATGGAATTTTAGAACCTCTT AAGGAAGGGACAACCAATGTCATTGTCAGTAAAGATGGCAAGGAAGTGAAAAAGATTCCT TTGAAGATTCTGGCCTCTGTTAAGGATGCATACACAGACCGTTTGGATGACTGGAATGGC ATCATCGCTGGGAATCAATACTATGATTCTAAAAATGAACAGATGGCCAAATTAAACCAG GAATTGGAAGGAAAGGTAGCTGATAGCCTATCCAGTATTTCAAGTCAGGCGGACCGCACC TATTTGTGGGAAAAATTTTCAAATTATAAAACGTCTGCAAATCTGACTGCCACTTATCGG AAATTGGAGGAGATGGCCAAGCAAGTGACCAATCCTTCTTCTCGTTATTATCAAGATGAA ACTGTCGTTCGAACAGTCAGGGATTCCATGGAATGGATGCATAAACATGTCTACAATAGT GAAAAGAGCATTGTTGGGAACTGGTGGGATTATGAAATCGGTACACCTCGTGCCATCAAC AATACCTTGTCTCTGATGAAAGAATACTTCTCTGATGAGGAAATTAAAAAATATACAGAT GTGATTGAAAAATTTGTACCAGATCCCGAACATTTCCGAAAGACGACTGATAACCCATTC AAGGCTCTAGGTGGAAACTTAGTTGATATGGGAAGGGTAAAAGTAATAGCTGGTTTACTG CGTAAGGATGATCAAGAAATTTCTTCTACCATTCGCTCGATTGAGCAAGTGTTCAAGTTG GTAGACCAAGGTGAAGGTTTTTATCAAGATGGATCCTATATCGACCACACCAATGTTGCC TATACGGGTGCTTATGGGAATGTTTTGATTGATGGCCTGTCTCAACTGTTGCCAGTCATT CAAAAGACCAAGAATCCAATCGATAAAGATAAAATGCAAACCATGTACCACTGGATTGAT AAATCGTTTGCTCCTTTGCTGGTGAATGGAGAGTTGATGGATATGAGTCGTGGACGCTCG ATCAGTCGTGCAAATAGCGAGGGGCACGTGGCCGCAGTAGAAGTACTAAGAGGGATTCAC CGAATAGCGGATATGTCTGAAGGAGAAACCAAACAATGTTTGCAGAGTCTTGTGAAGACC ATTGTTCAATCGGATAGTTATTATGATGTCTTTAAGAATTTGAAGACTTATAAGGATATC AGTTTGATGCAATCCTTGTTAAGTGATGCAGGAGTCGCAAGTGTTCCAAGACCAAGTTAC CTATCTGCCTTTAACAAGATGGATAAAACAGCCATGTACAATGCAGAGAAAGGGTTTGGA TTTGGCTTGTCACTCTTTTCCAGTCGTACCTTGAATTACGAACACATGAACAAGGAAAAT AAACGTGGTTGGTATACGAGTGATGGGATGTTCTATCTTTACAATGGCGATTTGAGTCAC TATAGCGATGGCTACTGGCCAACAGTTAATCCATATAAGATGCCTGGTACAACAGAGACG GATGCTAAGAGAGCGGATAGCGATACAGGTAAAGTTTTACCGTCTGCTTTCGTTGGAACG AGCAAACTAGATGATGCCAATGCGACAGCAACCATGGATTTCACCAACTGGAATCAAACA TTGACTGCTCATAAGAGCTGGTTTATGCTAAAGGATAAGATCGCCTTTTTAGGAAGCAAT ATCCAAAACACTTCAACAGATACTGCTGCAACTACAATTGACCAGAGAAAACTGGAATCA GGTAATCCATATAAAGTCTATGTCAATGATAAAGAAGCCTCCCTTACAGAACAAGAAAAG GATTATCCTGAAACCCAAAGTGTCTTTTTAGAATCGTTCGATTCGAAAAAGAATATTGGT TACTTTTTCTTTAAGAAGAGTTCAATCAGTATGAGTAAGGCTTTGCAAAAGGGAGCCTGG AAGGATATCAATGAAGGACAGTCAGACAAGGAAGTTGAAAATGAATTTCTTACGATTAGT CAGGCTCATAAGCAAAATAGAGATTCTTATGGCTATATGCTCATTCCTAACGTGGATCGT GCCACCTTCAATCAAATGATAAAAGAGTTAGAAAGTAGCCTCATCGAAAATAACGAAACC CTTCAGTCTGTTTATGATGCTAAACAAGGAGTTTGGGGCATTGTGAAATATGATGATTCT GTCTCTACTATTTCCAACCAATTCCAAGTTTTGAAACGTGGAGTCTATACCATTCGAAAA GAAGGGGATGAATATAAGATTGCCTACTATAATCCTGAAACCCAGGAATCAGCTCCAGAT CAGGAAGTCTTTAAAAAGCTAGAGCAAGCAGCTCAGCCACAAGTACAGAATTCAAAAGAA AAGGAAAAATCTGAAGAGGAAAAGAACCATTCGGATCAAAAGAATCTCCCTCAGACAGGA GAAGGTCAGTCAATCTTGGCAAGTCTAGGGTTCTTGCTACTTGGGGCATTTTATCTATTC CGTAGAGGAAAGAACAACTAA PF02018 CBM_4_9 PF00746 Gram_pos_anchor PF02278 Lyase_8 PF02884 Lyase_8_C PF08124 Lyase_8_N component cell surface component cell component extracellular region function carbon-oxygen lyase activity, acting on polysaccharides function catalytic activity function lyase activity function carbon-oxygen lyase activity "
drug:(2E,4R,5S)-2,3,4,5-TETRAHYDROXY-6-(PALMITOYLOXY)HEX-2-ENOIC ACIDrdfs:label"(2E,4R,5S)-2,3,4,5-TETRAHYDROXY-6-(PALMITOYLOXY)HEX-2-ENOIC ACID"
drug:(2E,4R,5S)-2,3,4,5-TETRAHYDROXY-6-(PALMITOYLOXY)HEX-2-ENOIC ACIDrdf:typedrugbank:drugs
drug:(2R)-({4-[AMINO(IMINO)METHYL]PHENYL}AMINO){5-ETHOXY-2-FLUORO-3-[(3R)-TETRAHYDROFURAN-3-YLOXY]PHENYL}ACETICACIDdrugbank:description" experimental This compound belongs to the phenylacetic acid derivatives. These are compounds containing a phenylacetic acid moiety, which consists of a phenyl group substituted at the second position by an acetic acid. Phenylacetic Acid Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenylacetic Acid Derivatives Alpha Amino Acids and Derivatives Phenol Ethers Alkyl Aryl Ethers Fluorobenzenes Aryl Fluorides Oxolanes Tetrahydrofurans Enolates Polyamines Secondary Amines Carboxylic Acids Carboxamidines Organofluorides phenol ether alkyl aryl ether fluorobenzene aryl fluoride aryl halide tetrahydrofuran oxolane enolate amidine polyamine secondary amine ether carboxylic acid amidine carboxylic acid derivative carboxylic acid amine organonitrogen compound organofluoride organohalogen logP 2.01 ALOGPS logS -4.2 ALOGPS Water Solubility 2.96e-02 g/l ALOGPS logP 0.22 ChemAxon IUPAC Name (2R)-2-[(4-carbamimidoylphenyl)amino]-2-{5-ethoxy-2-fluoro-3-[(3R)-oxolan-3-yloxy]phenyl}acetic acid ChemAxon Traditional IUPAC Name (R)-[(4-carbamimidoylphenyl)amino]({5-ethoxy-2-fluoro-3-[(3R)-oxolan-3-yloxy]phenyl})acetic acid ChemAxon Molecular Weight 417.4308 ChemAxon Monoisotopic Weight 417.169999098 ChemAxon SMILES CCOC1=CC([C@@H](NC2=CC=C(C=C2)C(N)=N)C(O)=O)=C(F)C(O[C@@H]2CCOC2)=C1 ChemAxon Molecular Formula C21H24FN3O5 ChemAxon InChI InChI=1S/C21H24FN3O5/c1-2-29-15-9-16(18(22)17(10-15)30-14-7-8-28-11-14)19(21(26)27)25-13-5-3-12(4-6-13)20(23)24/h3-6,9-10,14,19,25H,2,7-8,11H2,1H3,(H3,23,24)(H,26,27)/t14-,19-/m1/s1 ChemAxon InChIKey InChIKey=PGYOHIAQCFZQDK-AUUYWEPGSA-N ChemAxon Polar Surface Area (PSA) 126.89 ChemAxon Refractivity 119.87 ChemAxon Polarizability 41.82 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 8 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 3.78 ChemAxon pKa (strongest basic) 12.52 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 6852220 PubChem Substance 46505729 BindingDB 13590 PDB 346 BE0000333 Coagulation factor VII Human unknown Coagulation factor VII Involved in calcium ion binding Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium F7 13q34 Cytoplasmic None 7.23 51594.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3544 GenAtlas F7 GeneCards F7 GenBank Gene Database M13232 GenBank Protein Database 182801 UniProtKB P08709 UniProt Accession FA7_HUMAN Coagulation factor VII precursor EC 3.4.21.21 Eptacog alfa Proconvertin Serum prothrombin conversion accelerator SPCA >Coagulation factor VII precursor MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRR ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGS CKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSL LADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGG TLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTN HDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVL NVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTG IVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP >1401 bp ATGGTCTCCCAGGCCCTCAGGCTCCTCTGCCTTCTGCTTGGGCTTCAGGGCTGCCTGGCT GCAGGCGGGGTCGCTAAGGCCTCAGGAGGAGAAACACGGGACATGCCGTGGAAGCCGGGG CCTCACAGAGTCTTCGTAACCCAGGAGGAAGCCCACGGCGTCCTGCACCGGCGCCGGCGC GCCAACGCGTTCCTGGAGGAGCTGCGGCCGGGCTCCCTGGAGAGGGAGTGCAAGGAGGAG CAGTGCTCCTTCGAGGAGGCCCGGGAGATCTTCAAGGACGCGGAGAGGACGAAGCTGTTC TGGATTTCTTACAGTGATGGGGACCAGTGTGCCTCAAGTCCATGCCAGAATGGGGGCTCC TGCAAGGACCAGCTCCAGTCCTATATCTGCTTCTGCCTCCCTGCCTTCGAGGGCCGGAAC TGTGAGACGCACAAGGATGACCAGCTGATCTGTGTGAACGAGAACGGCGGCTGTGAGCAG TACTGCAGTGACCACACGGGCACCAAGCGCTCCTGTCGGTGCCACGAGGGGTACTCTCTG CTGGCAGACGGGGTGTCCTGCACACCCACAGTTGAATATCCATGTGGAAAAATACCTATT CTAGAAAAAAGAAATGCCAGCAAACCCCAAGGCCGAATTGTGGGGGGCAAGGTGTGCCCC AAAGGGGAGTGTCCATGGCAGGTCCTGTTGTTGGTGAATGGAGCTCAGTTGTGTGGGGGG ACCCTGATCAACACCATCTGGGTGGTCTCCGCGGCCCACTGTTTCGACAAAATCAAGAAC TGGAGGAACCTGATCGCGGTGCTGGGCGAGCACGACCTCAGCGAGCACGACGGGGATGAG CAGAGCCGGCGGGTGGCGCAGGTCATCATCCCCAGCACGTACGTCCCGGGCACCACCAAC CACGACATCGCGCTGCTCCGCCTGCACCAGCCCGTGGTCCTCACTGACCATGTGGTGCCC CTCTGCCTGCCCGAACGGACGTTCTCTGAGAGGACGCTGGCCTTCGTGCGCTTCTCATTG GTCAGCGGCTGGGGCCAGCTGCTGGACCGTGGCGCCACGGCCCTGGAGCTCATGGTGCTC AACGTGCCCCGGCTGATGACCCAGGACTGCCTGCAGCAGTCACGGAAGGTGGGAGACTCC CCAAATATCACGGAGTACATGTTCTGTGCCGGCTACTCGGATGGCAGCAAGGACTCCTGC AAGGGGGACAGTGGAGGCCCACATGCCACCCACTACCGGGGCACGTGGTACCTGACGGGC ATCGTCAGCTGGGGCCAGGGCTGCGCAACCGTGGGCCACTTTGGGGTGTACACCAGGGTC TCCCAGTACATCGAGTGGCTGCAAAAGCTCATGCGCTCAGAGCCACGCCCAGGAGTCCTC CTGCGAGCCCCATTTCCCTAG PF00008 EGF PF00594 Gla PF00089 Trypsin component extracellular region function endopeptidase activity function ion binding function serine-type endopeptidase activity function cation binding function binding function catalytic activity function calcium ion binding function hydrolase activity function peptidase activity process macromolecule metabolism process proteolysis process protein metabolism process cellular protein metabolism process organismal physiological process process regulation of body fluids process physiological process process hemostasis process blood coagulation process metabolism "
drug:(2R)-({4-[AMINO(IMINO)METHYL]PHENYL}AMINO){5-ETHOXY-2-FLUORO-3-[(3R)-TETRAHYDROFURAN-3-YLOXY]PHENYL}ACETICACIDrdfs:label"(2R)-({4-[AMINO(IMINO)METHYL]PHENYL}AMINO){5-ETHOXY-2-FLUORO-3-[(3R)-TETRAHYDROFURAN-3-YLOXY]PHENYL}ACETICACID"
drug:(2R)-({4-[AMINO(IMINO)METHYL]PHENYL}AMINO){5-ETHOXY-2-FLUORO-3-[(3R)-TETRAHYDROFURAN-3-YLOXY]PHENYL}ACETICACIDrdf:typedrugbank:drugs
drug:(2R)-1-(2,6-dimethylphenoxy)propan-2-aminedrugbank:description" experimental This compound belongs to the phenol ethers. These are aromatic compounds containing an ether group substituted with a benzene ring. Phenol Ethers Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenol Ethers Toluenes Alkyl Aryl Ethers Polyamines Monoalkylamines alkyl aryl ether toluene polyamine ether amine primary amine primary aliphatic amine organonitrogen compound logP 2.17 ALOGPS logS -2.5 ALOGPS Water Solubility 5.38e-01 g/l ALOGPS logP 2.46 ChemAxon IUPAC Name 2-[(2R)-2-aminopropoxy]-1,3-dimethylbenzene ChemAxon Traditional IUPAC Name mexiletine ChemAxon Molecular Weight 179.2588 ChemAxon Monoisotopic Weight 179.131014171 ChemAxon SMILES [H][C@](C)(N)COC1=C(C)C=CC=C1C ChemAxon Molecular Formula C11H17NO ChemAxon InChI InChI=1S/C11H17NO/c1-8-5-4-6-9(2)11(8)13-7-10(3)12/h4-6,10H,7,12H2,1-3H3/t10-/m1/s1 ChemAxon InChIKey InChIKey=VLPIATFUUWWMKC-SNVBAGLBSA-N ChemAxon Polar Surface Area (PSA) 35.25 ChemAxon Refractivity 54.97 ChemAxon Polarizability 21.16 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 9.52 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 180621 PubChem Substance 99443600 ChemSpider 157171 PDB 505 BE0000895 Urokinase-type plasminogen activator Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Urokinase-type plasminogen activator Involved in chemotaxis and signal transduction activity Specifically cleave the zymogen plasminogen to form the active enzyme plasmin PLAU 10q24 Secreted protein None 8.48 48526.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9052 GenAtlas PLAU GeneCards PLAU GenBank Gene Database X02419 GenBank Protein Database 1834524 UniProtKB P00749 UniProt Accession UROK_HUMAN EC 3.4.21.73 U-plasminogen activator uPA Urokinase-type plasminogen activator precursor >Urokinase-type plasminogen activator precursor MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQ HCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHN YCRNPDNRRRPWCYVQVGLKPLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKII GGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLMSPCWVISATHCFIDYPKKEDYIVYLG RSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICL PSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKML CAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIR SHTKEENGLAL >1296 bp ATGAGAGCCCTGCTGGCGCGCCTGCTTCTCTGCGTCCTGGTCGTGAGCGACTCCAAAGGC AGCAATGAACTTCATCAAGTTCCATCGAACTGTGACTGTCTAAATGGAGGAACATGTGTG TCCAACAAGTACTTCTCCAACATTCACTGGTGCAACTGCCCAAAGAAATTCGGAGGGCAG CACTGTGAAATAGATAAGTCAAAAACCTGCTATGAGGGGAATGGTCACTTTTACCGAGGA AAGGCCAGCACTGACACCATGGGCCGGCCCTGCCTGCCCTGGAACTCTGCCACTGTCCTT CAGCAAACGTACCATGCCCACAGATCTGATGCTCTTCAGCTGGGCCTGGGGAAACATAAT TACTGCAGGAACCCAGACAACCGGAGGCGACCCTGGTGCTATGTGCAGGTGGGCCTAAAG CCGCTTGTCCAAGAGTGCATGGTGCATGACTGCGCAGATGGAAAAAAGCCCTCCTCTCCT CCAGAAGAATTAAAATTTCAGTGTGGCCAAAAGACTCTGAGGCCCCGCTTTAAGATTATT GGGGGAGAATTCACCACCATCGAGAACCAGCCCTGGTTTGCGGCCATCTACAGGAGGCAC CGGGGGGGCTCTGTCACCTACGTGTGTGGAGGCAGCCTCATGAGCCCTTGCTGGGTGATC AGCGCCACACACTGCTTCATTGATTACCCAAAGAAGGAGGACTACATCGTCTACCTGGGT CGCTCAAGGCTTAACTCCAACACGCAAGGGGAGATGAAGTTTGAGGTGGAAAACCTCATC CTACACAAGGACTACAGCGCTGACACGCTTGCTCACCACAACGACATTGCCTTGCTGAAG ATCCGTTCCAAGGAGGGCAGGTGTGCGCAGCCATCCCGGACTATACAGACCATCTGCCTG CCCTCGATGTATAACGATCCCCAGTTTGGCACAAGCTGTGAGATCACTGGCTTTGGAAAA GAGAATTCTACCGACTATCTCTATCCGGAGCAGCTGAAAATGACTGTTGTGAAGCTGATT TCCCACCGGGAGTGTCAGCAGCCCCACTACTACGGCTCTGAAGTCACCACCAAAATGCTG TGTGCTGCTGACCCACAGTGGAAAACAGATTCCTGCCAGGGAGACTCAGGGGGACCCCTC GTCTGTTCCCTCCAAGGCCGCATGACTTTGACTGGAATTGTGAGCTGGGGCCGTGGATGT GCCCTGAAGGACAAGCCAGGCGTCTACACGAGAGTCTCACACTTCTTACCCTGGATCCGC AGTCACACCAAGGAAGAGAATGGCCTGGCCCTCTGA PF00051 Kringle PF00089 Trypsin function hydrolase activity function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity process metabolism process macromolecule metabolism process protein metabolism process cellular protein metabolism process proteolysis process physiological process "
drug:(2R)-1-(2,6-dimethylphenoxy)propan-2-aminerdfs:label"(2R)-1-(2,6-dimethylphenoxy)propan-2-amine"
drug:(2R)-1-(2,6-dimethylphenoxy)propan-2-aminerdf:typedrugbank:drugs
drug:(2R)-1-(DIMETHYLAMINO)-3-{4-[(6-{[2-FLUORO-5-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-4-YL)AMINO]PHENOXY}PROPAN-2-OLdrugbank:description" experimental This compound belongs to the phenol ethers. These are aromatic compounds containing an ether group substituted with a benzene ring. Phenol Ethers Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenol Ethers Alkyl Aryl Ethers Fluorobenzenes Aminopyrimidines and Derivatives Aryl Fluorides Tertiary Amines Secondary Alcohols Polyamines Secondary Amines Alkyl Fluorides Organofluorides alkyl aryl ether aminopyrimidine fluorobenzene pyrimidine aryl fluoride aryl halide secondary alcohol tertiary amine polyamine ether secondary amine organofluoride organohalogen amine alcohol alkyl halide alkyl fluoride organonitrogen compound logP 3.73 ALOGPS logS -4.3 ALOGPS Water Solubility 2.55e-02 g/l ALOGPS logP 4.37 ChemAxon IUPAC Name 4-N-{4-[(2R)-3-(dimethylamino)-2-hydroxypropoxy]phenyl}-6-N-[2-fluoro-5-(trifluoromethyl)phenyl]pyrimidine-4,6-diamine ChemAxon Traditional IUPAC Name 4-N-{4-[(2R)-3-(dimethylamino)-2-hydroxypropoxy]phenyl}-6-N-[2-fluoro-5-(trifluoromethyl)phenyl]pyrimidine-4,6-diamine ChemAxon Molecular Weight 465.4439 ChemAxon Monoisotopic Weight 465.178787825 ChemAxon SMILES [H][C@](O)(COC1=CC=C(NC2=NC=NC(NC3=C(F)C=CC(=C3)C(F)(F)F)=C2)C=C1)CN(C)C ChemAxon Molecular Formula C22H23F4N5O2 ChemAxon InChI InChI=1S/C22H23F4N5O2/c1-31(2)11-16(32)12-33-17-6-4-15(5-7-17)29-20-10-21(28-13-27-20)30-19-9-14(22(24,25)26)3-8-18(19)23/h3-10,13,16,32H,11-12H2,1-2H3,(H2,27,28,29,30)/t16-/m1/s1 ChemAxon InChIKey InChIKey=OSCWQKTUILTARV-MRXNPFEDSA-N ChemAxon Polar Surface Area (PSA) 82.54 ChemAxon Refractivity 116.96 ChemAxon Polarizability 45.07 ChemAxon Rotatable Bond Count 10 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 13.22 ChemAxon pKa (strongest basic) 8.7 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 448994 PubChem Substance 99443525 ChemSpider 395634 PDB 3FP BE0001072 Cyclin-dependent kinase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cyclin-dependent kinase 2 Involved in protein kinase activity ATP + a protein = ADP + a phosphoprotein CDK2deltaT None 9.76 30061.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1771 GenAtlas CDK2deltaT GeneCards CDK2deltaT GenBank Gene Database AB012305 GenBank Protein Database 3551191 UniProtKB P24941 UniProt Accession CDK2_HUMAN EC 2.7.11.22 p33 protein kinase >Cell division protein kinase 2 MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL >897 bp ATGGAGAACTTCCAAAAGGTGGAAAAGATCGGAGAGGGCACGTACGGAGTTGTGTACAAA GCCAGAAACAAGTTGACGGGAGAGGTGGTGGCGCTTAAGAAAATCCGCCTGGACACTGAG ACTGAGGGTGTGCCCAGTACTGCCATCCGAGAGATCTCTCTGCTTAAGGAGCTTAACCAT CCTAATATTGTCAAGCTGCTGGATGTCATTCACACAGAAAATAAACTCTACCTGGTTTTT GAATTTCTGCACCAAGATCTCAAGAAATTCATGGATGCCTCTGCTCTCACTGGCATTCCT CTTCCCCTCATCAAGAGCTATCTGTTCCAGCTGCTCCAGGGCCTAGCTTTCTGCCATTCT CATCGGGTCCTCCACCGAGACCTTAAACCTCAGAATCTGCTTATTAACACAGAGGGGGCC ATCAAGCTAGCAGACTTTGGACTAGCCAGAGCTTTTGGAGTCCCTGTTCGTACTTACACC CATGAGGTGGTGACCCTGTGGTACCGAGCTCCTGAAATCCTCCTGGGCTCGAAATATTAT TCCACAGCTGTGGACATCTGGAGCCTGGGCTGCATCTTTGCTGAGATGGTGACTCGCCGG GCCCTGTTCCCTGGAGATTCTGAGATTGACCAGCTCTTCCGGATCTTTCGGACTCTGGGG ACCCCAGATGAGGTGGTGTGGCCAGGAGTTACTTCTATGCCTGATTACAAGCCAAGTTTC CCCAAGTGGGCCCGGCAAGATTTTAGTAAAGTTGTACCTCCCCTGGATGAAGATGGACGG AGCTTGTTATCGCAAATGCTGCACTACGACCCTAACAAGCGGATTTCGGCCAAGGCAGCC CTGGCTCACCCTTTCTTCCAGGATGTGACCAAGCCAGTACCCCATCTTCGACTCTGA PF00069 Pkinase function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism "
drug:(2R)-1-(DIMETHYLAMINO)-3-{4-[(6-{[2-FLUORO-5-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-4-YL)AMINO]PHENOXY}PROPAN-2-OLrdfs:label"(2R)-1-(DIMETHYLAMINO)-3-{4-[(6-{[2-FLUORO-5-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-4-YL)AMINO]PHENOXY}PROPAN-2-OL"
drug:(2R)-1-(DIMETHYLAMINO)-3-{4-[(6-{[2-FLUORO-5-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-4-YL)AMINO]PHENOXY}PROPAN-2-OLrdf:typedrugbank:drugs
drug:(2R)-1-[(4-tert-butylphenyl)sulfonyl]-2-methyl-4-(4-nitrophenyl)piperazinedrugbank:description" experimental This compound belongs to the phenylpiperazines. These are compounds containing a phenylpiperazine skeleton, which consists of a piperazine bound to a phenyl group. Phenylpiperazines Organic Compounds Heterocyclic Compounds Piperazines Phenylpiperazines Benzenesulfonamides Cumenes Nitrobenzenes Diazinanes Sulfonyls Sulfonamides Nitronic Acids Nitro Compounds Tertiary Amines Polyamines Organic Oxoazanium Compounds benzenesulfonamide cumene nitrobenzene 1,4-diazinane benzene sulfonyl sulfonamide sulfonic acid derivative nitro compound tertiary amine nitronic acid organic oxoazanium polyamine organonitrogen compound amine logP 4.05 ALOGPS logS -4.7 ALOGPS Water Solubility 7.84e-03 g/l ALOGPS logP 4.67 ChemAxon IUPAC Name (2R)-1-[(4-tert-butylbenzene)sulfonyl]-2-methyl-4-(4-nitrophenyl)piperazine ChemAxon Traditional IUPAC Name (2R)-1-(4-tert-butylbenzenesulfonyl)-2-methyl-4-(4-nitrophenyl)piperazine ChemAxon Molecular Weight 417.522 ChemAxon Monoisotopic Weight 417.172227057 ChemAxon SMILES [H][C@@]1(C)CN(CCN1S(=O)(=O)C1=CC=C(C=C1)C(C)(C)C)C1=CC=C(C=C1)[N+]([O-])=O ChemAxon Molecular Formula C21H27N3O4S ChemAxon InChI InChI=1S/C21H27N3O4S/c1-16-15-22(18-7-9-19(10-8-18)24(25)26)13-14-23(16)29(27,28)20-11-5-17(6-12-20)21(2,3)4/h5-12,16H,13-15H2,1-4H3/t16-/m1/s1 ChemAxon InChIKey InChIKey=SOFGQQQVQZQJFS-MRXNPFEDSA-N ChemAxon Polar Surface Area (PSA) 86.44 ChemAxon Refractivity 114.97 ChemAxon Polarizability 44.68 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest basic) -1.5 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 24812720 PubChem Substance 99443520 ChemSpider 23315644 PDB 3CZ BE0000329 Corticosteroid 11-beta-dehydrogenase isozyme 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Corticosteroid 11-beta-dehydrogenase isozyme 1 Lipid transport and metabolism Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7- ketocholesterol to 7-beta-hydroxycholesterol HSD11B1 1q32-q41 Endoplasmic reticulum; endoplasmic reticulum membrane; single-pass type II membrane protein 7-23 8.77 32270.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:5208 GenAtlas HSD11B1 GeneCards HSD11B1 GenBank Gene Database M76665 GenBank Protein Database 179475 UniProtKB P28845 UniProt Accession DHI1_HUMAN 11-beta-HSD1 11-beta-hydroxysteroid dehydrogenase 1 11-DH EC 1.1.1.146 >Corticosteroid 11-beta-dehydrogenase isozyme 1 AFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHV VVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHI TNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVA AYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEEC ALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK >879 bp ATGGCTTTTATGAAAAAATATCTCCTCCCCATTCTGGGGCTCTTCATGGCCTACTACTAC TATTCTGCAAACGAGGAATTCAGACCAGAGATGCTCCAAGGAAAGAAAGTGATTGTCACA GGGGCCAGCAAAGGGATCGGAAGAGAGATGGCTTATCATCTGGCGAAGATGGGAGCCCAT GTGGTGGTGACAGCGAGGTCAAAAGAAACTCTACAGAAGGTGGTATCCCACTGCCTGGAG CTTGGAGCAGCCTCAGCACACTACATTGCTGGCACCATGGAAGACATGACCTTCGCAGAG CAATTTGTTGCCCAAGCAGGAAAGCTCATGGGAGGACTAGACATGCTCATTCTCAACCAC ATCACCAACACTTCTTTGAATCTTTTTCATGATGATATTCACCATGTGCGCAAAAGCATG GAAGTCAACTTCCTCAGTTACGTGGTCCTGACTGTAGCTGCCTTGCCCATGCTGAAGCAG AGCAATGGAAGCATTGTTGTCGTCTCCTCTCTGGCTGGGAAAGTGGCTTATCCAATGGTT GCTGCCTATTCTGCAAGCAAGTTTGCTTTGGATGGGTTCTTCTCCTCCATCAGAAAGGAA TATTCAGTGTCCAGGGTCAATGTATCAATCACTCTCTGTGTTCTTGGCCTCATAGACACA GAAACAGCCATGAAGGCAGTTTCTGGGATAGTCCATATGCAAGCAGCTCCAAAGGAGGAA TGTGCCCTGGAGATCATCAAAGGGGGAGCTCTGCGCCAAGAAGAAGTGTATTATGACAGC TCACTCTGGACCACTCTTCTGATCAGAAATCCATGCAGGAAGATCCTGGAATTTCTCTAC TCAACGAGCTATAATATGGACAGATTCATAAACAAGTAG PF00106 adh_short function catalytic activity function oxidoreductase activity process physiological process process metabolism "
drug:(2R)-1-[(4-tert-butylphenyl)sulfonyl]-2-methyl-4-(4-nitrophenyl)piperazinerdfs:label"(2R)-1-[(4-tert-butylphenyl)sulfonyl]-2-methyl-4-(4-nitrophenyl)piperazine"
drug:(2R)-1-[(4-tert-butylphenyl)sulfonyl]-2-methyl-4-(4-nitrophenyl)piperazinerdf:typedrugbank:drugs
drug:(2R)-1-[(5,6-DIPHENYL-7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)AMINO]PROPAN-2-OLdrugbank:description" experimental This compound belongs to the stilbenes. These are organic compounds containing a 1,2-diphenylethylene moiety. Stilbenes (C6-C2-C6 ) are derived from the common phenylpropene (C6-C3) skeleton building block. The introduction of one or more hydroxyl groups to a phenyl ring lead to stilbenoids. Stilbenes Organic Compounds Phenylpropanoids and Polyketides Stilbenes Phenylpyrroles Pyrrolopyrimidines Aminopyrimidines and Derivatives Benzene and Substituted Derivatives Secondary Alcohols 1,2-Aminoalcohols Polyamines Secondary Amines 3-phenylpyrrole 2-phenylpyrrole pyrrolopyrimidine aminopyrimidine substituted pyrrole pyrimidine benzene pyrrole 1,2-aminoalcohol secondary alcohol secondary amine polyamine amine alcohol organonitrogen compound logP 3.93 ALOGPS logS -4.7 ALOGPS Water Solubility 7.44e-03 g/l ALOGPS logP 3.52 ChemAxon IUPAC Name (2R)-1-({5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl}amino)propan-2-ol ChemAxon Traditional IUPAC Name (2R)-1-({5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl}amino)propan-2-ol ChemAxon Molecular Weight 344.4097 ChemAxon Monoisotopic Weight 344.163711282 ChemAxon SMILES [H][C@](C)(O)CNC1=C2C(NC(=C2C2=CC=CC=C2)C2=CC=CC=C2)=NC=N1 ChemAxon Molecular Formula C21H20N4O ChemAxon InChI InChI=1S/C21H20N4O/c1-14(26)12-22-20-18-17(15-8-4-2-5-9-15)19(16-10-6-3-7-11-16)25-21(18)24-13-23-20/h2-11,13-14,26H,12H2,1H3,(H2,22,23,24,25)/t14-/m1/s1 ChemAxon InChIKey InChIKey=VBASHTSSQNDDAS-CQSZACIVSA-N ChemAxon Polar Surface Area (PSA) 73.83 ChemAxon Refractivity 105.13 ChemAxon Polarizability 37.69 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 12.28 ChemAxon pKa (strongest basic) 7.07 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 4369434 PubChem Substance 99444118 ChemSpider 3571996 PDB DF1 BE0003382 Serine/threonine-protein kinase Chk1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Serine/threonine-protein kinase Chk1 Involved in protein kinase activity Required for checkpoint mediated cell cycle arrest in response to DNA damage or the presence of unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Recognizes the substrate consensus sequence [R-X-X- S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser- 293' promotes proteolysis of CDC25A. Inhibition of CDC25 activity leads to increased inhibitory tyrosine phosphorylation of CDK- cyclin complexes and blocks cell cycle progression. Binds to and phosphorylates RAD51 at 'Thr-309', which may enhance the association of RAD51 with chromatin and promote DNA repair by homologous recombination. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may affect chromatin assembly during S phase or DNA repair. May also phosphorylate multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and enhances suppression of cellular proliferation CHEK1 11q24-q24 Nucleus. Cytoplasm None 8.38 54420.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1925 GenAtlas CHEK1 GenBank Gene Database AF016582 UniProtKB O14757 UniProt Accession CHK1_HUMAN EC 2.7.11.1 >Serine/threonine-protein kinase Chk1 MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINK MLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVY LHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLK RREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLA LLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGFSKHIQSNLDF SPVNSASSEENVKYSSSQPEPRTGLSLWDTSPSYIDKLVQGISFSQPTCPDHMLLNSQLL GTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETCEKLGYQWKKSCMNQVTISTTDRR NNKLIFKVNLLEMDDKILVDFRLSKGDGLEFKRHFLKIKGKLIDIVSSQKVWLPAT >1431 bp ATGGCAGTGCCCTTTGTGGAAGACTGGGACTTGGTGCAAACCCTGGGAGAAGGTGCCTAT GGAGAAGTTCAACTTGCTGTGAATAGAGTAACTGAAGAAGCAGTCGCAGTGAAGATTGTA GATATGAAGCGTGCCGTAGACTGTCCAGAAAATATTAAGAAAGAGATCTGTATCAATAAA ATGCTAAATCATGAAAATGTAGTAAAATTCTATGGTCACAGGAGAGAAGGCAATATCCAA TATTTATTTCTGGAGTACTGTAGTGGAGGAGAGCTTTTTGACAGAATAGAGCCAGACATA GGCATGCCTGAACCAGATGCTCAGAGATTCTTCCATCAACTCATGGCAGGGGTGGTTTAT CTGCATGGTATTGGAATAACTCACAGGGATATTAAACCAGAAAATCTTCTGTTGGATGAA AGGGATAACCTCAAAATCTCAGACTTTGGCTTGGCAACAGTATTTCGGTATAATAATCGT GAGCGTTTGTTGAACAAGATGTGTGGTACTTTACCATATGTTGCTCCAGAACTTCTGAAG AGAAGAGAATTTCATGCAGAACCAGTTGATGTTTGGTCCTGTGGAATAGTACTTACTGCA ATGCTCGCTGGAGAATTGCCATGGGACCAACCCAGTGACAGCTGTCAGGAGTATTCTGAC TGGAAAGAAAAAAAAACATACCTCAACCCTTGGAAAAAAATCGATTCTGCTCCTCTAGCT CTGCTGCATAAAATCTTAGTTGAGAATCCATCAGCAAGAATTACCATTCCAGACATCAAA AAAGATAGATGGTACAACAAACCCCTCAAGAAAGGGGCAAAAAGGCCCCGAGTCACTTCA GGTGGTGTGTCAGAGTCTCCCAGTGGATTTTCTAAGCACATTCAATCCAATTTGGACTTC TCTCCAGTAAACAGTGCTTCTAGTGAAGAAAATGTGAAGTACTCCAGTTCTCAGCCAGAA CCCCGCACAGGTCTTTCCTTATGGGATACCAGCCCCTCATACATTGATAAATTGGTACAA GGGATCAGCTTTTCCCAGCCCACATGTCCTGATCATATGCTTTTGAATAGTCAGTTACTT GGCACCCCAGGATCCTCACAGAACCCCTGGCAGCGGTTGGTCAAAAGAATGACACGATTC TTTACCAAATTGGATGCAGACAAATCTTATCAATGCCTGAAAGAGACTTGTGAGAAGTTG GGCTATCAATGGAAGAAAAGTTGTATGAATCAGGTTACTATATCAACAACTGATAGGAGA AACAATAAACTCATTTTCAAAGTGAATTTGTTAGAAATGGATGATAAAATATTGGTTGAC TTCCGGCTTTCTAAGGGTGATGGATTGGAGTTCAAGAGACACTTCCTGAAGATTAAAGGG AAGCTGATTGATATTGTGAGCAGCCAGAAGGTTTGGCTTCCTGCCACATGA PF00069 Pkinase function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity process protein modification process physiological process process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification "
drug:(2R)-1-[(5,6-DIPHENYL-7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)AMINO]PROPAN-2-OLrdfs:label"(2R)-1-[(5,6-DIPHENYL-7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)AMINO]PROPAN-2-OL"
drug:(2R)-1-[(5,6-DIPHENYL-7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)AMINO]PROPAN-2-OLrdf:typedrugbank:drugs
drug:(2R)-1-[4-({4-[(2,5-DICHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)PHENOXY]-3-(DIMETHYLAMINO)PROPAN-2-OLdrugbank:description" experimental This compound belongs to the phenol ethers. These are aromatic compounds containing an ether group substituted with a benzene ring. Phenol Ethers Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenol Ethers Dichlorobenzenes Aminopyrimidines and Derivatives Alkyl Aryl Ethers Aryl Chlorides Tertiary Amines Secondary Alcohols Polyamines Secondary Amines Organochlorides alkyl aryl ether aminopyrimidine chlorobenzene aryl chloride aryl halide pyrimidine secondary alcohol tertiary amine polyamine secondary amine ether amine organochloride organohalogen alcohol organonitrogen compound logP 4.38 ALOGPS logS -4.3 ALOGPS Water Solubility 2.00e-02 g/l ALOGPS logP 4.64 ChemAxon IUPAC Name 4-N-(2,5-dichlorophenyl)-2-N-{4-[(2R)-3-(dimethylamino)-2-hydroxypropoxy]phenyl}pyrimidine-2,4-diamine ChemAxon Traditional IUPAC Name 4-N-(2,5-dichlorophenyl)-2-N-{4-[(2R)-3-(dimethylamino)-2-hydroxypropoxy]phenyl}pyrimidine-2,4-diamine ChemAxon Molecular Weight 448.346 ChemAxon Monoisotopic Weight 447.122880419 ChemAxon SMILES [H][C@](O)(COC1=CC=C(NC2=NC(NC3=C(Cl)C=CC(Cl)=C3)=CC=N2)C=C1)CN(C)C ChemAxon Molecular Formula C21H23Cl2N5O2 ChemAxon InChI InChI=1S/C21H23Cl2N5O2/c1-28(2)12-16(29)13-30-17-6-4-15(5-7-17)25-21-24-10-9-20(27-21)26-19-11-14(22)3-8-18(19)23/h3-11,16,29H,12-13H2,1-2H3,(H2,24,25,26,27)/t16-/m1/s1 ChemAxon InChIKey InChIKey=GNLAGGCSJGJECE-MRXNPFEDSA-N ChemAxon Polar Surface Area (PSA) 82.54 ChemAxon Refractivity 120.01 ChemAxon Polarizability 47.32 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 13.61 ChemAxon pKa (strongest basic) 8.7 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 445952 PubChem Substance 99444221 ChemSpider 393432 PDB FAL BE0001072 Cyclin-dependent kinase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cyclin-dependent kinase 2 Involved in protein kinase activity ATP + a protein = ADP + a phosphoprotein CDK2deltaT None 9.76 30061.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1771 GenAtlas CDK2deltaT GeneCards CDK2deltaT GenBank Gene Database AB012305 GenBank Protein Database 3551191 UniProtKB P24941 UniProt Accession CDK2_HUMAN EC 2.7.11.22 p33 protein kinase >Cell division protein kinase 2 MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL >897 bp ATGGAGAACTTCCAAAAGGTGGAAAAGATCGGAGAGGGCACGTACGGAGTTGTGTACAAA GCCAGAAACAAGTTGACGGGAGAGGTGGTGGCGCTTAAGAAAATCCGCCTGGACACTGAG ACTGAGGGTGTGCCCAGTACTGCCATCCGAGAGATCTCTCTGCTTAAGGAGCTTAACCAT CCTAATATTGTCAAGCTGCTGGATGTCATTCACACAGAAAATAAACTCTACCTGGTTTTT GAATTTCTGCACCAAGATCTCAAGAAATTCATGGATGCCTCTGCTCTCACTGGCATTCCT CTTCCCCTCATCAAGAGCTATCTGTTCCAGCTGCTCCAGGGCCTAGCTTTCTGCCATTCT CATCGGGTCCTCCACCGAGACCTTAAACCTCAGAATCTGCTTATTAACACAGAGGGGGCC ATCAAGCTAGCAGACTTTGGACTAGCCAGAGCTTTTGGAGTCCCTGTTCGTACTTACACC CATGAGGTGGTGACCCTGTGGTACCGAGCTCCTGAAATCCTCCTGGGCTCGAAATATTAT TCCACAGCTGTGGACATCTGGAGCCTGGGCTGCATCTTTGCTGAGATGGTGACTCGCCGG GCCCTGTTCCCTGGAGATTCTGAGATTGACCAGCTCTTCCGGATCTTTCGGACTCTGGGG ACCCCAGATGAGGTGGTGTGGCCAGGAGTTACTTCTATGCCTGATTACAAGCCAAGTTTC CCCAAGTGGGCCCGGCAAGATTTTAGTAAAGTTGTACCTCCCCTGGATGAAGATGGACGG AGCTTGTTATCGCAAATGCTGCACTACGACCCTAACAAGCGGATTTCGGCCAAGGCAGCC CTGGCTCACCCTTTCTTCCAGGATGTGACCAAGCCAGTACCCCATCTTCGACTCTGA PF00069 Pkinase function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism "
drug:(2R)-1-[4-({4-[(2,5-DICHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)PHENOXY]-3-(DIMETHYLAMINO)PROPAN-2-OLrdfs:label"(2R)-1-[4-({4-[(2,5-DICHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)PHENOXY]-3-(DIMETHYLAMINO)PROPAN-2-OL"
drug:(2R)-1-[4-({4-[(2,5-DICHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)PHENOXY]-3-(DIMETHYLAMINO)PROPAN-2-OLrdf:typedrugbank:drugs
drug:(2R)-1-[4-({6-[(2,6-DIFLUOROPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)PHENOXY]-3-(DIMETHYLAMINO)PROPAN-2-OLdrugbank:description" experimental This compound belongs to the phenol ethers. These are aromatic compounds containing an ether group substituted with a benzene ring. Phenol Ethers Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenol Ethers Alkyl Aryl Ethers Fluorobenzenes Aminopyrimidines and Derivatives Aryl Fluorides Tertiary Amines Secondary Alcohols Polyamines Secondary Amines Organofluorides alkyl aryl ether aminopyrimidine fluorobenzene aryl fluoride aryl halide pyrimidine secondary alcohol tertiary amine polyamine secondary amine ether amine organofluoride organohalogen alcohol organonitrogen compound logP 3.45 ALOGPS logS -4.1 ALOGPS Water Solubility 3.61e-02 g/l ALOGPS logP 3.63 ChemAxon IUPAC Name 4-N-(2,6-difluorophenyl)-6-N-{4-[(2R)-3-(dimethylamino)-2-hydroxypropoxy]phenyl}pyrimidine-4,6-diamine ChemAxon Traditional IUPAC Name 4-N-(2,6-difluorophenyl)-6-N-{4-[(2R)-3-(dimethylamino)-2-hydroxypropoxy]phenyl}pyrimidine-4,6-diamine ChemAxon Molecular Weight 415.4364 ChemAxon Monoisotopic Weight 415.181981415 ChemAxon SMILES [H][C@](O)(COC1=CC=C(NC2=NC=NC(NC3=C(F)C=CC=C3F)=C2)C=C1)CN(C)C ChemAxon Molecular Formula C21H23F2N5O2 ChemAxon InChI InChI=1S/C21H23F2N5O2/c1-28(2)11-15(29)12-30-16-8-6-14(7-9-16)26-19-10-20(25-13-24-19)27-21-17(22)4-3-5-18(21)23/h3-10,13,15,29H,11-12H2,1-2H3,(H2,24,25,26,27)/t15-/m1/s1 ChemAxon InChIKey InChIKey=ZVSBKYYVBCKDBO-OAHLLOKOSA-N ChemAxon Polar Surface Area (PSA) 82.54 ChemAxon Refractivity 111.2 ChemAxon Polarizability 42.83 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 11.33 ChemAxon pKa (strongest basic) 8.7 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 445951 PubChem Substance 99444232 ChemSpider 393431 PDB FCP BE0001072 Cyclin-dependent kinase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cyclin-dependent kinase 2 Involved in protein kinase activity ATP + a protein = ADP + a phosphoprotein CDK2deltaT None 9.76 30061.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1771 GenAtlas CDK2deltaT GeneCards CDK2deltaT GenBank Gene Database AB012305 GenBank Protein Database 3551191 UniProtKB P24941 UniProt Accession CDK2_HUMAN EC 2.7.11.22 p33 protein kinase >Cell division protein kinase 2 MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL >897 bp ATGGAGAACTTCCAAAAGGTGGAAAAGATCGGAGAGGGCACGTACGGAGTTGTGTACAAA GCCAGAAACAAGTTGACGGGAGAGGTGGTGGCGCTTAAGAAAATCCGCCTGGACACTGAG ACTGAGGGTGTGCCCAGTACTGCCATCCGAGAGATCTCTCTGCTTAAGGAGCTTAACCAT CCTAATATTGTCAAGCTGCTGGATGTCATTCACACAGAAAATAAACTCTACCTGGTTTTT GAATTTCTGCACCAAGATCTCAAGAAATTCATGGATGCCTCTGCTCTCACTGGCATTCCT CTTCCCCTCATCAAGAGCTATCTGTTCCAGCTGCTCCAGGGCCTAGCTTTCTGCCATTCT CATCGGGTCCTCCACCGAGACCTTAAACCTCAGAATCTGCTTATTAACACAGAGGGGGCC ATCAAGCTAGCAGACTTTGGACTAGCCAGAGCTTTTGGAGTCCCTGTTCGTACTTACACC CATGAGGTGGTGACCCTGTGGTACCGAGCTCCTGAAATCCTCCTGGGCTCGAAATATTAT TCCACAGCTGTGGACATCTGGAGCCTGGGCTGCATCTTTGCTGAGATGGTGACTCGCCGG GCCCTGTTCCCTGGAGATTCTGAGATTGACCAGCTCTTCCGGATCTTTCGGACTCTGGGG ACCCCAGATGAGGTGGTGTGGCCAGGAGTTACTTCTATGCCTGATTACAAGCCAAGTTTC CCCAAGTGGGCCCGGCAAGATTTTAGTAAAGTTGTACCTCCCCTGGATGAAGATGGACGG AGCTTGTTATCGCAAATGCTGCACTACGACCCTAACAAGCGGATTTCGGCCAAGGCAGCC CTGGCTCACCCTTTCTTCCAGGATGTGACCAAGCCAGTACCCCATCTTCGACTCTGA PF00069 Pkinase function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism "
drug:(2R)-1-[4-({6-[(2,6-DIFLUOROPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)PHENOXY]-3-(DIMETHYLAMINO)PROPAN-2-OLrdfs:label"(2R)-1-[4-({6-[(2,6-DIFLUOROPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)PHENOXY]-3-(DIMETHYLAMINO)PROPAN-2-OL"
drug:(2R)-1-[4-({6-[(2,6-DIFLUOROPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)PHENOXY]-3-(DIMETHYLAMINO)PROPAN-2-OLrdf:typedrugbank:drugs
drug:(2R)-1-{4-[(4-ANILINO-5-BROMOPYRIMIDIN-2-YL)AMINO]PHENOXY}-3-(DIMETHYLAMINO)PROPAN-2-OLdrugbank:description" experimental This compound belongs to the phenol ethers. These are aromatic compounds containing an ether group substituted with a benzene ring. Phenol Ethers Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenol Ethers Alkyl Aryl Ethers Halopyrimidines Aminopyrimidines and Derivatives Aryl Bromides Tertiary Amines Secondary Alcohols Polyamines Secondary Amines Organobromides alkyl aryl ether aminopyrimidine halopyrimidine aryl bromide aryl halide pyrimidine secondary alcohol tertiary amine polyamine secondary amine ether amine organobromide organohalogen alcohol organonitrogen compound logP 3.83 ALOGPS logS -4.1 ALOGPS Water Solubility 3.50e-02 g/l ALOGPS logP 4.2 ChemAxon IUPAC Name 5-bromo-2-N-{4-[(2R)-3-(dimethylamino)-2-hydroxypropoxy]phenyl}-4-N-phenylpyrimidine-2,4-diamine ChemAxon Traditional IUPAC Name 5-bromo-2-N-{4-[(2R)-3-(dimethylamino)-2-hydroxypropoxy]phenyl}-4-N-phenylpyrimidine-2,4-diamine ChemAxon Molecular Weight 458.352 ChemAxon Monoisotopic Weight 457.111337684 ChemAxon SMILES [H][C@](O)(COC1=CC=C(NC2=NC(NC3=CC=CC=C3)=C(Br)C=N2)C=C1)CN(C)C ChemAxon Molecular Formula C21H24BrN5O2 ChemAxon InChI InChI=1S/C21H24BrN5O2/c1-27(2)13-17(28)14-29-18-10-8-16(9-11-18)25-21-23-12-19(22)20(26-21)24-15-6-4-3-5-7-15/h3-12,17,28H,13-14H2,1-2H3,(H2,23,24,25,26)/t17-/m1/s1 ChemAxon InChIKey InChIKey=MEIJADBULOETOV-QGZVFWFLSA-N ChemAxon Polar Surface Area (PSA) 82.54 ChemAxon Refractivity 118.02 ChemAxon Polarizability 46.26 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 13.63 ChemAxon pKa (strongest basic) 8.7 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 445957 PubChem Substance 99443975 ChemSpider 393437 PDB BYP BE0001072 Cyclin-dependent kinase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cyclin-dependent kinase 2 Involved in protein kinase activity ATP + a protein = ADP + a phosphoprotein CDK2deltaT None 9.76 30061.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1771 GenAtlas CDK2deltaT GeneCards CDK2deltaT GenBank Gene Database AB012305 GenBank Protein Database 3551191 UniProtKB P24941 UniProt Accession CDK2_HUMAN EC 2.7.11.22 p33 protein kinase >Cell division protein kinase 2 MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL >897 bp ATGGAGAACTTCCAAAAGGTGGAAAAGATCGGAGAGGGCACGTACGGAGTTGTGTACAAA GCCAGAAACAAGTTGACGGGAGAGGTGGTGGCGCTTAAGAAAATCCGCCTGGACACTGAG ACTGAGGGTGTGCCCAGTACTGCCATCCGAGAGATCTCTCTGCTTAAGGAGCTTAACCAT CCTAATATTGTCAAGCTGCTGGATGTCATTCACACAGAAAATAAACTCTACCTGGTTTTT GAATTTCTGCACCAAGATCTCAAGAAATTCATGGATGCCTCTGCTCTCACTGGCATTCCT CTTCCCCTCATCAAGAGCTATCTGTTCCAGCTGCTCCAGGGCCTAGCTTTCTGCCATTCT CATCGGGTCCTCCACCGAGACCTTAAACCTCAGAATCTGCTTATTAACACAGAGGGGGCC ATCAAGCTAGCAGACTTTGGACTAGCCAGAGCTTTTGGAGTCCCTGTTCGTACTTACACC CATGAGGTGGTGACCCTGTGGTACCGAGCTCCTGAAATCCTCCTGGGCTCGAAATATTAT TCCACAGCTGTGGACATCTGGAGCCTGGGCTGCATCTTTGCTGAGATGGTGACTCGCCGG GCCCTGTTCCCTGGAGATTCTGAGATTGACCAGCTCTTCCGGATCTTTCGGACTCTGGGG ACCCCAGATGAGGTGGTGTGGCCAGGAGTTACTTCTATGCCTGATTACAAGCCAAGTTTC CCCAAGTGGGCCCGGCAAGATTTTAGTAAAGTTGTACCTCCCCTGGATGAAGATGGACGG AGCTTGTTATCGCAAATGCTGCACTACGACCCTAACAAGCGGATTTCGGCCAAGGCAGCC CTGGCTCACCCTTTCTTCCAGGATGTGACCAAGCCAGTACCCCATCTTCGACTCTGA PF00069 Pkinase function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism "
drug:(2R)-1-{4-[(4-ANILINO-5-BROMOPYRIMIDIN-2-YL)AMINO]PHENOXY}-3-(DIMETHYLAMINO)PROPAN-2-OLrdfs:label"(2R)-1-{4-[(4-ANILINO-5-BROMOPYRIMIDIN-2-YL)AMINO]PHENOXY}-3-(DIMETHYLAMINO)PROPAN-2-OL"
drug:(2R)-1-{4-[(4-ANILINO-5-BROMOPYRIMIDIN-2-YL)AMINO]PHENOXY}-3-(DIMETHYLAMINO)PROPAN-2-OLrdf:typedrugbank:drugs
drug:(2R)-2-(4-CHLOROPHENYL)-2-PHENYLETHANAMINEdrugbank:description" experimental This compound belongs to the diphenylmethanes. These are compounds containing a diphenylmethane moiety, which consists of a methane wherein two hydrogen atoms are replaced by two phenyl groups. Diphenylmethanes Organic Compounds Benzenoids Benzene and Substituted Derivatives Diphenylmethanes Phenylpropylamines Chlorobenzenes Aryl Chlorides Polyamines Monoalkylamines Organochlorides phenylpropylamine chlorobenzene aryl chloride aryl halide polyamine organochloride primary amine organohalogen primary aliphatic amine amine organonitrogen compound logP 3.74 ALOGPS logS -4.2 ALOGPS Water Solubility 1.63e-02 g/l ALOGPS logP 3.49 ChemAxon IUPAC Name (2R)-2-(4-chlorophenyl)-2-phenylethan-1-amine ChemAxon Traditional IUPAC Name (2R)-2-(4-chlorophenyl)-2-phenylethanamine ChemAxon Molecular Weight 231.721 ChemAxon Monoisotopic Weight 231.08147716 ChemAxon SMILES [H][C@@](CN)(C1=CC=CC=C1)C1=CC=C(Cl)C=C1 ChemAxon Molecular Formula C14H14ClN ChemAxon InChI InChI=1S/C14H14ClN/c15-13-8-6-12(7-9-13)14(10-16)11-4-2-1-3-5-11/h1-9,14H,10,16H2/t14-/m1/s1 ChemAxon InChIKey InChIKey=PNKKPFLBOWGVSF-CQSZACIVSA-N ChemAxon Polar Surface Area (PSA) 26.02 ChemAxon Refractivity 68.66 ChemAxon Polarizability 25.29 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 9.7 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 16122635 PubChem Substance 99444331 ChemSpider 17279548 PDB GVQ BE0003761 cAMP-dependent protein kinase catalytic subunit alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown cAMP-dependent protein kinase catalytic subunit alpha Involved in ATP binding Phosphorylates a large number of substrates in the cytoplasm and the nucleus PRKACA 19p13.1 Cytoplasm (By similarity). Nucleus (By similarity) None 9.22 40589.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9380 GeneCards PRKACA GenBank Gene Database X07767 GenBank Protein Database 35479 UniProtKB P17612 UniProt Accession KAPCA_HUMAN PKA C-alpha >cAMP-dependent protein kinase catalytic subunit alpha MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVML VKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF >1056 bp ATGGGCAACGCCGCCGCCGCCAAGAAGGGCAGCGAGCAGGAGAGCGTGAAAGAATTCTTA GCCAAAGCCAAAGAAGATTTTCTTAAAAAATGGGAAAGTCCCGCTCAGAACACAGCCCAC TTGGATCAGTTTGAACGAATCAAGACCCTCGGCACGGGCTCCTTCGGGCGGGTGATGCTG GTGAAACACAAGGAGACCGGGAACCACTATGCCATGAAGATCCTCGACAAACAGAAGGTG GTGAAACTGAAACAGATCGAACACACCCTGAATGAAAAGCGCATCCTGCAAGCTGTCAAC TTTCCGTTCCTCGTCAAACTCGAGTTCTCCTTCAAGGACAACTCAAACTTATACATGGTC ATGGAGTACGTGCCCGGCGGGGAGATGTTCTCACACCTACGGCGGATCGGAAGGTTCAGT GAGCCCCATGCCCGTTTCTACGCGGCCCAGATCGTCCTGACCTTTGAGTATCTGCACTCG CTGGATCTCATCTACAGGGACCTGAAGCCGGAGAATCTGCTCATTGACCAGCAGGGCTAC ATTCAGGTGACAGACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGC GGCACCCCTGAGTACCTGGCCCCTGAGATTATCCTGAGCAAAGGCTACAACAAGGCCGTG GACTGGTGGGCCCTGGGGGTTCTTATCTATGAAATGGCCGCTGGCTACCCGCCCTTCTTC GCAGACCAGCCCATCCAGATCTATGAGAAGATCGTCTCTGGGAAGGTGCGCTTCCCTTCC CACTTCAGCTCTGACTTGAAGGACCTGCTGCGGAACCTCCTGCAGGTAGATCTCACCAAG CGCTTTGGGAACCTCAAGAATGGGGTCAACGATATCAAGAACCACAAGTGGTTTGCCACA ACTGACTGGATTGCCATCTACCAGAGGAAGGTGGAAGCTCCCTTCATACCAAAGTTTAAA GGCCCTGGGGATACGAGTAACTTTGACGACTATGAGGAAGAAGAAATCCGGGTCTCCATC AATGAGAAGTGTGGCAAGGAGTTTTCTGAGTTTTAG PF00069 Pkinase function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process BE0003762 cAMP-dependent protein kinase inhibitor alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown cAMP-dependent protein kinase inhibitor alpha Involved in cAMP-dependent protein kinase inhibitor act Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains PKIA 8q21.12 None 4.18 7988.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9017 GeneCards PKIA GenBank Gene Database S76965 GenBank Protein Database 243494 UniProtKB P61925 UniProt Accession IPKA_HUMAN cAMP-dependent protein kinase inhibitor, muscle/brain isoform PKI-alpha >cAMP-dependent protein kinase inhibitor alpha MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSS TEQSGEAQGEAAKSES >231 bp ATGACTGATGTGGAAACTACATATGCAGATTTTATTGCTTCAGGAAGAACAGGTAGAAGA AATGCAATACATGATATCCTGGTTTCCTCTGCAAGTGGCAACAGCAATGAATTAGCCTTG AAATTAGCAGGTCTTGATATCAACAAGACAGAAGGTGAAGAAGATGCACAACGAAGTTCT ACAGAACAAAGTGGGGAAGCCCAGGGAGAAGCAGCAAAATCTGAAAGCTAA PF02827 PKI function enzyme regulator activity function enzyme inhibitor activity function kinase inhibitor activity function protein kinase inhibitor activity function cAMP-dependent protein kinase inhibitor activity process regulation of kinase activity process regulation of protein kinase activity process negative regulation of protein kinase activity process regulation of biological process process regulation of enzyme activity process regulation of transferase activity "
drug:(2R)-2-(4-CHLOROPHENYL)-2-PHENYLETHANAMINErdfs:label"(2R)-2-(4-CHLOROPHENYL)-2-PHENYLETHANAMINE"
drug:(2R)-2-(4-CHLOROPHENYL)-2-PHENYLETHANAMINErdf:typedrugbank:drugs
drug:(2R)-2-(4-CHLOROPHENYL)-2-[4-(1H-PYRAZOL-4-YL)PHENYL]ETHANAMINEdrugbank:description" experimental This compound belongs to the diphenylmethanes. These are compounds containing a diphenylmethane moiety, which consists of a methane wherein two hydrogen atoms are replaced by two phenyl groups. Diphenylmethanes Organic Compounds Benzenoids Benzene and Substituted Derivatives Diphenylmethanes Phenylpyrazoles Aromatic Monoterpenes Phenylpropylamines Chlorobenzenes Aryl Chlorides Polyamines Monoalkylamines Organochlorides phenylpyrazole aromatic monoterpene p-cymene monoterpene phenylpropylamine chlorobenzene aryl halide aryl chloride pyrazole azole polyamine organochloride amine organohalogen primary amine primary aliphatic amine organonitrogen compound logP 3.74 ALOGPS logS -5 ALOGPS Water Solubility 3.14e-03 g/l ALOGPS logP 3.44 ChemAxon IUPAC Name (2R)-2-(4-chlorophenyl)-2-[4-(1H-pyrazol-4-yl)phenyl]ethan-1-amine ChemAxon Traditional IUPAC Name (2R)-2-(4-chlorophenyl)-2-[4-(1H-pyrazol-4-yl)phenyl]ethanamine ChemAxon Molecular Weight 297.782 ChemAxon Monoisotopic Weight 297.103275234 ChemAxon SMILES [H][C@](CN)(C1=CC=C(Cl)C=C1)C1=CC=C(C=C1)C1=CNN=C1 ChemAxon Molecular Formula C17H16ClN3 ChemAxon InChI InChI=1S/C17H16ClN3/c18-16-7-5-14(6-8-16)17(9-19)13-3-1-12(2-4-13)15-10-20-21-11-15/h1-8,10-11,17H,9,19H2,(H,20,21)/t17-/m1/s1 ChemAxon InChIKey InChIKey=HWVGILTYGZFGLR-QGZVFWFLSA-N ChemAxon Polar Surface Area (PSA) 54.7 ChemAxon Refractivity 87.48 ChemAxon Polarizability 32.23 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 14.63 ChemAxon pKa (strongest basic) 9.68 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 15602983 PubChem Substance 99444328 ChemSpider 13078464 PDB GVN BE0003761 cAMP-dependent protein kinase catalytic subunit alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown cAMP-dependent protein kinase catalytic subunit alpha Involved in ATP binding Phosphorylates a large number of substrates in the cytoplasm and the nucleus PRKACA 19p13.1 Cytoplasm (By similarity). Nucleus (By similarity) None 9.22 40589.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9380 GeneCards PRKACA GenBank Gene Database X07767 GenBank Protein Database 35479 UniProtKB P17612 UniProt Accession KAPCA_HUMAN PKA C-alpha >cAMP-dependent protein kinase catalytic subunit alpha MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVML VKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF >1056 bp ATGGGCAACGCCGCCGCCGCCAAGAAGGGCAGCGAGCAGGAGAGCGTGAAAGAATTCTTA GCCAAAGCCAAAGAAGATTTTCTTAAAAAATGGGAAAGTCCCGCTCAGAACACAGCCCAC TTGGATCAGTTTGAACGAATCAAGACCCTCGGCACGGGCTCCTTCGGGCGGGTGATGCTG GTGAAACACAAGGAGACCGGGAACCACTATGCCATGAAGATCCTCGACAAACAGAAGGTG GTGAAACTGAAACAGATCGAACACACCCTGAATGAAAAGCGCATCCTGCAAGCTGTCAAC TTTCCGTTCCTCGTCAAACTCGAGTTCTCCTTCAAGGACAACTCAAACTTATACATGGTC ATGGAGTACGTGCCCGGCGGGGAGATGTTCTCACACCTACGGCGGATCGGAAGGTTCAGT GAGCCCCATGCCCGTTTCTACGCGGCCCAGATCGTCCTGACCTTTGAGTATCTGCACTCG CTGGATCTCATCTACAGGGACCTGAAGCCGGAGAATCTGCTCATTGACCAGCAGGGCTAC ATTCAGGTGACAGACTTCGGTTTCGCCAAGCGCGTGAAGGGCCGCACTTGGACCTTGTGC GGCACCCCTGAGTACCTGGCCCCTGAGATTATCCTGAGCAAAGGCTACAACAAGGCCGTG GACTGGTGGGCCCTGGGGGTTCTTATCTATGAAATGGCCGCTGGCTACCCGCCCTTCTTC GCAGACCAGCCCATCCAGATCTATGAGAAGATCGTCTCTGGGAAGGTGCGCTTCCCTTCC CACTTCAGCTCTGACTTGAAGGACCTGCTGCGGAACCTCCTGCAGGTAGATCTCACCAAG CGCTTTGGGAACCTCAAGAATGGGGTCAACGATATCAAGAACCACAAGTGGTTTGCCACA ACTGACTGGATTGCCATCTACCAGAGGAAGGTGGAAGCTCCCTTCATACCAAAGTTTAAA GGCCCTGGGGATACGAGTAACTTTGACGACTATGAGGAAGAAGAAATCCGGGTCTCCATC AATGAGAAGTGTGGCAAGGAGTTTTCTGAGTTTTAG PF00069 Pkinase function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process BE0003762 cAMP-dependent protein kinase inhibitor alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown cAMP-dependent protein kinase inhibitor alpha Involved in cAMP-dependent protein kinase inhibitor act Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains PKIA 8q21.12 None 4.18 7988.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9017 GeneCards PKIA GenBank Gene Database S76965 GenBank Protein Database 243494 UniProtKB P61925 UniProt Accession IPKA_HUMAN cAMP-dependent protein kinase inhibitor, muscle/brain isoform PKI-alpha >cAMP-dependent protein kinase inhibitor alpha MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSS TEQSGEAQGEAAKSES >231 bp ATGACTGATGTGGAAACTACATATGCAGATTTTATTGCTTCAGGAAGAACAGGTAGAAGA AATGCAATACATGATATCCTGGTTTCCTCTGCAAGTGGCAACAGCAATGAATTAGCCTTG AAATTAGCAGGTCTTGATATCAACAAGACAGAAGGTGAAGAAGATGCACAACGAAGTTCT ACAGAACAAAGTGGGGAAGCCCAGGGAGAAGCAGCAAAATCTGAAAGCTAA PF02827 PKI function enzyme regulator activity function enzyme inhibitor activity function kinase inhibitor activity function protein kinase inhibitor activity function cAMP-dependent protein kinase inhibitor activity process regulation of kinase activity process regulation of protein kinase activity process negative regulation of protein kinase activity process regulation of biological process process regulation of enzyme activity process regulation of transferase activity "
drug:(2R)-2-(4-CHLOROPHENYL)-2-[4-(1H-PYRAZOL-4-YL)PHENYL]ETHANAMINErdfs:label"(2R)-2-(4-CHLOROPHENYL)-2-[4-(1H-PYRAZOL-4-YL)PHENYL]ETHANAMINE"
drug:(2R)-2-(4-CHLOROPHENYL)-2-[4-(1H-PYRAZOL-4-YL)PHENYL]ETHANAMINErdf:typedrugbank:drugs
drug:(2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDEdrugbank:description" experimental This compound belongs to the morpholines. These are organic compounds containing a morpholine moiety, which consists of a six-member aliphatic saturated ring with the formula C4H9NO, where the oxygen and nitrogen atoms lie at positions 1 and 4, respectively. Morpholines Organic Compounds Heterocyclic Compounds Oxazinanes Morpholines Aryl Chlorides Pyrrolidones Thiophenes Sulfonyls Sulfonamides Tertiary Carboxylic Acid Amides Tertiary Amines Lactams Carboxylic Acids Ethers Enolates Polyamines Organochlorides sulfonic acid derivative sulfonyl tertiary carboxylic acid amide pyrrolidine thiophene sulfonamide tertiary amine lactam carboxamide group carboxylic acid derivative carboxylic acid polyamine ether enolate organohalogen organochloride amine organonitrogen compound logP 0.87 ALOGPS logS -3.8 ALOGPS Water Solubility 8.04e-02 g/l ALOGPS logP 0.69 ChemAxon IUPAC Name (1E)-2-(5-chlorothiophen-2-yl)-N-[(3S)-1-[(2S)-1-(morpholin-4-yl)-1-oxopropan-2-yl]-2-oxopyrrolidin-3-yl]prop-1-ene-1-sulfonamide ChemAxon Traditional IUPAC Name (1E)-2-(5-chlorothiophen-2-yl)-N-[(3S)-1-[(2S)-1-(morpholin-4-yl)-1-oxopropan-2-yl]-2-oxopyrrolidin-3-yl]prop-1-ene-1-sulfonamide ChemAxon Molecular Weight 461.983 ChemAxon Monoisotopic Weight 461.08458998 ChemAxon SMILES C\C(=C/S(=O)(=O)N[C@@]1([H])CCN([C@](C)([H])C(=O)N2CCOCC2)C1=O)C1=CC=C(Cl)S1 ChemAxon Molecular Formula C18H24ClN3O5S2 ChemAxon InChI InChI=1S/C18H24ClN3O5S2/c1-12(15-3-4-16(19)28-15)11-29(25,26)20-14-5-6-22(18(14)24)13(2)17(23)21-7-9-27-10-8-21/h3-4,11,13-14,20H,5-10H2,1-2H3/b12-11+/t13-,14-/m0/s1 ChemAxon InChIKey InChIKey=YMJHMJLNQLVUAV-GHYUOPHCSA-N ChemAxon Polar Surface Area (PSA) 96.02 ChemAxon Refractivity 109.64 ChemAxon Polarizability 46.39 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 9.05 ChemAxon pKa (strongest basic) -3.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 10095865 PubChem Substance 99443682 ChemSpider 8271400 PDB 701 BE0000048 Prothrombin Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Prothrombin Involved in blood clotting cascade Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C F2 11p11-q12 Secreted protein; extracellular space None 5.7 70037.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3535 GenAtlas F2 GeneCards F2 GenBank Gene Database M17262 GenBank Protein Database 339641 UniProtKB P00734 UniProt Accession THRB_HUMAN Activated Factor II [IIa] Coagulation factor II EC 3.4.21.5 Prothrombin precursor Thrombin >Prothrombin precursor MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY GFYTHVFRLKKWIQKVIDQFGE >1869 bp ATGGCGCACGTCCGAGGCTTGCAGCTGCCTGGCTGCCTGGCCCTGGCTGCCCTGTGTAGC CTTGTGCACAGCCAGCATGTGTTCCTGGCTCCTCAGCAAGCACGGTCGCTGCTCCAGCGG GTCCGGCGAGCCAACACCTTCTTGGAGGAGGTGCGCAAGGGCAACCTAGAGCGAGAGTGC GTGGAGGAGACGTGCAGCTACGAGGAGGCCTTCGAGGCTCTGGAGTCCTCCACGGCTACG GATGTGTTCTGGGCCAAGTACACAGCTTGTGAGACAGCGAGGACGCCTCGAGATAAGCTT GCTGCATGTCTGGAAGGTAACTGTGCTGAGGGTCTGGGTACGAACTACCGAGGGCATGTG AACATCACCCGGTCAGGCATTGAGTGCCAGCTATGGAGGAGTCGCTACCCACATAAGCCT GAAATCAACTCCACTACCCATCCTGGGGCCGACCTACAGGAGAATTTCTGCCGCAACCCC GACAGCAGCACCACGGGACCCTGGTGCTACACTACAGACCCCACCGTGAGGAGGCAGGAA TGCAGCATCCCTGTCTGTGGCCAGGATCAAGTCACTGTAGCGATGACTCCACGCTCCGAA GGCTCCAGTGTGAATCTGTCACCTCCATTGGAGCAGTGTGTCCCTGATCGGGGGCAGCAG TACCAGGGGCGCCTGGCGGTGACCACACATGGGCTCCCCTGCCTGGCCTGGGCCAGCGCA CAGGCCAAGGCCCTGAGCAAGCACCAGGACTTCAACTCAGCTGTGCAGCTGGTGGAGAAC TTCTGCCGCAACCCAGACGGGGATGAGGAGGGCGTGTGGTGCTATGTGGCCGGGAAGCCT GGCGACTTTGGGTACTGCGACCTCAACTATTGTGAGGAGGCCGTGGAGGAGGAGACAGGA GATGGGCTGGATGAGGACTCAGACAGGGCCATCGAAGGGCGTACCGCCACCAGTGAGTAC CAGACTTTCTTCAATCCGAGGACCTTTGGCTCGGGAGAGGCAGACTGTGGGCTGCGACCT CTGTTCGAGAAGAAGTCGCTGGAGGACAAAACCGAAAGAGAGCTCCTGGAATCCTACATC GACGGGCGCATTGTGGAGGGCTCGGATGCAGAGATCGGCATGTCACCTTGGCAGGTGATG CTTTTCCGGAAGAGTCCCCAGGAGCTGCTGTGTGGGGCCAGCCTCATCAGTGACCGCTGG GTCCTCACCGCCGCCCACTGCCTCCTGTACCCGCCCTGGGACAAGAACTTCACCGAGAAT GACCTTCTGGTGCGCATTGGCAAGCACTCCCGCACAAGGTACGAGCGAAACATTGAAAAG ATATCCATGTTGGAAAAGATCTACATCCACCCCAGGTACAACTGGCGGGAGAACCTGGAC CGGGACATTGCCCTGATGAAGCTGAAGAAGCCTGTTGCCTTCAGTGACTACATTCACCCT GTGTGTCTGCCCGACAGGGAGACGGCAGCCAGCTTGCTCCAGGCTGGATACAAGGGGCGG GTGACAGGCTGGGGCAACCTGAAGGAGACGTGGACAGCCAACGTTGGTAAGGGGCAGCCC AGTGTCCTGCAGGTGGTGAACCTGCCCATTGTGGAGCGGCCGGTCTGCAAGGACTCCACC CGGATCCGCATCACTGACAACATGTTCTGTGCTGGTTACAAGCCTGATGAAGGGAAACGA GGGGATGCCTGTGAAGGTGACAGTGGGGGACCCTTTGTCATGAAGAGCCCCTTTAACAAC CGCTGGTATCAAATGGGCATCGTCTCATGGGGTGAAGGCTGTGACCGGGATGGGAAATAT GGCTTCTACACACATGTGTTCCGCCTGAAGAAGTGGATACAGAAGGTCATTGATCAGTTT GGAGAGTAG PF00594 Gla PF00051 Kringle PF00089 Trypsin component extracellular region function catalytic activity function thrombin activity function hydrolase activity function calcium ion binding function peptidase activity function ion binding function endopeptidase activity function cation binding function serine-type endopeptidase activity function binding process blood coagulation process metabolism process macromolecule metabolism process protein metabolism process proteolysis process cellular protein metabolism process organismal physiological process process regulation of body fluids process physiological process process hemostasis BE0000216 Coagulation factor X Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Coagulation factor X Involved in calcium ion binding Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting F10 13q34 Cytoplasmic 7-26 5.74 54732.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3528 GenAtlas F10 GeneCards F10 GenBank Gene Database K03194 GenBank Protein Database 182841 UniProtKB P00742 UniProt Accession FA10_HUMAN Coagulation factor X precursor EC 3.4.21.6 Stuart factor Stuart- Prower factor >Coagulation factor X precursor MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEE TCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKN CELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERR KRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQE CKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGE AVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGI VSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSG GPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPE VITSSPLK >1433 bp CCTCCCTGGCTGGCCTCCTGCTGCTCGGGGAAAGTCTGTTCATCCGCAGGGAGCAGGCCA ACAACATCCTGGCGAGGGTCACGAGGGCCAATTCCTTTCTTGAAGAGATGAAGAAAGGAC ACCTCGAAAGAGAGTGCATGGAAGAGACCTGCTCATACGAAGAGGCCCGCGAGGTCTTTG AGGACAGCGACAAGACGAATGAATTCTGGAATAAATACAAAGATGGCGACCAGTGTGAGA CCAGTCCTTGCCAGAACCAGGGCAAATGTAAAGACGGCCTCGGGGAATACACCTGCACCT GTTTAGAAGGATTCGAAGGCAAAAACTGTGAATTATTCACACGGAAGCTCTGCAGCCTGG ACAACGGGGACTGTGACCAGTTCTGCCACGAGGAACAGAACTCTGTGGTGTGCTCCTGCG CCCGCGGGTACACCCTGGCTGACAACGGCAAGGCCTGCATTCCCACAGGGCCCTACCCCT GTGGGAAACAGACCCTGGAACGCAGGAAGAGGTCAGTGGCCCAGGCCACCAGCAGCAGCG GGGAGGCCCCTGACAGCATCACATGGAAGCCATATGATGCAGCCGACCTGGACCCCACCG AGAACCCCTTCGACCTGCTTGACTTCAACCAGACGCAGCCTGAGAGGGGCGACAACAACC TCACCAGGATCGTGGGAGGCCAGGAATGCAAGGACGGGGAGTGTCCCTGGCAGGCCCTGC TCATCAATGAGGAAAACGAGGGTTTCTGTGGTGGAACTATTCTGAGCGAGTTCTACATCC TAACGGCAGCCCACTGTCTCTACCAAGCCAAGAGATTCAAGGTGAGGGTAGGGGACCGGA ACACGGAGCAGGAGGAGGGCGGTGAGGCGGTGCACGAGGTGGAGGTGGTCATCAAGCACA ACCGGTTCACAAAGGAGACCTATGACTTCGACATCGCCGTGCTCCGGCTCAAGACCCCCA TCACCTTCCGCATGAACGTGGCGCCTGCCTGCCTCCCCGAGCGTGACTGGGCCGAGTCCA CGCTGATGACGCAGAAGACGGGGATTGTGAGCGGCTTCGGGCGCACCCACGAGAAGGGCC GGCAGTCCACCAGGCTCAAGATGCTGGAGGTGCCCTACGTGGACCGCAACAGCTGCAAGC TGTCCAGCAGCTTCATCATCACCCAGAACATGTTCTGTGCCGGCTACGACACCAAGCAGG AGGATGCCTGCCAGGGGGACAGCGGGGGCCCGCACGTCACCCGCTTCAAGGACACCTACT TCGTGACAGGCATCGTCAGCTGGGGAGAGAGCTGTGCCCGTAAGGGGAAGTACGGGATCT ACACCAAGGTCACCGCCTTCCTCAAGTGGATCGACAGGTCCATGAAAACCAGGGGCTTGC CCAAGGCCAAGAGCCATGCCCCGGAGGTCATAACGTCCTCTCCATTAAAGTGA PF00008 EGF PF00594 Gla PF00089 Trypsin component extracellular region function calcium ion binding function hydrolase activity function peptidase activity function endopeptidase activity function ion binding function serine-type endopeptidase activity function cation binding function binding function catalytic activity process metabolism process macromolecule metabolism process proteolysis process protein metabolism process cellular protein metabolism process organismal physiological process process regulation of body fluids process physiological process process hemostasis process blood coagulation "
drug:(2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDErdfs:label"(2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE"
drug:(2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDErdf:typedrugbank:drugs
drug:(2R)-2-(7-carbamoyl-1H-benzimidazol-2-yl)-2-methylpyrrolidiniumdrugbank:description" experimental This compound belongs to the benzimidazoles. These are organic compounds containing a benzene ring fused to an imidazole ring (five member ring containing a nitrogen atom, 4 carbon atoms, and two double bonds). Benzimidazoles Organic Compounds Heterocyclic Compounds Benzimidazoles Benzamides Benzoyl Derivatives Pyrrolidines Imidazoles Primary Carboxylic Acid Amides Dialkylamines Carboxylic Acids Polyamines Enolates benzoyl benzene pyrrolidine imidazole azole carboxamide group primary carboxylic acid amide secondary aliphatic amine carboxylic acid derivative secondary amine carboxylic acid enolate polyamine amine organonitrogen compound logP 1.1 ALOGPS logS -3 ALOGPS Water Solubility 2.75e-01 g/l ALOGPS logP 0.18 ChemAxon IUPAC Name 2-[(2R)-2-methylpyrrolidin-2-yl]-1H-1,3-benzodiazole-7-carboxamide ChemAxon Traditional IUPAC Name 2-[(2R)-2-methylpyrrolidin-2-yl]-3H-1,3-benzodiazole-4-carboxamide ChemAxon Molecular Weight 244.2923 ChemAxon Monoisotopic Weight 244.132411154 ChemAxon SMILES C[C@@]1(CCCN1)C1=NC2=CC=CC(C(N)=O)=C2N1 ChemAxon Molecular Formula C13H16N4O ChemAxon InChI InChI=1S/C13H16N4O/c1-13(6-3-7-15-13)12-16-9-5-2-4-8(11(14)18)10(9)17-12/h2,4-5,15H,3,6-7H2,1H3,(H2,14,18)(H,16,17)/t13-/m1/s1 ChemAxon InChIKey InChIKey=JNAHVYVRKWKWKQ-CYBMUJFWSA-N ChemAxon Polar Surface Area (PSA) 83.8 ChemAxon Refractivity 68.62 ChemAxon Polarizability 26.31 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 9.21 ChemAxon pKa (strongest basic) 8.97 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11960529 PubChem Substance 99443703 ChemSpider 10134775 PDB 78P BE0001717 Poly [ADP-ribose] polymerase 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Poly [ADP-ribose] polymerase 1 Involved in DNA binding Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks PARP1 1q41-q42 Nucleus None 9.34 113085.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:270 GenAtlas PARP1 GeneCards PARP1 GenBank Gene Database X16674 GenBank Protein Database 1017423 UniProtKB P09874 UniProt Accession PARP1_HUMAN ADPRT EC 2.4.2.30 NAD(+) ADP-ribosyltransferase 1 PARP-1 Poly[ADP-ribose] synthetase 1 >Poly [ADP-ribose] polymerase 1 MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKV GHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKS NRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQ LKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKA QNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSG QLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPE TSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLT GTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSP WGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLE HSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNK LEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPG TKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAV SQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRG GSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIE REGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSA NISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW >3045 bp ATGGCGGAGTCTTCGGATAAGCTCTATCGAGTCGAGTACGCCAAGAGCGGGCGCGCCTCT TGCAAGAAATGCAGCGAGAGCATCCCCAAGGACTCGCTCCGGATGGCCATCATGGTGCAG TCGCCCATGTTTGATGGAAAAGTCCCACACTGGTACCACTTCTCCTGCTTCTGGAAGGTG GGCCACTCCATCCGGCACCCTGACGTTCAGGTGGATGGGTTCTCTGAGCTTCGGTGGGAT GACCAGCAGAAAGTCAAGAAGACAGCGGAAGCTGGAGGAGTGACAGGCAAAGGCCAGGAT GGAATTGGTAGCAAGGCAGAGAAGACTCTGGGTGACTTTGCAGCAGAGTATGCCAAGTCC AACAGAAGTACGTGCAAGGGGTGTATGGAGAAGATAGAAAAGGGCCAGGTGCGCCTGTCC AAGAAGATGGTGGACCCGGAGAAGCCACAGCTAGGCATGATTGACCGCTGGTACCATCCA GGCTGCTTTGTCAAGAACAGGGAGGAGCTGGGTTTCCGGCCCGAGTACAGTGCGAGTCAG CTCAAGGGCTTCAGCCTCCTTGCTACAGAGGATAAAGAAGCCCTGAAGAAGCAGCTCCCA GGAGTCAAGAGTGAAGGAAAGAGAAAAGGCGATGAGGTGGATGGAGTGGATGAAGTGGCG AAGAAGAAATCTAAAAAAGAAAAAGACAAGGATAGTAAGCTTGAAAAAGCCCTAAAGGCT CAGAACGACCTGATCTGGAACATCAAGGACGAGCTAAAGAAAGTGTGTTCAACTAATGAC CTGAAGGAGCTACTCATCTTCAACAAGCAGCAAGTGCCTTCTGGGGAGTCGGCGATCTTG GACCGAGTAGCTGATGGCATGGTGTTCGGTGCCCTCCTTCCCTGCGAGGAATGCTCGGGT CAGCTGGTCTTCAAGAGCGATGCCTATTACTGCACTGGGGACGTCACTGCCTGGACCAAG TGTATGGTCAAGACACAGACACCCAACCGGAAGGAGTGGGTAACCCCAAAGGAATTCCGA GAAATCTCTTACCTCAAGAAATTGAAGGTTAAAAAGCAGGACCGTATATTCCCCCCAGAA ACCAGCGCCTCCGTGGCGGCCACGCCTCCGCCCTCCACAGCCTCGGCTCCTGCTGCTGTG AACTCCTCTGCTTCAGCAGATAAGCCATTATCCAACATGAAGATCCTGACTCTCGGGAAG CTGTCCCGGAACAAGGATGAAGTGAAGGCCATGATTGAGAAACTCGGGGGGAAGTTGACG GGGACGGCCAACAAGGCTTCCCTGTGCATCAGCACCAAAAAGGAGGTGGAAAAGATGAAT AAGAAGATGGAGGAAGTAAAGGAAGCCAACATCCGAGTTGTGTCTGAGGACTTCCTCCAG GACGTCTCCGCCTCCACCAAGAGCCTTCAGGAGTTGTTCTTAGCGCACATCTTGTCCCCT TGGGGGGCAGAGGTGAAGGCAGAGCCTGTTGAAGTTGTGGCCCCAAGAGGGAAGTCAGGG GCTGCGCTCTCCAAAAAAAGCAAGGGCCAGGTCAAGGAGGAAGGTATCAACAAATCTGAA AAGAGAATGAAATTAACTCTTAAAGGAGGAGCAGCTGTGGATCCTGATTCTGGACTGGAA CACTCTGCGCATGTCCTGGAGAAAGGTGGGAAGGTCTTCAGTGCCACCCTTGGCCTGGTG GACATCGTTAAAGGAACCAACTCCTACTACAAGCTGCAGCTTCTGGAGGACGACAAGGAA AACAGGTATTGGATATTCAGGTCCTGGGGCCGTGTGGGTACGGTGATCGGTAGCAACAAA CTGGAACAGATGCCGTCCAAGGAGGATGCCATTGAGCACTTCATGAAATTATATGAAGAA AAAACCGGGAACGCTTGGCACTCCAAAAATTTCACGAAGTATCCCAAAAAGTTCTACCCC CTGGAGATTGACTATGGCCAGGATGAAGAGGCAGTGAAGAAGCTGACAGTAAATCCTGGC ACCAAGTCCAAGCTCCCCAAGCCAGTTCAGGACCTCATCAAGATGATCTTTGATGTGGAA AGTATGAAGAAAGCCATGGTGGAGTATGAGATCGACCTTCAGAAGATGCCCTTGGGGAAG CTGAGCAAAAGGCAGATCCAGGCCGCATACTCCATCCTCAGTGAGGTCCAGCAGGCGGTG TCTCAGGGCAGCAGCGACTCTCAGATCCTGGATCTCTCAAATCGCTTTTACACCCTGATC CCCCACGACTTTGGGATGAAGAAGCCTCCGCTCCTGAACAATGCAGACAGTGTGCAGGCC AAGGTGGAAATGCTTGACAACCTGCTGGACATCGAGGTGGCCTACAGTCTGCTCAGGGGA GGGTCTGATGATAGCAGCAAGGATCCCATCGATGTCAACTATGAGAAGCTCAAAACTGAC ATTAAGGTGGTTGACAGAGATTCTGAAGAAGCCGAGATCATCAGGAAGTATGTTAAGAAC ACTCATGCAACCACACACAATGCGTATGACTTGGAAGTCATCGATATCTTTAAGATAGAG CGTGAAGGCGAATGCCAGCGTTACAAGCCCTTTAAGCAGCTTCATAACCGAAGATTGCTG TGGCACGGGTCCAGGACCACCAACTTTGCTGGGATCCTGTCCCAGGGTCTTCGGATAGCC CCGCCTGAAGCGCCCGTGACAGGCTACATGTTTGGTAAAGGGATCTATTTCGCTGACATG GTCTCCAAGAGTGCCAACTACTGCCATACGTCTCAGGGAGACCCAATAGGCTTAATCCTG TTGGGAGAAGTTGCCCTTGGAAACATGTATGAACTGAAGCACGCTTCACATATCAGCAAG TTACCCAAGGGCAAGCACAGTGTCAAAGGTTTGGGCAAAACTACCCCTGATCCTTCAGCT AACATTAGTCTGGATGGTGTAGACGTTCCTCTTGGGACCGGGATTTCATCTGGTGTGAAT GACACCTCTCTACTATATAACGAGTACATTGTCTATGATATTGCTCAGGTAAATCTGAAG TATCTGCTGAAACTGAAATTCAATTTTAAGACCTCCCTGTGGTAA PF00645 zf-PARP PF00644 PARP PF00533 BRCT PF08063 PADR1 PF02877 PARP_reg PF05406 WGR component nucleus component cell component intracellular component organelle component membrane-bound organelle component intracellular membrane-bound organelle function transferase activity, transferring pentosyl groups function DNA binding function transferase activity function transferase activity, transferring glycosyl groups function binding function NAD+ ADP-ribosyltransferase activity function catalytic activity function nucleic acid binding process biopolymer modification process protein modification process DNA metabolism process protein amino acid ADP-ribosylation process physiological process process metabolism process cellular metabolism process macromolecule metabolism process biopolymer metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism BE0003798 Poly [ADP-ribose] polymerase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Poly [ADP-ribose] polymerase 2 Involved in DNA binding Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks PARP2 14q11.2-q12 Nucleus None 9.22 66205.3 Human HUGO Gene Nomenclature Committee (HGNC) GNC:272 GeneCards PARP2 GenBank Gene Database AJ236912 GenBank Protein Database 6688130 UniProtKB Q9UGN5 UniProt Accession PARP2_HUMAN hPARP-2 NAD(+) ADP-ribosyltransferase 2 pADPRT-2 PARP-2 Poly[ADP-ribose] synthetase 2 >Poly [ADP-ribose] polymerase 2 MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKD RTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLN QTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKF LDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQE LIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALME ACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQ HYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDL HNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLK NTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGP ASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW >1713 bp ATGGCGGCGCGGCGGCGACGGAGCACCGGCGGCGGCAGGGCGAGAGCATTAAATGAAAGC AAAAGAGTTAATAATGGCAACACGGCTCCAGAAGACTCTTCCCCTGCCAAGAAAACTCGT AGATGCCAGAGACAGGAGTCGAAAAAGATGCCTGTGGCTGGAGGAAAAGCTAATAAGGAC AGGACAGAAGACAAGCAAGATGAATCTGTGAAGGCCTTGCTGTTAAAGGGCAAAGCTCCT GTGGACCCAGAGTGTACAGCCAAGGTGGGGAAGGCTCATGTGTATTGTGAAGGAAATGAT GTCTATGATGTCATGCTAAATCAGACCAATCTCCAGTTCAACAACAACAAGTACTATCTG ATTCAGCTATTAGAAGATGATGCCCAGAGGAACTTCAGTGTTTGGATGAGATGGGGCCGA GTTGGGAAAATGGGACAGCACAGCCTGGTGGCTTGTTCAGGCAATCTCAACAAGGCCAAG GAAATCTTTCAGAAGAAATTCCTTGACAAAACGAAAAACAATTGGGAAGATCGAGAAAAG TTTGAGAAGGTGCCTGGAAAATATGATATGCTACAGATGGACTATGCCACCAATACTCAG GATGAAGAGGAAACAAAGAAAGAGGAATCTCTTAAATCTCCCTTGAAGCCAGAGTCACAG CTAGATCTTCGGGTACAGGAGTTAATAAAGTTGATCTGTAATGTTCAGGCCATGGAAGAA ATGATGATGGAAATGAAGTATAATACCAAGAAAGCCCCACTTGGGAAGCTGACAGTGGCA CAAATCAAGGCAGGTTACCAGTCTCTTAAGAAGATTGAGGATTGTATTCGGGCTGGCCAG CATGGACGAGCTCTCATGGAAGCATGCAATGAATTCTACACCAGGATTCCGCATGACTTT GGACTCCGTACTCCTCCACTAATCCGGACACAGAAGGAACTGTCAGAAAAAATACAATTA CTAGAGGCTTTGGGAGACATTGAAATTGCTATTAAGCTGGTGAAAACAGAGCTACAAAGC CCAGAACACCCATTGGACCAACACTATAGAAACCTACATTGTGCCTTGCGCCCCCTTGAC CATGAAAGTTATGAGTTCAAAGTGATTTCCCAGTACCTACAATCTACCCATGCTCCCACA CACAGCGACTATACCATGACCTTGCTGGATTTGTTTGAAGTGGAGAAGGATGGTGAGAAA GAAGCCTTCAGAGAGGACCTTCATAACAGGATGCTTCTATGGCATGGTTCCAGGATGAGT AACTGGGTGGGAATCTTGAGCCATGGGCTTCGAATTGCCCCACCTGAAGCTCCCATCACA GGTTACATGTTTGGGAAAGGAATCTACTTTGCTGACATGTCTTCCAAGAGTGCCAATTAC TGCTTTGCCTCTCGCCTAAAGAATACAGGACTGCTGCTCTTATCAGAGGTAGCTCTAGGT CAGTGTAATGAACTACTAGAGGCCAATCCTAAGGCCGAAGGATTGCTTCAAGGTAAACAT AGCACCAAGGGGCTGGGCAAGATGGCTCCCAGTTCTGCCCACTTCGTCACCCTGAATGGG AGTACAGTGCCATTAGGACCAGCAAGTGACACAGGAATTCTGAATCCAGATGGTTATACC CTCAACTACAATGAATATATTGTATATAACCCCAACCAGGTCCGTATGCGGTACCTTTTA AAGGTTCAGTTTAATTTCCTTCAGCTGTGGTGA PF00644 PARP PF02877 PARP_reg PF05406 WGR component organelle component membrane-bound organelle component intracellular membrane-bound organelle component nucleus function transferase activity function transferase activity, transferring glycosyl groups function catalytic activity function transferase activity, transferring pentosyl groups function NAD+ ADP-ribosyltransferase activity process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism process protein amino acid ADP-ribosylation process biopolymer metabolism "
drug:(2R)-2-(7-carbamoyl-1H-benzimidazol-2-yl)-2-methylpyrrolidiniumrdfs:label"(2R)-2-(7-carbamoyl-1H-benzimidazol-2-yl)-2-methylpyrrolidinium"
drug:(2R)-2-(7-carbamoyl-1H-benzimidazol-2-yl)-2-methylpyrrolidiniumrdf:typedrugbank:drugs
drug:(2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-oldrugbank:description" experimental This compound belongs to the phenylpyridines. These are polycyclic aromatic compounds containing a benzene ring linked to a pyridine ring through a CC or CN bond. Phenylpyridines Organic Compounds Heterocyclic Compounds Pyridines and Derivatives Phenylpyridines Purines and Purine Derivatives Aminopyrimidines and Derivatives N-substituted Imidazoles Benzene and Substituted Derivatives 1,2-Aminoalcohols Polyamines Primary Alcohols Secondary Amines purine imidazopyrimidine aminopyrimidine pyrimidine benzene n-substituted imidazole azole imidazole 1,2-aminoalcohol primary alcohol polyamine secondary amine amine alcohol organonitrogen compound logP 4.24 ALOGPS logS -4.4 ALOGPS Water Solubility 1.77e-02 g/l ALOGPS logP 3.71 ChemAxon IUPAC Name (2R)-2-{[9-(propan-2-yl)-6-({[4-(pyridin-2-yl)phenyl]methyl}amino)-9H-purin-2-yl]amino}butan-1-ol ChemAxon Traditional IUPAC Name (2R)-2-{[9-isopropyl-6-({[4-(pyridin-2-yl)phenyl]methyl}amino)purin-2-yl]amino}butan-1-ol ChemAxon Molecular Weight 431.5334 ChemAxon Monoisotopic Weight 431.243358585 ChemAxon SMILES [H][C@@](CC)(CO)NC1=NC2=C(N=CN2C(C)C)C(NCC2=CC=C(C=C2)C2=CC=CC=N2)=N1 ChemAxon Molecular Formula C24H29N7O ChemAxon InChI InChI=1S/C24H29N7O/c1-4-19(14-32)28-24-29-22(21-23(30-24)31(15-27-21)16(2)3)26-13-17-8-10-18(11-9-17)20-7-5-6-12-25-20/h5-12,15-16,19,32H,4,13-14H2,1-3H3,(H2,26,28,29,30)/t19-/m1/s1 ChemAxon InChIKey InChIKey=HOCBJBNQIQQQGT-LJQANCHMSA-N ChemAxon Polar Surface Area (PSA) 100.78 ChemAxon Refractivity 128.75 ChemAxon Polarizability 49.6 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 14.34 ChemAxon pKa (strongest basic) 5.58 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 10224714 PubChem Substance 99444934 ChemSpider 8400205 PDB RC8 BE0001072 Cyclin-dependent kinase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cyclin-dependent kinase 2 Involved in protein kinase activity ATP + a protein = ADP + a phosphoprotein CDK2deltaT None 9.76 30061.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1771 GenAtlas CDK2deltaT GeneCards CDK2deltaT GenBank Gene Database AB012305 GenBank Protein Database 3551191 UniProtKB P24941 UniProt Accession CDK2_HUMAN EC 2.7.11.22 p33 protein kinase >Cell division protein kinase 2 MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL >897 bp ATGGAGAACTTCCAAAAGGTGGAAAAGATCGGAGAGGGCACGTACGGAGTTGTGTACAAA GCCAGAAACAAGTTGACGGGAGAGGTGGTGGCGCTTAAGAAAATCCGCCTGGACACTGAG ACTGAGGGTGTGCCCAGTACTGCCATCCGAGAGATCTCTCTGCTTAAGGAGCTTAACCAT CCTAATATTGTCAAGCTGCTGGATGTCATTCACACAGAAAATAAACTCTACCTGGTTTTT GAATTTCTGCACCAAGATCTCAAGAAATTCATGGATGCCTCTGCTCTCACTGGCATTCCT CTTCCCCTCATCAAGAGCTATCTGTTCCAGCTGCTCCAGGGCCTAGCTTTCTGCCATTCT CATCGGGTCCTCCACCGAGACCTTAAACCTCAGAATCTGCTTATTAACACAGAGGGGGCC ATCAAGCTAGCAGACTTTGGACTAGCCAGAGCTTTTGGAGTCCCTGTTCGTACTTACACC CATGAGGTGGTGACCCTGTGGTACCGAGCTCCTGAAATCCTCCTGGGCTCGAAATATTAT TCCACAGCTGTGGACATCTGGAGCCTGGGCTGCATCTTTGCTGAGATGGTGACTCGCCGG GCCCTGTTCCCTGGAGATTCTGAGATTGACCAGCTCTTCCGGATCTTTCGGACTCTGGGG ACCCCAGATGAGGTGGTGTGGCCAGGAGTTACTTCTATGCCTGATTACAAGCCAAGTTTC CCCAAGTGGGCCCGGCAAGATTTTAGTAAAGTTGTACCTCCCCTGGATGAAGATGGACGG AGCTTGTTATCGCAAATGCTGCACTACGACCCTAACAAGCGGATTTCGGCCAAGGCAGCC CTGGCTCACCCTTTCTTCCAGGATGTGACCAAGCCAGTACCCCATCTTCGACTCTGA PF00069 Pkinase function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism BE0003734 Cyclin-A2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cyclin-A2 Involved in protein binding Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions CCNA2 4q25-q31 Nucleus. Cytoplasm None 6.52 48536.3 Human HUGO Gene Nomenclature Committee (HGNC) GNC:1578 GeneCards CCNA2 GenBank Gene Database X51688 GenBank Protein Database 30307 UniProtKB P20248 UniProt Accession CCNA2_HUMAN Cyclin-A >Cyclin-A2 MLGNSAPGPATREAGSALLALQQTALQEDQENINPEKAAPVQQPRTRAALAVLKSGNPRG LAQQQRPKTRRVAPLKDLPVNDEHVTVPPWKANSKQPAFTIHVDEAEKEAQKKPAESQKI EREDALAFNSAISLPGPRKPLVPLDYPMDGSFESPHTMDMSIVLEDEKPVSVNEVPDYHE DIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYID RFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLK VLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLPSVIAGAAF HLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNSKYHG VSLLNPPETLNL >1299 bp ATGTTGGGCAACTCTGCGCCGGGGCCTGCGACCCGCGAGGCGGGCTCGGCGCTGCTAGCA TTGCAGCAGACGGCGCTCCAAGAGGACCAGGAGAATATCAACCCGGAAAAGGCAGCGCCC GTCCAACAACCGCGGACCCGGGCCGCGCTGGCGGTACTGAAGTCCGGGAACCCGCGGGGT CTAGCGCAGCAGCAGAGGCCGAAGACGAGACGGGTTGCACCCCTTAAGGATCTTCCTGTA AATGATGAGCATGTCACCGTTCCTCCTTGGAAAGCAAACAGTAAACAGCCTGCGTTCACC ATTCATGTGGATGAAGCAGAAAAAGAAGCTCAGAAGAAGCCAGCTGAATCTCAAAAAATA GAGCGTGAAGATGCCCTGGCTTTTAATTCAGCCATTAGTTTACCTGGACCCAGAAAACCA TTGGTCCCTCTTGATTATCCAATGGATGGTAGTTTTGAGTCACCACATACTATGGACATG TCAATTGTATTAGAAGATGAAAAGCCAGTGAGTGTTAATGAAGTACCAGACTACCATGAG GATATTCACACATACCTTAGGGAAATGGAGGTTAAATGTAAACCTAAAGTGGGTTACATG AAGAAACAGCCAGACATCACTAACAGTATGAGAGCTATCCTCGTGGACTGGTTAGTTGAA GTAGGAGAAGAATATAAACTACAGAATGAGACCCTGCATTTGGCTGTGAACTACATTGAT AGGTTCCTGTCTTCCATGTCAGTGCTGAGAGGAAAACTTCAGCTTGTGGGCACTGCTGCT ATGCTGTTAGCCTCAAAGTTTGAAGAAATATACCCCCCAGAAGTAGCAGAGTTTGTGTAC ATTACAGATGATACCTACACCAAGAAACAAGTTCTGAGAATGGAGCATCTAGTTTTGAAA GTCCTTACTTTTGACTTAGCTGCTCCAACAGTAAATCAGTTTCTTACCCAATACTTTCTG CATCAGCAGCCTGCAAACTGCAAAGTTGAAAGTTTAGCAATGTTTTTGGGAGAATTAAGT TTGATAGATGCTGACCCATACCTCAAGTATTTGCCATCAGTTATTGCTGGAGCTGCCTTT CATTTAGCACTCTACACAGTCACGGGACAAAGCTGGCCTGAATCATTAATACGAAAGACT GGATATACCCTGGAAAGTCTTAAGCCTTGTCTCATGGACCTTCACCAGACCTACCTCAAA GCACCACAGCATGCACAACAGTCAATAAGAGAAAAGTACAAAAATTCAAAGTATCATGGT GTTTCTCTCCTCAACCCACCAGAGACACTAAATCTGTAA PF02984 Cyclin_C PF00134 Cyclin_N component intracellular membrane-bound organelle component nucleus component organelle component membrane-bound organelle process regulation of biological process process regulation of physiological process process regulation of cellular physiological process process regulation of cell cycle process regulation of progression through cell cycle "
drug:(2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-olrdfs:label"(2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol"
drug:(2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-olrdf:typedrugbank:drugs
drug:(2R)-2-AMINO-3,3,3-TRIFLUORO-N-HYDROXY-2-{[(4-PHENOXYPHENYL)SULFONYL]METHYL}PROPANAMIDEdrugbank:description" experimental This compound belongs to the alpha amino acid amides. These are amide derivatives of alpha amino acids. Alpha Amino Acid Amides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Diarylethers Phenol Ethers Sulfones Sulfoxides Hydroxamic Acids Enolates Polyamines Organofluorides Monoalkylamines Alkyl Fluorides phenol ether benzene sulfone sulfonyl sulfoxide hydroxamic acid carboxamide group ether enolate polyamine organonitrogen compound amine organofluoride organohalogen primary amine primary aliphatic amine alkyl halide alkyl fluoride logP 2.4 ALOGPS logS -4.2 ALOGPS Water Solubility 2.58e-02 g/l ALOGPS logP 1.58 ChemAxon IUPAC Name (2R)-2-amino-3,3,3-trifluoro-N-hydroxy-2-{[(4-phenoxybenzene)sulfonyl]methyl}propanamide ChemAxon Traditional IUPAC Name (2R)-2-amino-3,3,3-trifluoro-N-hydroxy-2-[(4-phenoxybenzenesulfonyl)methyl]propanamide ChemAxon Molecular Weight 404.361 ChemAxon Monoisotopic Weight 404.065376905 ChemAxon SMILES N[C@](CS(=O)(=O)C1=CC=C(OC2=CC=CC=C2)C=C1)(C(=O)NO)C(F)(F)F ChemAxon Molecular Formula C16H15F3N2O5S ChemAxon InChI InChI=1S/C16H15F3N2O5S/c17-16(18,19)15(20,14(22)21-23)10-27(24,25)13-8-6-12(7-9-13)26-11-4-2-1-3-5-11/h1-9,23H,10,20H2,(H,21,22)/t15-/m1/s1 ChemAxon InChIKey InChIKey=MKRPIBSCGZAUCH-OAHLLOKOSA-N ChemAxon Polar Surface Area (PSA) 118.72 ChemAxon Refractivity 88.59 ChemAxon Polarizability 34.11 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 8.6 ChemAxon pKa (strongest basic) 1.86 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 16129579 PubChem Substance 99443717 ChemSpider 17286395 PDB 7MR BE0000058 Matrix metalloproteinase-9 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Matrix metalloproteinase-9 Involved in proteolysis and tissue remodeling May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond 20q11.2-q13.1 Cytoplasmic None 5.92 78428.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7176 GenAtlas MMP9 GeneCards MMP9 GenBank Gene Database J05070 GenBank Protein Database 177205 UniProtKB P14780 UniProt Accession MMP9_HUMAN 92 kDa gelatinase 92 kDa type IV collagenase EC 3.4.24.35 Gelatinase B GELB Matrix metalloproteinase-9 precursor MMP-9 >Matrix metalloproteinase-9 precursor MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEM RGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHN ITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYP FDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRS YSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTRDGNADGKPCQFPFIFQGQSYS ACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYST CTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMY PMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSER PTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYW RFSEGRGSRPQGPFLIADKWPALPRKLDSVFEEPLSKKLFFFSGRQVWVYTGASVLGPRR LDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLD THDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED >2124 bp ATGAGCCTCTGGCAGCCCCTGGTCCTGGTGCTCCTGGTGCTGGGCTGCTGCTTTGCTGCC CCCAGACAGCGCCAGTCCACCCTTGTGCTCTTCCCTGGAGACCTGAGAACCAATCTCACC GACAGGCAGCTGGCAGAGGAATACCTGTACCGCTATGGTTACACTCGGGTGGCAGAGATG CGTGGAGAGTCGAAATCTCTGGGGCCTGCGCTGCTGCTTCTCCAGAAGCAACTGTCCCTG CCCGAGACCGGTGAGCTGGATAGCGCCACGCTGAAGGCCATGCGAACCCCACGGTGCGGG GTCCCAGACCTGGGCAGATTCCAAACCTTTGAGGGCGACCTCAAGTGGCACCACCACAAC ATCACCTATTGGATCCAAAACTACTCGGAAGACTTGCCGCGGGCGGTGATTGACGACGCC TTTGCCCGCGCCTTCGCACTGTGGAGCGCGGTGACGCCGCTCACCTTCACTCGCGTGTAC AGCCGGGACGCAGACATCGTCATCCAGTTTGGTGTCGCGGAGCACGGAGACGGGTATCCC TTCGACGGGAAGGACGGGCTCCTGGCACACGCCTTTCCTCCTGGCCCCGGCATTCAGGGA GACGCCCATTTCGACGATGACGAGTTGTGGTCCCTGGGCAAGGGCGTCGTGGTTCCAACT CGGTTTGGAAACGCAGATGGCGCGGCCTGCCACTTCCCCTTCATCTTCGAGGGCCGCTCC TACTCTGCCTGCACCACCGACGGTCGCTCCGACGGCTTGCCCTGGTGCAGTACCACGGCC AACTACGACACCGACGACCGGTTTGGCTTCTGCCCCAGCGAGAGACTCTACACCCGGGAC GGCAATGCTGATGGGAAACCCTGCCAGTTTCCATTCATCTTCCAAGGCCAATCCTACTCC GCCTGCACCACGGACGGTCGCTCCGACGGCTACCGCTGGTGCGCCACCACCGCCAACTAC GACCGGGACAAGCTCTTCGGCTTCTGCCCGACCCGAGCTGACTCGACGGTGATGGGGGGC AACTCGGCGGGGGAGCTGTGCGTCTTCCCCTTCACTTTCCTGGGTAAGGAGTACTCGACC TGTACCAGCGAGGGCCGCGGAGATGGGCGCCTCTGGTGCGCTACCACCTCGAACTTTGAC AGCGACAAGAAGTGGGGCTTCTGCCCGGACCAAGGATACAGTTTGTTCCTCGTGGCGGCG CATGAGTTCGGCCACGCGCTGGGCTTAGATCATTCCTCAGTGCCGGAGGCGCTCATGTAC CCTATGTACCGCTTCACTGAGGGGCCCCCCTTGCATAAGGACGACGTGAATGGCATCCGG CACCTCTATGGTCCTCGCCCTGAACCTGAGCCACGGCCTCCAACCACCACCACACCGCAG CCCACGGCTCCCCCGACGGTCTGCCCCACCGGACCCCCCACTGTCCACCCCTCAGAGCGC CCCACAGCTGGCCCCACAGGTCCCCCCTCAGCTGGCCCCACAGGTCCCCCCACTGCTGGC CCTTCTACGGCCACTACTGTGCCTTTGAGTCCGGTGGACGATGCCTGCAACGTGAACATC TTCGACGCCATCGCGGAGATTGGGAACCAGCTGTATTTGTTCAAGGATGGGAAGTACTGG CGATTCTCTGAGGGCAGGGGGAGCCGGCCGCAGGGCCCCTTCCTTATCGCCGACAAGTGG CCCGCGCTGCCCCGCAAGCTGGACTCGGTCTTTGAGGAGCCGCTCTCCAAGAAGCTTTTC TTCTTCTCTGGGCGCCAGGTGTGGGTGTACACAGGCGCGTCGGTGCTGGGCCCGAGGCGT CTGGACAAGCTGGGCCTGGGAGCCGACGTGGCCCAGGTGACCGGGGCCCTCCGGAGTGGC AGGGGGAAGATGCTGCTGTTCAGCGGGCGGCGCCTCTGGAGGTTCGACGTGAAGGCGCAG ATGGTGGATCCCCGGAGCGCCAGCGAGGTGGACCGGATGTTCCCCGGGGTGCCTTTGGAC ACGCACGACGTCTTCCAGTACCGAGAGAAAGCCTATTTCTGCCAGGACCGCTTCTACTGG CGCGTGAGTTCCCGGAGTGAGTTGAACCAGGTGGACCAAGTGGGCTACGTGACCTATGAC ATCCTGCAGTGCCCTGAGGACTAG PF00040 fn2 PF00045 Hemopexin PF00413 Peptidase_M10 PF01471 PG_binding_1 PF04886 PT component extracellular matrix (sensu Metazoa) component extracellular matrix function catalytic activity function hydrolase activity function ion binding function peptidase activity function cation binding function endopeptidase activity function transition metal ion binding function metallopeptidase activity function zinc ion binding function metalloendopeptidase activity function binding process protein metabolism process metabolism process cellular protein metabolism process cellular carbohydrate metabolism process macromolecule metabolism process peptidoglycan metabolism process proteolysis process carbohydrate metabolism process physiological process "
drug:(2R)-2-AMINO-3,3,3-TRIFLUORO-N-HYDROXY-2-{[(4-PHENOXYPHENYL)SULFONYL]METHYL}PROPANAMIDErdfs:label"(2R)-2-AMINO-3,3,3-TRIFLUORO-N-HYDROXY-2-{[(4-PHENOXYPHENYL)SULFONYL]METHYL}PROPANAMIDE"
drug:(2R)-2-AMINO-3,3,3-TRIFLUORO-N-HYDROXY-2-{[(4-PHENOXYPHENYL)SULFONYL]METHYL}PROPANAMIDErdf:typedrugbank:drugs
drug:(2R)-2-ETHYL-1-HEXANESULFONIC ACIDdrugbank:description" experimental This compound belongs to the sulfuric acid monoesters. These are organic compounds containing the sulfuric acid monoester functional group. Sulfuric Acid Monoesters Organic Compounds Organic Acids and Derivatives Organic Sulfuric Acids and Derivatives Sulfuric Acid Monoesters Polyamines polyamine logP 0.93 ALOGPS logS -2.5 ALOGPS Water Solubility 7.21e-01 g/l ALOGPS logP 2.56 ChemAxon IUPAC Name {[(2R)-2-ethylhexyl]oxy}sulfonic acid ChemAxon Traditional IUPAC Name [(2R)-2-ethylhexyl]oxysulfonic acid ChemAxon Molecular Weight 210.291 ChemAxon Monoisotopic Weight 210.092579754 ChemAxon SMILES [H][C@@](CC)(CCCC)COS(O)(=O)=O ChemAxon Molecular Formula C8H18O4S ChemAxon InChI InChI=1S/C8H18O4S/c1-3-5-6-8(4-2)7-12-13(9,10)11/h8H,3-7H2,1-2H3,(H,9,10,11)/t8-/m1/s1 ChemAxon InChIKey InChIKey=MHGOKSLTIUHUBF-MRVPVSSYSA-N ChemAxon Polar Surface Area (PSA) 63.6 ChemAxon Refractivity 50.4 ChemAxon Polarizability 22.47 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) -1.2 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 5496779 PubChem Substance 99443989 ChemSpider 4593490 PDB C26 BE0003185 Putative alkylsulfatase Pseudomonas putida # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Putative alkylsulfatase Involved in oxidoreductase activity atsK None 7.06 33202.0 Pseudomonas putida GenBank Gene Database AF126201 UniProtKB Q9WWU5 UniProt Accession Q9WWU5_PSEPU >Putative alkylsulfatase MSNAALATAPHALELDVHPVAGRIGAEIRGVKLSPDLDAATVEAIQAALVRHKVIFFRGQ THLDDQSQEGFAKLLGEPVAHPTVPVVDGTRYLLQLDGAQGQRANSWHTDVTFVEAYPKA SILRSVVAPASGGDTVWANTAAAYQELPEPLRELADKLWAVHSNEYDYASLKPDIDPAKL ERHRKVFTSTVYETEHPVVRVHPISGERALQLGHFVKRIKGYSLADSQHLFAVLQGHVTR LENTVRWRWEAGDVAIWDNRATQHYAVDDYGTQPRIVRRVTLAGEVPVGVDGQLSRTTRK G >906 bp TCAGCCTTTACGCGTAGTACGGCTCAGTTGGCCATCCACGCCCACCGGCACTTCACCGGC CAGCGTTACCCGGCGCACGATACGTGGCTGGGTCCCATAATCATCCACCGCGTAGTGCTG TGTCGCACGGTTATCCCAGATAGCCACATCGCCCGCCTCCCAGCGCCAGCGCACGGTGTT CTCAAGGCGCGTGACATGCCCTTGCAGCACCGCGAACAAGTGCTGCGAATCGGCCAGCGA ATAGCCCTTGATGCGTTTGACGAAATGCCCCAGCTGCAGCGCCCGCTCACCGCTGATCGG GTGCACTCGCACCACCGGGTGCTCGGTCTCATACACCGTCGAGGTGAACACTTTGCGATG ACGCTCGAGTTTGGCAGGGTCGATATCGGGCTTGAGGCTGGCATAGTCGTACTCGTTGCT GTGCACCGCCCACAGCTTGTCGGCCAGCTCGCGCAGGGGCTCGGGCAACTCCTGATAGGC CGCAGCGGTATTGGCCCATACAGTATCGCCGCCCGACGCAGGGGCCACCACACTGCGCAG GATCGAGGCCTTGGGGTAGGCCTCTACGAAGGTCACATCGGTGTGCCAGGAGTTGGCCCG CTGCCCTTGGGCGCCATCGAGCTGGAGCAGGTAGCGGGTACCGTCGACCACTGGCACGGT GGGGTGAGCGACCGGCTCGCCCAGCAGCTTGGCAAAACCTTCCTGGCTTTGATCGTCCAG GTGGGTCTGGCCACGGAAGAAGATGACCTTGTGCCGCACCAACGCAGCCTGGATGGCCTC GACTGTGGCGGCATCGAGGTCGGGGGACAGTTTGACCCCGCGTATTTCGGCGCCGATACG GCCGGCGACCGGGTGGACATCAAGTTCGAGGGCGTGCGGCGCGGTGGCCAGTGCAGCGTT GCTCAT PF02668 TauD function oxidoreductase activity function catalytic activity process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process "
drug:(2R)-2-ETHYL-1-HEXANESULFONIC ACIDrdfs:label"(2R)-2-ETHYL-1-HEXANESULFONIC ACID"
drug:(2R)-2-ETHYL-1-HEXANESULFONIC ACIDrdf:typedrugbank:drugs
drug:(2R)-2-PHENYL-N-PYRIDIN-4-YLBUTANAMIDEdrugbank:description" experimental This compound belongs to the phenylpropylamines. These are compounds containing a phenylpropylamine moiety, which consists of a phenyl group substituted at the third carbon by an propan-1-amine. Phenylpropylamines Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenylpropylamines Aminopyridines and Derivatives Secondary Carboxylic Acid Amides Polyamines Carboxylic Acids Enolates aminopyridine pyridine secondary carboxylic acid amide carboxamide group polyamine enolate carboxylic acid derivative carboxylic acid amine organonitrogen compound logP 2.69 ALOGPS logS -3.1 ALOGPS Water Solubility 1.75e-01 g/l ALOGPS logP 2.82 ChemAxon IUPAC Name (2R)-2-phenyl-N-(pyridin-4-yl)butanamide ChemAxon Traditional IUPAC Name (2R)-2-phenyl-N-(pyridin-4-yl)butanamide ChemAxon Molecular Weight 240.3003 ChemAxon Monoisotopic Weight 240.126263144 ChemAxon SMILES [H][C@](CC)(C(=O)NC1=CC=NC=C1)C1=CC=CC=C1 ChemAxon Molecular Formula C15H16N2O ChemAxon InChI InChI=1S/C15H16N2O/c1-2-14(12-6-4-3-5-7-12)15(18)17-13-8-10-16-11-9-13/h3-11,14H,2H2,1H3,(H,16,17,18)/t14-/m1/s1 ChemAxon InChIKey InChIKey=MODBYAQUXXEFRM-CQSZACIVSA-N ChemAxon Polar Surface Area (PSA) 41.99 ChemAxon Refractivity 72.66 ChemAxon Polarizability 25.62 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 13.25 ChemAxon pKa (strongest basic) 5.65 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 670006 PubChem Substance 99443361 ChemSpider 583213 PDB 1CM BE0001730 Lanosterol 14-alpha demethylase Mycobacterium tuberculosis # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Lanosterol 14-alpha demethylase Secondary metabolites biosynthesis, transport and catabolism Its precise biological substrate is not known. Catalyzes C14-demethylation of lanosterol, 24,25-dihydrolanosterol and obtusifoliol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene- 3-beta-ol cyp51 Cytoplasm None 5.71 50878.0 Mycobacterium tuberculosis GenBank Gene Database BX842574 GenBank Protein Database 1550642 UniProtKB P0A512 UniProt Accession CP51_MYCTU CYPLI EC 1.14.13.70 Lanosterol 14-alpha demethylase P450-14DM P450-LIA1 Sterol 14- alpha demethylase >Cytochrome P450 51 MSAVALPRVSGGHDEHGHLEEFRTDPIGLMQRVRDECGDVGTFQLAGKQVVLLSGSHANE FFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEMLHNAALRGEQMKGHAATIEDQ VRRMIADWGEAGEIDLLDFFAELTIYTSSACLIGKKFRDQLDGRFAKLYHELERGTDPLA YVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPR FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHA LRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFP DPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA QPPESYRNDHSKMVVQLAQPACVRYRRRTGV >1356 bp TTAAACTCCCGTTCGCCGGCGGTAGCGCACGCAAGCGGGCTGGGCCAACTGCACCACCAT CTTCGAATGGTCGTTACGATAGCTTTCTGGCGGTTGCGCCATCTCAAACTCATACTCGCG CAACAACACCGAGAAGATCGCTTTGATCTGCATGATGGCGAACGCCGCCCCCACGCAACG ATGCCGGCCGGCGCCGAACGGAATCCACGTCCAGCGGTTGAGCAGATCTTCCTGGCGCGG CTGCTCGTATCGTGCTGGCACGAAGTCGTGGGGATCGGGGAAGTCTTCGGGGATCCGGTT GGAGATCGCCGGGGAGGCCGCCACCAGATCGCCCTCATGAATCCGGTGGCCTTGCACCTC GAACTCGCCCTTGGCCACTCGCATGAGGATGATCAGCGGAGGGTGCAGGCGCAGCGTCTC TTTCAGCACGTTTTCCAGCTGCGGAATCTGGCGCAGCGCATGGAAACTCACCGATCGGCC GTCGCCGTACAGCTCGTCGAGTTCGTCGATCACGGCCGCGTAGGCGTCGCGATGGCGCAT CAACTCGATCAGCGTCCACGAAGCCGTACCCGAGCTGGTGTGATGGCCGGCGAACATCAT CGAGATGAACATGCCGGTGATCTCGTCGGCCGAGAACCGGGGAGTGCCGGTCTCAGCCTT GACGGCGATGAGCACGTCGAGCATGTCACGGTCGCTCTTGTCGGTGGGTGGGTTGGCGAT CCGGCCGTTCATGATGTCCGCAACCAGTGCCACCAGACCATTGCGGGCTTCGTCGCGGCG ACGGAAGCTCTCGATCGGCAGATACGGGTCGACGTAGGCTAGTGGGTCGGTGCCGCGCTC CAACTCGTGATAGAGCTTGGCGAATCGCCCGTCGAGCTGGTCGCGGAACTTCTTGCCGAT CAGGCAGGCCGAGGAGGTGTAGATGGTCAGCTCGGCGAAGAAGTCCAGCAGATCGATCTC GCCGGCCTCACCCCAGTCGGCGATCATCCGTCGGACTTGATCTTCGATGGTGGCAGCGTG GCCCTTCATCTGCTCGCCGCGTAGCGCGGCATTGTGCAGCATCTCTTTACGCCGTTCCGG GCTGGCGTCGAACACCACGCCCTCGCCGAAGATCGGCGTCATGAACGGGTATGCCTTGGC CTGGTCCAGGTCGTCGTCGCCCGCCCGGAAGAAGAATTCGTTGGCGTGCGAGCCGGACAG CAGCACGACCTGCTTCCCGGCCAGCTGGAAGGTACCGACGTCTCCGCATTCGTCGCGGAC CCGTTGCATCAGCCCGATCGGATCGGTGCGGAACTCCTCGAGGTGGCCGTGTTCGTCGTG GCCACCCGAAACCCGGGGTAGTGCAACAGCGCTCAT PF00067 p450 function cation binding function transition metal ion binding function iron ion binding function binding function tetrapyrrole binding function catalytic activity function heme binding function monooxygenase activity function oxidoreductase activity function ion binding process generation of precursor metabolites and energy process electron transport process physiological process process metabolism process cellular metabolism "
drug:(2R)-2-PHENYL-N-PYRIDIN-4-YLBUTANAMIDErdfs:label"(2R)-2-PHENYL-N-PYRIDIN-4-YLBUTANAMIDE"
drug:(2R)-2-PHENYL-N-PYRIDIN-4-YLBUTANAMIDErdf:typedrugbank:drugs
drug:(2R)-2-benzyl-3-nitropropanoic aciddrugbank:description" experimental This compound belongs to the beta amino acids and derivatives. These are amino acids having a (-NH2) group attached to the beta carbon atom. Beta Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Phenylpropanoic Acids Phenylpropylamines Nitro Compounds Nitronic Acids Organic Oxoazanium Compounds Polyamines Enolates Carboxylic Acids benzene nitronic acid nitro compound organic oxoazanium polyamine enolate carboxylic acid organonitrogen compound amine logP 1.44 ALOGPS logS -2.7 ALOGPS Water Solubility 4.45e-01 g/l ALOGPS logP 1.86 ChemAxon IUPAC Name (2R)-2-benzyl-3-nitropropanoic acid ChemAxon Traditional IUPAC Name (2R)-2-benzyl-3-nitropropanoic acid ChemAxon Molecular Weight 209.1986 ChemAxon Monoisotopic Weight 209.068807845 ChemAxon SMILES [H][C@@](CC1=CC=CC=C1)(C[N+]([O-])=O)C(O)=O ChemAxon Molecular Formula C10H11NO4 ChemAxon InChI InChI=1S/C10H11NO4/c12-10(13)9(7-11(14)15)6-8-4-2-1-3-5-8/h1-5,9H,6-7H2,(H,12,13)/t9-/m1/s1 ChemAxon InChIKey InChIKey=GCXOTBPCUQHSAO-SECBINFHSA-N ChemAxon Polar Surface Area (PSA) 83.12 ChemAxon Refractivity 52.64 ChemAxon Polarizability 19.68 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 3.94 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 24768537 PubChem Substance 99443395 ChemSpider 23319419 PDB 23N BE0003753 Carboxypeptidase A1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Carboxypeptidase A1 Amino acid transport and metabolism Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro CPA1 7q32 Secreted None 5.55 47139.9 Human HUGO Gene Nomenclature Committee (HGNC) GNC:2296 GeneCards CPA1 GenBank Gene Database X67318 GenBank Protein Database 35330 UniProtKB P15085 UniProt Accession CBPA1_HUMAN >Carboxypeptidase A1 MRGLLVLSVLLGAVFGKEDFVGHQVLRISVADEAQVQKVKELEDLEHLQLDFWRGPAHPG SPIDVRVPFPSIQAVKIFLESHGISYETMIEDVQSLLDEEQEQMFAFRSRARSTDTFNYA TYHTLEEIYDFLDLLVAENPHLVSKIQIGNTYEGRPIYVLKFSTGGSKRPAIWIDTGIHS REWVTQASGVWFAKKITQDYGQDAAFTAILDTLDIFLEIVTNPDGFAFTHSTNRMWRKTR SHTAGSLCIGVDPNRNWDAGFGLSGASSNPCSETYHGKFANSEVEVKSIVDFVKDHGNIK AFISIHSYSQLLMYPYGYKTEPVPDQDELDQLSKAAVTALASLYGTKFNYGSIIKAIYQA SGSTIDWTYSQGIKYSFTFELRDTGRYGFLLPASQIIPTAKETWLALLTIMEHTLNHPY >1260 bp ATGCGGGGGTTGCTGGTGTTGAGTGTCCTGTTGGGGGCTGTCTTTGGCAAGGAGGACTTT GTGGGGCATCAGGTGCTCCGAATCTCTGTAGCCGATGAGGCCCAGGTACAGAAGGTGAAG GAGCTGGAGGACCTGGAGCACCTGCAGCTGGACTTCTGGCGGGGGCCTGCCCACCCTGGC TCCCCCATCGACGTCCGAGTGCCCTTCCCCAGCATCCAGGCGGTCAAGATCTTTCTGGAG TCCCACGGCATCAGCTATGAGACCATGATCGAGGACGTGCAGTCGCTGCTGGACGAGGAG CAGGAGCAGATGTTCGCCTTCCGGTCCCGGGCGCGCTCCACCGACACTTTTAACTACGCC ACCTACCACACCCTGGAGGAGATCTATGACTTCCTGGACCTGCTGGTGGCGGAGAACCCG CACCTTGTCAGCAAGATCCAGATTGGCAACACCTATGAAGGGCGTCCCATTTATGTGCTG AAGTTCAGCACGGGGGGCAGTAAGCGTCCAGCCATCTGGATCGACACGGGCATCCATTCC CGGGAGTGGGTCACCCAGGCCAGTGGGGTCTGGTTTGCAAAGAAGATCACTCAAGACTAT GGGCAGGATGCAGCTTTCACCGCCATTCTCGACACCTTGGACATCTTCCTGGAGATCGTC ACCAACCCTGATGGCTTTGCCTTCACGCACAGCACGAATCGCATGTGGCGCAAGACTCGG TCCCACACAGCAGGCTCCCTCTGTATTGGCGTGGACCCCAACAGGAACTGGGACGCTGGC TTTGGGTTGTCCGGAGCCAGCAGTAACCCCTGCTCGGAGACTTACCACGGCAAGTTTGCC AATTCCGAAGTGGAGGTCAAGTCCATTGTAGACTTTGTGAAGGACCATGGGAACATCAAG GCCTTCATCTCCATCCACAGCTACTCCCAGCTCCTCATGTATCCCTATGGCTACAAAACA GAACCAGTCCCTGACCAGGATGAGCTGGATCAGCTTTCCAAGGCTGCTGTGACAGCCCTG GCCTCTCTCTACGGGACCAAGTTCAACTATGGCAGCATCATCAAGGCAATTTATCAAGCC AGTGGAAGCACTATTGACTGGACCTACAGCCAGGGCATCAAGTACTCCTTCACCTTCGAG CTCCGGGACACTGGGCGCTATGGCTTCCTGCTGCCAGCCTCCCAGATCATCCCCACAGCC AAGGAGACGTGGCTGGCGCTTCTGACCATCATGGAGCACACCCTGAATCACCCCTACTGA PF00246 Peptidase_M14 PF02244 Propep_M14 function peptidase activity function exopeptidase activity function carboxypeptidase activity function metallocarboxypeptidase activity function catalytic activity function carboxypeptidase A activity function hydrolase activity process protein metabolism process cellular protein metabolism process proteolysis process physiological process process metabolism process macromolecule metabolism "
drug:(2R)-2-benzyl-3-nitropropanoic acidrdfs:label"(2R)-2-benzyl-3-nitropropanoic acid"
drug:(2R)-2-benzyl-3-nitropropanoic acidrdf:typedrugbank:drugs
drug:(2R)-2-{[(4-FLUORO-3-METHYLPHENYL)SULFONYL]AMINO}-N-HYDROXY-2-TETRAHYDRO-2H-PYRAN-4-YLACETAMIDEdrugbank:description" experimental This compound belongs to the alpha amino acid amides. These are amide derivatives of alpha amino acids. Alpha Amino Acid Amides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Benzenesulfonamides Toluenes Fluorobenzenes Oxanes Aryl Fluorides Sulfonamides Sulfonyls Hydroxamic Acids Polyamines Enolates Ethers Organofluorides benzenesulfonamide fluorobenzene toluene aryl fluoride aryl halide benzene oxane sulfonyl sulfonamide sulfonic acid derivative carboxamide group hydroxamic acid polyamine ether enolate organofluoride amine organohalogen organonitrogen compound logP 0.12 ALOGPS logS -2.5 ALOGPS Water Solubility 1.16e+00 g/l ALOGPS logP 0.76 ChemAxon IUPAC Name (2R)-2-[(4-fluoro-3-methylbenzene)sulfonamido]-N-hydroxy-2-(oxan-4-yl)acetamide ChemAxon Traditional IUPAC Name (2R)-2-(4-fluoro-3-methylbenzenesulfonamido)-N-hydroxy-2-(oxan-4-yl)acetamide ChemAxon Molecular Weight 346.374 ChemAxon Monoisotopic Weight 346.099870623 ChemAxon SMILES [H][C@@](NS(=O)(=O)C1=CC(C)=C(F)C=C1)(C1CCOCC1)C(=O)NO ChemAxon Molecular Formula C14H19FN2O5S ChemAxon InChI InChI=1S/C14H19FN2O5S/c1-9-8-11(2-3-12(9)15)23(20,21)17-13(14(18)16-19)10-4-6-22-7-5-10/h2-3,8,10,13,17,19H,4-7H2,1H3,(H,16,18)/t13-/m1/s1 ChemAxon InChIKey InChIKey=LUCFRFDOOYLALP-CYBMUJFWSA-N ChemAxon Polar Surface Area (PSA) 104.73 ChemAxon Refractivity 81.08 ChemAxon Polarizability 32.84 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 8.68 ChemAxon pKa (strongest basic) -4.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 4369384 PubChem Substance 99443761 ChemSpider 3571962 PDB 915 BE0001363 Lethal factor Bacillus anthracis # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Lethal factor Involved in protease activity One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. LF is the lethal factor that, when associated with PA, causes death. LF is not toxic by itself. It is a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5). Cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LeTx intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates lef Secreted protein None 5.69 93771.0 Bacillus anthracis GenBank Gene Database M29081 GenBank Protein Database 143144 UniProtKB P15917 UniProt Accession LEF_BACAN Anthrax lethal toxin endopeptidase component EC 3.4.24.83 Lethal factor precursor LF >Lethal factor precursor MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEE RNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGD ITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNV YYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLE QNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLAR YEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSS DFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYD INQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLT ATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSP DTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNIN QEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNG RFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHE FGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHST DHAERLKVQKNAPKTFQFINDQIKFIINS >2430 bp ATGAATATAAAAAAAGAATTTATAAAAGTAATTAGTATGTCATGTTTAGTAACAGCAATT ACTTTGAGTGGTCCCGTCTTTATCCCCCTTGTACAGGGGGCGGGCGGTCATGGTGATGTA GGTATGCACGTAAAAGAGAAAGAGAAAAATAAAGATGAGAATAAGAGAAAAGATGAAGAA CGAAATAAAACACAGGAAGAGCATTTAAAGGAAATCATGAAACACATTGTAAAAATAGAA GTAAAAGGGGAGGAAGCTGTTAAAAAAGAGGCAGCAGAAAAGCTACTTGAGAAAGTACCA TCTGATGTTTTAGAGATGTATAAAGCAATTGGAGGAAAGATATATATTGTGGATGGTGAT ATTACAAAACATATATCTTTAGAAGCATTATCTGAAGATAAGAAAAAAATAAAAGACATT TATGGGAAAGATGCTTTATTACATGAACATTATGTATATGCAAAAGAAGGATATGAACCC GTACTTGTAATCCAATCTTCGGAAGATTATGTAGAAAATACTGAAAAGGCACTGAACGTT TATTATGAAATAGGTAAGATATTATCAAGGGATATTTTAAGTAAAATTAATCAACCATAT CAGAAATTTTTAGATGTATTAAATACCATTAAAAATGCATCTGATTCAGATGGACAAGAT CTTTTATTTACTAATCAGCTTAAGGAACATCCCACAGACTTTTCTGTAGAATTCTTGGAA CAAAATAGCAATGAGGTACAAGAAGTATTTGCGAAAGCTTTTGCATATTATATCGAGCCA CAGCATCGTGATGTTTTACAGCTTTATGCACCGGAAGCTTTTAATTACATGGATAAATTT AACGAACAAGAAATAAATCTATCCTTGGAAGAACTTAAAGATCAACGGATGCTGTCAAGA TATGAAAAATGGGAAAAGATAAAACAGCACTATCAACACTGGAGCGATTCTTTATCTGAA GAAGGAAGAGGACTTTTAAAAAAGCTGCAGATTCCTATTGAGCCAAAGAAAGATGACATA ATTCATTCTTTATCTCAAGAAGAAAAAGAGCTTCTAAAAAGAATACAAATTGATAGTAGT GATTTTTTATCTACTGAGGAAAAAGAGTTTTTAAAAAAGCTACAAATTGATATTCGTGAT TCTTTATCTGAAGAAGAAAAAGAGCTTTTAAATAGAATACAGGTGGATAGTAGTAATCCT TTATCTGAAAAAGAAAAAGAGTTTTTAAAAAAGCTGAAACTTGATATTCAACCATATGAT ATTAATCAAAGGTTGCAAGATACAGGAGGGTTAATTGATAGTCCGTCAATTAATCTTGAT GTAAGAAAGCAGTATAAAAGGGATATTCAAAATATTGATGCTTTATTACATCAATCCATT GGAAGTACCTTGTACAATAAAATTTATTTGTATGAAAATATGAATATCAATAACCTTACA GCAACCCTAGGTGCGGATTTAGTTGATTCCACTGATAATACTAAAATTAATAGAGGTATT TTCAATGAATTCAAAAAAAATTTCAAATATAGTATTTCTAGTAACTATATGATTGTTGAT ATAAATGAAAGGCCTGCATTAGATAATGAGCGTTTGAAATGGAGAATCCAATTATCACCA GATACTCGAGCAGGATATTTAGAAAATGGAAAGCTTATATTACAAAGAAACATCGGTCTG GAAATAAAGGATGTACAAATAATTAAGCAATCCGAAAAAGAATATATAAGGATTGATGCG AAAGTAGTGCCAAAGAGTAAAATAGATACAAAAATTCAAGAAGCACAGTTAAATATAAAT CAGGAATGGAATAAAGCATTAGGGTTACCAAAATATACAAAGCTTATTACATTCAACGTG CATAATAGATATGCATCCAATATTGTAGAAAGTGCTTATTTAATATTGAATGAATGGAAA AATAATATTCAAAGTGATCTTATAAAAAAGGTAACAAATTACTTAGTTGATGGTAATGGA AGATTTGTTTTTACCGATATTACTCTCCCTAATATAGCTGAACAATATACACATCAAGAT GAGATATATGAGCAAGTTCATTCAAAAGGGTTATATGTTCCAGAATCCCGTTCTATATTA CTCCATGGACCTTCAAAAGGTGTAGAATTAAGGAATGATAGTGAGGGTTTTATACACGAA TTTGGACATGCTGTGGATGATTATGCTGGATATCTATTAGATAAGAACCAATCTGATTTA GTTACAAATTCTAAAAAATTCATTGATATTTTTAAGGAAGAAGGGAGTAATTTAACTTCG TATGGGAGAACAAATGAAGCGGAATTTTTTGCAGAAGCCTTTAGGTTAATGCATTCTACG GACCATGCTGAACGTTTAAAAGTTCAAAAAAATGCTCCGAAAACTTTCCAATTTATTAAC GATCAGATTAAGTTCATTATTAACTCATAA PF09156 Anthrax-tox_M PF07737 ATLF component extracellular region function peptidase activity function catalytic activity function hydrolase activity function metallopeptidase activity function ion binding function cation binding function transition metal ion binding function zinc ion binding function binding process proteolysis process metabolism process macromolecule metabolism process interaction between organisms process interspecies interaction between organisms process symbiosis, encompassing mutualism through parasitism process pathogenesis process protein metabolism process cellular protein metabolism process physiological process "
drug:(2R)-2-{[(4-FLUORO-3-METHYLPHENYL)SULFONYL]AMINO}-N-HYDROXY-2-TETRAHYDRO-2H-PYRAN-4-YLACETAMIDErdfs:label"(2R)-2-{[(4-FLUORO-3-METHYLPHENYL)SULFONYL]AMINO}-N-HYDROXY-2-TETRAHYDRO-2H-PYRAN-4-YLACETAMIDE"
drug:(2R)-2-{[(4-FLUORO-3-METHYLPHENYL)SULFONYL]AMINO}-N-HYDROXY-2-TETRAHYDRO-2H-PYRAN-4-YLACETAMIDErdf:typedrugbank:drugs
drug:(2R)-2-{[4-(benzylamino)-8-(1-methylethyl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-oldrugbank:description" experimental This compound belongs to the pyrazolotriazines. These are compounds containing a pyrazolotriazine skeleton, which consists of a pyrazole fused to a triazine. Pyrazolotriazines Organic Compounds Heterocyclic Compounds Pyrazolotriazines Aminotriazines Benzene and Substituted Derivatives Pyrazoles 1,2-Aminoalcohols Polyamines Primary Alcohols Secondary Amines amino-1,3,5-triazine triazine benzene pyrazole azole 1,2-aminoalcohol polyamine secondary amine primary alcohol alcohol amine organonitrogen compound logP 3.21 ALOGPS logS -4.4 ALOGPS Water Solubility 1.32e-02 g/l ALOGPS logP 3.49 ChemAxon IUPAC Name (2R)-2-{[4-(benzylamino)-8-(propan-2-yl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-ol ChemAxon Traditional IUPAC Name (2R)-2-{[4-(benzylamino)-8-isopropylpyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-ol ChemAxon Molecular Weight 354.4493 ChemAxon Monoisotopic Weight 354.216809484 ChemAxon SMILES [H][C@@](CC)(CO)NC1=NC2=C(C=NN2C(NCC2=CC=CC=C2)=N1)C(C)C ChemAxon Molecular Formula C19H26N6O ChemAxon InChI InChI=1S/C19H26N6O/c1-4-15(12-26)22-18-23-17-16(13(2)3)11-21-25(17)19(24-18)20-10-14-8-6-5-7-9-14/h5-9,11,13,15,26H,4,10,12H2,1-3H3,(H2,20,22,23,24)/t15-/m1/s1 ChemAxon InChIKey InChIKey=SQUNOCMDMIQIQK-OAHLLOKOSA-N ChemAxon Polar Surface Area (PSA) 87.37 ChemAxon Refractivity 116.79 ChemAxon Polarizability 40.38 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 13.05 ChemAxon pKa (strongest basic) 4.62 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 25190761 PubChem Substance 99444756 ChemSpider 24700216 PDB NNN BE0001072 Cyclin-dependent kinase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cyclin-dependent kinase 2 Involved in protein kinase activity ATP + a protein = ADP + a phosphoprotein CDK2deltaT None 9.76 30061.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1771 GenAtlas CDK2deltaT GeneCards CDK2deltaT GenBank Gene Database AB012305 GenBank Protein Database 3551191 UniProtKB P24941 UniProt Accession CDK2_HUMAN EC 2.7.11.22 p33 protein kinase >Cell division protein kinase 2 MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL >897 bp ATGGAGAACTTCCAAAAGGTGGAAAAGATCGGAGAGGGCACGTACGGAGTTGTGTACAAA GCCAGAAACAAGTTGACGGGAGAGGTGGTGGCGCTTAAGAAAATCCGCCTGGACACTGAG ACTGAGGGTGTGCCCAGTACTGCCATCCGAGAGATCTCTCTGCTTAAGGAGCTTAACCAT CCTAATATTGTCAAGCTGCTGGATGTCATTCACACAGAAAATAAACTCTACCTGGTTTTT GAATTTCTGCACCAAGATCTCAAGAAATTCATGGATGCCTCTGCTCTCACTGGCATTCCT CTTCCCCTCATCAAGAGCTATCTGTTCCAGCTGCTCCAGGGCCTAGCTTTCTGCCATTCT CATCGGGTCCTCCACCGAGACCTTAAACCTCAGAATCTGCTTATTAACACAGAGGGGGCC ATCAAGCTAGCAGACTTTGGACTAGCCAGAGCTTTTGGAGTCCCTGTTCGTACTTACACC CATGAGGTGGTGACCCTGTGGTACCGAGCTCCTGAAATCCTCCTGGGCTCGAAATATTAT TCCACAGCTGTGGACATCTGGAGCCTGGGCTGCATCTTTGCTGAGATGGTGACTCGCCGG GCCCTGTTCCCTGGAGATTCTGAGATTGACCAGCTCTTCCGGATCTTTCGGACTCTGGGG ACCCCAGATGAGGTGGTGTGGCCAGGAGTTACTTCTATGCCTGATTACAAGCCAAGTTTC CCCAAGTGGGCCCGGCAAGATTTTAGTAAAGTTGTACCTCCCCTGGATGAAGATGGACGG AGCTTGTTATCGCAAATGCTGCACTACGACCCTAACAAGCGGATTTCGGCCAAGGCAGCC CTGGCTCACCCTTTCTTCCAGGATGTGACCAAGCCAGTACCCCATCTTCGACTCTGA PF00069 Pkinase function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism BE0003734 Cyclin-A2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cyclin-A2 Involved in protein binding Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions CCNA2 4q25-q31 Nucleus. Cytoplasm None 6.52 48536.3 Human HUGO Gene Nomenclature Committee (HGNC) GNC:1578 GeneCards CCNA2 GenBank Gene Database X51688 GenBank Protein Database 30307 UniProtKB P20248 UniProt Accession CCNA2_HUMAN Cyclin-A >Cyclin-A2 MLGNSAPGPATREAGSALLALQQTALQEDQENINPEKAAPVQQPRTRAALAVLKSGNPRG LAQQQRPKTRRVAPLKDLPVNDEHVTVPPWKANSKQPAFTIHVDEAEKEAQKKPAESQKI EREDALAFNSAISLPGPRKPLVPLDYPMDGSFESPHTMDMSIVLEDEKPVSVNEVPDYHE DIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYID RFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLK VLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLPSVIAGAAF HLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNSKYHG VSLLNPPETLNL >1299 bp ATGTTGGGCAACTCTGCGCCGGGGCCTGCGACCCGCGAGGCGGGCTCGGCGCTGCTAGCA TTGCAGCAGACGGCGCTCCAAGAGGACCAGGAGAATATCAACCCGGAAAAGGCAGCGCCC GTCCAACAACCGCGGACCCGGGCCGCGCTGGCGGTACTGAAGTCCGGGAACCCGCGGGGT CTAGCGCAGCAGCAGAGGCCGAAGACGAGACGGGTTGCACCCCTTAAGGATCTTCCTGTA AATGATGAGCATGTCACCGTTCCTCCTTGGAAAGCAAACAGTAAACAGCCTGCGTTCACC ATTCATGTGGATGAAGCAGAAAAAGAAGCTCAGAAGAAGCCAGCTGAATCTCAAAAAATA GAGCGTGAAGATGCCCTGGCTTTTAATTCAGCCATTAGTTTACCTGGACCCAGAAAACCA TTGGTCCCTCTTGATTATCCAATGGATGGTAGTTTTGAGTCACCACATACTATGGACATG TCAATTGTATTAGAAGATGAAAAGCCAGTGAGTGTTAATGAAGTACCAGACTACCATGAG GATATTCACACATACCTTAGGGAAATGGAGGTTAAATGTAAACCTAAAGTGGGTTACATG AAGAAACAGCCAGACATCACTAACAGTATGAGAGCTATCCTCGTGGACTGGTTAGTTGAA GTAGGAGAAGAATATAAACTACAGAATGAGACCCTGCATTTGGCTGTGAACTACATTGAT AGGTTCCTGTCTTCCATGTCAGTGCTGAGAGGAAAACTTCAGCTTGTGGGCACTGCTGCT ATGCTGTTAGCCTCAAAGTTTGAAGAAATATACCCCCCAGAAGTAGCAGAGTTTGTGTAC ATTACAGATGATACCTACACCAAGAAACAAGTTCTGAGAATGGAGCATCTAGTTTTGAAA GTCCTTACTTTTGACTTAGCTGCTCCAACAGTAAATCAGTTTCTTACCCAATACTTTCTG CATCAGCAGCCTGCAAACTGCAAAGTTGAAAGTTTAGCAATGTTTTTGGGAGAATTAAGT TTGATAGATGCTGACCCATACCTCAAGTATTTGCCATCAGTTATTGCTGGAGCTGCCTTT CATTTAGCACTCTACACAGTCACGGGACAAAGCTGGCCTGAATCATTAATACGAAAGACT GGATATACCCTGGAAAGTCTTAAGCCTTGTCTCATGGACCTTCACCAGACCTACCTCAAA GCACCACAGCATGCACAACAGTCAATAAGAGAAAAGTACAAAAATTCAAAGTATCATGGT GTTTCTCTCCTCAACCCACCAGAGACACTAAATCTGTAA PF02984 Cyclin_C PF00134 Cyclin_N component intracellular membrane-bound organelle component nucleus component organelle component membrane-bound organelle process regulation of biological process process regulation of physiological process process regulation of cellular physiological process process regulation of cell cycle process regulation of progression through cell cycle "
drug:(2R)-2-{[4-(benzylamino)-8-(1-methylethyl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-olrdfs:label"(2R)-2-{[4-(benzylamino)-8-(1-methylethyl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-ol"
drug:(2R)-2-{[4-(benzylamino)-8-(1-methylethyl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-olrdf:typedrugbank:drugs
drug:(2R)-3-(phosphonooxy)propane-1,2-diyl diheptanoatedrugbank:description" experimental This compound belongs to the phosphatidic acids. These are glycerophosphates in which the glycerol moeity is bonded to two aliphatic chains through ester linkages. Phosphatidic Acids Organic Compounds Lipids Glycerophospholipids Glycerophosphates Fatty Acid Esters Organophosphate Esters Organic Phosphoric Acids Dicarboxylic Acids and Derivatives Carboxylic Acid Esters Enolates Ethers Polyamines fatty acid ester phosphoric acid ester dicarboxylic acid derivative organic phosphate carboxylic acid ester enolate ether polyamine carboxylic acid derivative logP 2.77 ALOGPS logS -3.3 ALOGPS Water Solubility 2.00e-01 g/l ALOGPS logP 3.88 ChemAxon IUPAC Name [(2R)-2,3-bis(heptanoyloxy)propoxy]phosphonic acid ChemAxon Traditional IUPAC Name (2R)-2,3-bis(heptanoyloxy)propoxyphosphonic acid ChemAxon Molecular Weight 396.4129 ChemAxon Monoisotopic Weight 396.191304544 ChemAxon SMILES [H][C@@](COC(=O)CCCCCC)(COP(O)(O)=O)OC(=O)CCCCCC ChemAxon Molecular Formula C17H33O8P ChemAxon InChI InChI=1S/C17H33O8P/c1-3-5-7-9-11-16(18)23-13-15(14-24-26(20,21)22)25-17(19)12-10-8-6-4-2/h15H,3-14H2,1-2H3,(H2,20,21,22)/t15-/m1/s1 ChemAxon InChIKey InChIKey=JAXUAGQDLYDLQB-OAHLLOKOSA-N ChemAxon Polar Surface Area (PSA) 119.36 ChemAxon Refractivity 95.75 ChemAxon Polarizability 42.29 ChemAxon Rotatable Bond Count 18 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 1.32 ChemAxon pKa (strongest basic) -6.7 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 23629653 PubChem Substance 99444847 ChemSpider 24700518 PDB PD7 BE0004291 Phospholipase D Streptomyces antibioticus # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Phospholipase D Involved in NAPE-specific phospholipase D activity A phosphatidylcholine + H(2)O = choline + a phosphatidate Secreted None 6.39 58931.5 Streptomyces antibioticus GenBank Gene Database D16444 GenBank Protein Database 517155 UniProtKB Q53728 UniProt Accession PLD_STRAT Choline phosphatase >Phospholipase D MTSDQRPARLPTHKGKLLAPHRLHRLIPVSVALTTVCAALPSSTAYAADTPPTPHLDAIE RSLRDTSPGLEGSVWQRTDGNRLDAPDGDPAGWLLQTPGCWGDAGCKDRAGTRRLLDKMT RNIADARHTVDISSLAPFPNGGFEDAVVDGLKAVVAAGHSPRVRILVGAAPIYHLNVVPS RYRDELIGKLGAAAGKVTLNVASMTTSKTSLSWNHSKLLVVDGKTAITGGINGWKDDYLD TAHPVSDVDMALSGPAAASAGKYLDTLWDWTCRNASDPAKVWLATSNGASCMPSMEQDEA GSAPAEPTGDVPVIAVGGLGVGIKESDPSSGYHPDLPTAPDTKCTVGLHDNTNADRDYDT VNPEENALRSLIASARSHVEISQQDLNATCPPLPRYDIRTYDTLAGKLAAGVKVRIVVSD PANRGAVGSGGYSQIKSLDEISDTLRTRLVALTGDNEKASRALCGNLQLASFRSSDAAKW ADGKPYALHHKLVSVDDSAFYIGSKNLYPAWLQDFGYIVESPAAAQQLKTELLDPEWKYS QQAAATPAGCPARQAG >1671 bp ATGACCAGTGATCAGCGCCCGGCTCGCCTCCCCACGCACAAAGGCAAGCTCTTGGCTCCT CACCGACTCCACCGCCTGATACCGGTGTCCGTCGCCCTGACGACCGTGTGCGCGGCACTG CCGTCCTCGACGGCCTACGCCGCGGACACACCGCCCACCCCCCATCTGGACGCCATCGAG CGGTCGCTGCGCGACACCTCCCCCGGCCTCGAAGGCTCGGTGTGGCAGCGCACGGACGGC AACCGCCTGGACGCCCCGGACGGCGACCCCGCCGGCTGGCTGCTGCAGACCCCCGGCTGC TGGGGCGACGCCGGCTGCAAGGACCGCGCCGGCACCCGGCGGCTGCTCGACAAGATGACC CGCAACATCGCCGACGCCCGGCACACCGTGGACATCTCCTCGCTGGCCCCCTTCCCCAAC GGCGGGTTCGAGGACGCGGTCGTCGACGGCCTCAAGGCGGTCGTCGCGGCGGGGCACTCC CCGCGGGTGCGCATCCTGGTCGGCGCCGCCCCGATCTACCACCTCAACGTGGTGCCGTCC CGCTACCGCGACGAGCTGATCGGCAAGCTCGGCGCGGCGGCCGGCAAGGTCACGCTCAAC GTCGCCTCGATGACCACGTCCAAGACGTCGCTCTCCTGGAACCACTCCAAGCTCCTCGTG GTCGACGGGAAGACGGCCATCACGGGCGGGATCAACGGCTGGAAGGACGACTACCTCGAC ACCGCCCACCCGGTGTCGGACGTGGACATGGCGCTCAGCGGCCCGGCCGCCGCCTCGGCG GGGAAGTACCTCGACACCCTCTGGGACTGGACCTGCCGCAACGCGTCCGACCCGGCCAAG GTGTGGCTCGCCACGTCGAACGGCGCCTCCTGCATGCCGTCGATGGAGCAGGACGAGGCG GGATCCGCCCCCGCCGAGCCCACCGGTGACGTCCCCGTCATCGCGGTCGGCGGCCTCGGC GTGGGCATCAAGGAGTCCGACCCCTCCTCGGGATACCACCCGGACCTGCCGACGGCCCCG GACACCAAGTGCACCGTGGGGCTGCACGACAACACCAACGCCGACCGCGACTACGACACG GTCAACCCCGAGGAGAACGCGCTGCGTTCGCTCATCGCCAGCGCGCGCAGCCACGTCGAG ATCTCCCAGCAGGACCTCAACGCCACCTGCCCGCCGTTGCCGCGCTACGACATCCGGACC TACGACACCCTCGCGGGCAAGCTGGCCGCCGGGGTCAAGGTCCGCATCGTCGTCAGCGAT CCCGCCAACCGCGGCGCCGTCGGCAGCGGGGGCTACTCCCAGATCAAGTCCCTGGACGAG ATCAGCGACACCCTCCGCACGCGTCTCGTCGCCCTGACCGGCGACAACGAGAAGGCGTCG CGGGCCCTGTGCGGCAACCTGCAGCTCGCCTCGTTCCGCAGCTCGGACGCCGCGAAGTGG GCCGACGGCAAGCCGTACGCGCTGCACCACAAGCTGGTGTCGGTGGACGACTCGGCGTTC TACATCGGCTCCAAGAACCTCTACCCGGCCTGGCTGCAGGACTTCGGCTACATCGTCGAG AGCCCCGCCGCGGCCCAGCAGCTCAAGACCGAGCTGCTCGACCCGGAGTGGAAGTACTCC CAGCAGGCGGCGGCCACCCCGGCCGGCTGCCCGGCTCGCCAGGCGGGCTGA PF00614 PLDc function catalytic activity process metabolism process physiological process "
drug:(2R)-3-(phosphonooxy)propane-1,2-diyl diheptanoaterdfs:label"(2R)-3-(phosphonooxy)propane-1,2-diyl diheptanoate"
drug:(2R)-3-(phosphonooxy)propane-1,2-diyl diheptanoaterdf:typedrugbank:drugs
drug:(2R)-3-{[(4Z)-5,6-DIPHENYL-6,7-DIHYDRO-4H-PYRROLO[2,3-D]PYRIMIDIN-4-YLIDENE]AMINO}PROPANE-1,2-DIOLdrugbank:description" experimental This compound belongs to the stilbenes. These are organic compounds containing a 1,2-diphenylethylene moiety. Stilbenes (C6-C2-C6 ) are derived from the common phenylpropene (C6-C3) skeleton building block. The introduction of one or more hydroxyl groups to a phenyl ring lead to stilbenoids. Stilbenes Organic Compounds Phenylpropanoids and Polyketides Stilbenes Phenylpyrroles Pyrrolopyrimidines Aminopyrimidines and Derivatives Benzene and Substituted Derivatives 1,2-Diols Secondary Alcohols 1,2-Aminoalcohols Polyamines Primary Alcohols Secondary Amines 3-phenylpyrrole 2-phenylpyrrole pyrrolopyrimidine aminopyrimidine pyrimidine substituted pyrrole benzene pyrrole 1,2-aminoalcohol secondary alcohol 1,2-diol secondary amine polyamine primary alcohol alcohol amine organonitrogen compound logP 2.58 ALOGPS logS -4.1 ALOGPS Water Solubility 2.75e-02 g/l ALOGPS logP 2.48 ChemAxon IUPAC Name (2R)-3-({5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl}amino)propane-1,2-diol ChemAxon Traditional IUPAC Name (2R)-3-({5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl}amino)propane-1,2-diol ChemAxon Molecular Weight 360.4091 ChemAxon Monoisotopic Weight 360.158625904 ChemAxon SMILES [H][C@](O)(CO)CNC1=C2C(NC(=C2C2=CC=CC=C2)C2=CC=CC=C2)=NC=N1 ChemAxon Molecular Formula C21H20N4O2 ChemAxon InChI InChI=1S/C21H20N4O2/c26-12-16(27)11-22-20-18-17(14-7-3-1-4-8-14)19(15-9-5-2-6-10-15)25-21(18)24-13-23-20/h1-10,13,16,26-27H,11-12H2,(H2,22,23,24,25)/t16-/m1/s1 ChemAxon InChIKey InChIKey=TWEONIHFGKSPLC-MRXNPFEDSA-N ChemAxon Polar Surface Area (PSA) 94.06 ChemAxon Refractivity 106.67 ChemAxon Polarizability 38.77 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 12.27 ChemAxon pKa (strongest basic) 7.07 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 4369435 PubChem Substance 99444119 ChemSpider 3571997 PDB DF2 BE0003382 Serine/threonine-protein kinase Chk1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Serine/threonine-protein kinase Chk1 Involved in protein kinase activity Required for checkpoint mediated cell cycle arrest in response to DNA damage or the presence of unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Recognizes the substrate consensus sequence [R-X-X- S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser- 293' promotes proteolysis of CDC25A. Inhibition of CDC25 activity leads to increased inhibitory tyrosine phosphorylation of CDK- cyclin complexes and blocks cell cycle progression. Binds to and phosphorylates RAD51 at 'Thr-309', which may enhance the association of RAD51 with chromatin and promote DNA repair by homologous recombination. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may affect chromatin assembly during S phase or DNA repair. May also phosphorylate multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and enhances suppression of cellular proliferation CHEK1 11q24-q24 Nucleus. Cytoplasm None 8.38 54420.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1925 GenAtlas CHEK1 GenBank Gene Database AF016582 UniProtKB O14757 UniProt Accession CHK1_HUMAN EC 2.7.11.1 >Serine/threonine-protein kinase Chk1 MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINK MLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVY LHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLK RREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLA LLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGFSKHIQSNLDF SPVNSASSEENVKYSSSQPEPRTGLSLWDTSPSYIDKLVQGISFSQPTCPDHMLLNSQLL GTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETCEKLGYQWKKSCMNQVTISTTDRR NNKLIFKVNLLEMDDKILVDFRLSKGDGLEFKRHFLKIKGKLIDIVSSQKVWLPAT >1431 bp ATGGCAGTGCCCTTTGTGGAAGACTGGGACTTGGTGCAAACCCTGGGAGAAGGTGCCTAT GGAGAAGTTCAACTTGCTGTGAATAGAGTAACTGAAGAAGCAGTCGCAGTGAAGATTGTA GATATGAAGCGTGCCGTAGACTGTCCAGAAAATATTAAGAAAGAGATCTGTATCAATAAA ATGCTAAATCATGAAAATGTAGTAAAATTCTATGGTCACAGGAGAGAAGGCAATATCCAA TATTTATTTCTGGAGTACTGTAGTGGAGGAGAGCTTTTTGACAGAATAGAGCCAGACATA GGCATGCCTGAACCAGATGCTCAGAGATTCTTCCATCAACTCATGGCAGGGGTGGTTTAT CTGCATGGTATTGGAATAACTCACAGGGATATTAAACCAGAAAATCTTCTGTTGGATGAA AGGGATAACCTCAAAATCTCAGACTTTGGCTTGGCAACAGTATTTCGGTATAATAATCGT GAGCGTTTGTTGAACAAGATGTGTGGTACTTTACCATATGTTGCTCCAGAACTTCTGAAG AGAAGAGAATTTCATGCAGAACCAGTTGATGTTTGGTCCTGTGGAATAGTACTTACTGCA ATGCTCGCTGGAGAATTGCCATGGGACCAACCCAGTGACAGCTGTCAGGAGTATTCTGAC TGGAAAGAAAAAAAAACATACCTCAACCCTTGGAAAAAAATCGATTCTGCTCCTCTAGCT CTGCTGCATAAAATCTTAGTTGAGAATCCATCAGCAAGAATTACCATTCCAGACATCAAA AAAGATAGATGGTACAACAAACCCCTCAAGAAAGGGGCAAAAAGGCCCCGAGTCACTTCA GGTGGTGTGTCAGAGTCTCCCAGTGGATTTTCTAAGCACATTCAATCCAATTTGGACTTC TCTCCAGTAAACAGTGCTTCTAGTGAAGAAAATGTGAAGTACTCCAGTTCTCAGCCAGAA CCCCGCACAGGTCTTTCCTTATGGGATACCAGCCCCTCATACATTGATAAATTGGTACAA GGGATCAGCTTTTCCCAGCCCACATGTCCTGATCATATGCTTTTGAATAGTCAGTTACTT GGCACCCCAGGATCCTCACAGAACCCCTGGCAGCGGTTGGTCAAAAGAATGACACGATTC TTTACCAAATTGGATGCAGACAAATCTTATCAATGCCTGAAAGAGACTTGTGAGAAGTTG GGCTATCAATGGAAGAAAAGTTGTATGAATCAGGTTACTATATCAACAACTGATAGGAGA AACAATAAACTCATTTTCAAAGTGAATTTGTTAGAAATGGATGATAAAATATTGGTTGAC TTCCGGCTTTCTAAGGGTGATGGATTGGAGTTCAAGAGACACTTCCTGAAGATTAAAGGG AAGCTGATTGATATTGTGAGCAGCCAGAAGGTTTGGCTTCCTGCCACATGA PF00069 Pkinase function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity process protein modification process physiological process process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification "
drug:(2R)-3-{[(4Z)-5,6-DIPHENYL-6,7-DIHYDRO-4H-PYRROLO[2,3-D]PYRIMIDIN-4-YLIDENE]AMINO}PROPANE-1,2-DIOLrdfs:label"(2R)-3-{[(4Z)-5,6-DIPHENYL-6,7-DIHYDRO-4H-PYRROLO[2,3-D]PYRIMIDIN-4-YLIDENE]AMINO}PROPANE-1,2-DIOL"
drug:(2R)-3-{[(4Z)-5,6-DIPHENYL-6,7-DIHYDRO-4H-PYRROLO[2,3-D]PYRIMIDIN-4-YLIDENE]AMINO}PROPANE-1,2-DIOLrdf:typedrugbank:drugs
drug:(2R)-3-{[(BENZYLAMINO)CARBONYL]AMINO}-2-HYDROXYPROPANOIC ACIDdrugbank:description" experimental This compound belongs to the benzene and substituted derivatives. These are aromatic compounds containing at least one benzene ring. Benzene and Substituted Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Alpha Hydroxy Acids and Derivatives Secondary Alcohols Enolates Carboxylic Acids Polyamines Aldehydes secondary alcohol enolate carboxylic acid derivative carboxylic acid polyamine organonitrogen compound amine alcohol aldehyde logP -0.25 ALOGPS logS -2.3 ALOGPS Water Solubility 1.08e+00 g/l ALOGPS logP -0.19 ChemAxon IUPAC Name (2R)-3-[(benzylcarbamoyl)amino]-2-hydroxypropanoic acid ChemAxon Traditional IUPAC Name (2R)-3-[(benzylcarbamoyl)amino]-2-hydroxypropanoic acid ChemAxon Molecular Weight 238.2399 ChemAxon Monoisotopic Weight 238.095356946 ChemAxon SMILES [H][C@@](O)(CNC(=O)NCC1=CC=CC=C1)C(O)=O ChemAxon Molecular Formula C11H14N2O4 ChemAxon InChI InChI=1S/C11H14N2O4/c14-9(10(15)16)7-13-11(17)12-6-8-4-2-1-3-5-8/h1-5,9,14H,6-7H2,(H,15,16)(H2,12,13,17)/t9-/m1/s1 ChemAxon InChIKey InChIKey=KGFDIRSBGRVEFZ-SECBINFHSA-N ChemAxon Polar Surface Area (PSA) 98.66 ChemAxon Refractivity 59.67 ChemAxon Polarizability 23.78 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 3.67 ChemAxon pKa (strongest basic) -2.1 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 24820112 PubChem Substance 99444478 PDB J54 BE0003758 Chymotrypsin-like elastase family member 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Chymotrypsin-like elastase family member 1 Involved in calcium ion binding Acts upon elastin CELA1 12q13 Secreted None 8.38 27798.0 Human HUGO Gene Nomenclature Committee (HGNC) GNC:3308 GeneCards CELA1 GenBank Gene Database AF120493 GenBank Protein Database 4731318 UniProtKB Q9UNI1 UniProt Accession CELA1_HUMAN Elastase-1 >Chymotrypsin-like elastase family member 1 MLVLYGHSTQDLPETNARVVGGTEAGRNSWPSQISLQYRSGGSRYHTCGGTLIRQNWVMT AAHCVDYQKTFRVVAGDHNLSQNDGTEQYVSVQKIVVHPYWNSDNVAAGYDIALLRLAQS VTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGQLAQTLQQAYLPSVDYAICSSSS YWGSTVKNTMVCAGGDGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFVSSRGCNVSRKPTV FTQVSAYISWINNVIASN >777 bp ATGCTGGTCCTTTATGGACACAGCACCCAGGACCTTCCGGAAACCAATGCCCGCGTAGTC GGAGGGACTGAGGCCGGGAGGAATTCCTGGCCCTCTCAGATTTCCCTCCAGTACCGGTCT GGAGGTTCCCGGTATCACACCTGTGGAGGGACCCTTATCAGACAGAACTGGGTGATGACA GCTGCTCACTGCGTGGATTACCAGAAGACTTTCCGCGTGGTGGCTGGAGACCATAACCTG AGCCAGAATGATGGCACTGAGCAGTACGTGAGTGTGCAGAAGATCGTGGTGCATCCATAC TGGAACAGCGATAACGTGGCTGCCGGCTATGACATCGCCCTGCTGCGCCTGGCCCAGAGC GTTACCCTCAATAGCTATGTCCAGCTGGGTGTTCTGCCCCAGGAGGGAGCCATCCTGGCT AACAACAGTCCCTGCTACATCACAGGCTGGGGCAAGACCAAGACCAATGGGCAGCTGGCC CAGACCCTGCAGCAGGCTTACCTGCCCTCTGTGGACTATGCCATCTGCTCCAGCTCCTCC TACTGGGGCTCCACTGTGAAGAACACCATGGTGTGTGCTGGTGGAGATGGAGTTCGCTCT GGATGCCAGGGTGACTCTGGGGGCCCCCTCCATTGCTTGGTGAATGGCAAGTATTCTCTC CATGGAGTGACCAGCTTTGTGTCCAGCCGGGGCTGTAATGTCTCCAGGAAGCCTACAGTC TTCACCCAGGTCTCTGCTTACATCTCCTGGATAAATAATGTCATCGCCTCCAACTGA PF00089 Trypsin function hydrolase activity function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity process metabolism process macromolecule metabolism process protein metabolism process cellular protein metabolism process proteolysis process physiological process "
drug:(2R)-3-{[(BENZYLAMINO)CARBONYL]AMINO}-2-HYDROXYPROPANOIC ACIDrdfs:label"(2R)-3-{[(BENZYLAMINO)CARBONYL]AMINO}-2-HYDROXYPROPANOIC ACID"
drug:(2R)-3-{[(BENZYLAMINO)CARBONYL]AMINO}-2-HYDROXYPROPANOIC ACIDrdf:typedrugbank:drugs
drug:(2R)-3-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-[(9E)-HEXADEC-9-ENOYLOXY]PROPYL (9E)-OCTADEC-9-ENOATEdrugbank:description" experimental This compound belongs to the phosphatidylglycerols. These are glycerophosphoglycerols in which two fatty acids are bonded to the 1-glycerol moiety through ester linkages. Phosphatidylglycerols Organic Compounds Lipids Glycerophospholipids Glycerophosphoglycerols Monosaccharide Phosphates Fatty Acid Esters Trioses Dicarboxylic Acids and Derivatives Organophosphate Esters Organic Phosphoric Acids Carboxylic Acid Esters 1,2-Diols Secondary Alcohols Enolates Ethers Primary Alcohols Polyamines monosaccharide phosphate fatty acid ester monosaccharide dicarboxylic acid derivative triose monosaccharide saccharide organic phosphate phosphoric acid ester 1,2-diol carboxylic acid ester secondary alcohol ether enolate polyamine carboxylic acid derivative primary alcohol alcohol logP 8.02 ALOGPS logS -6.8 ALOGPS Water Solubility 1.05e-04 g/l ALOGPS logP 11.1 ChemAxon IUPAC Name [(2R)-2,3-dihydroxypropoxy][(2R)-2-[(9Z)-hexadec-9-enoyloxy]-3-[(9Z)-octadec-9-enoyloxy]propoxy]phosphinic acid ChemAxon Traditional IUPAC Name (2R)-2,3-dihydroxypropoxy(2R)-2-[(9Z)-hexadec-9-enoyloxy]-3-[(9Z)-octadec-9-enoyloxy]propoxyphosphinic acid ChemAxon Molecular Weight 746.9913 ChemAxon Monoisotopic Weight 746.509785132 ChemAxon SMILES CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@H](CO[P@](O)(=O)OC[C@H](O)CO)OC(=O)CCCCCCC\C=C/CCCCCC ChemAxon Molecular Formula C40H75O10P ChemAxon InChI InChI=1S/C40H75O10P/c1-3-5-7-9-11-13-15-17-18-20-21-23-25-27-29-31-39(43)47-35-38(36-49-51(45,46)48-34-37(42)33-41)50-40(44)32-30-28-26-24-22-19-16-14-12-10-8-6-4-2/h14,16-18,37-38,41-42H,3-13,15,19-36H2,1-2H3,(H,45,46)/b16-14-,18-17-/t37-,38-/m1/s1 ChemAxon InChIKey InChIKey=QGIXWNRQEFVVRM-CTDKCSBDSA-N ChemAxon Polar Surface Area (PSA) 148.82 ChemAxon Refractivity 206.74 ChemAxon Polarizability 89.88 ChemAxon Rotatable Bond Count 40 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 1.89 ChemAxon pKa (strongest basic) -3 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 0 ChemAxon Bioavailability 0 ChemAxon PubChem Compound 5288113 PubChem Substance 46507864 PDB DR9 BE0003359 Steroidogenic factor 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Steroidogenic factor 1 Involved in transcription factor activity Seems to be essential for sexual differentiation and formation of the primary steroidogenic tissues. Binds to the Ad4 site found in the promoter region of steroidogenic P-450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the Muellerian inhibiting substance (AMH) gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1/FTZF1. The SFPQ-NONO- NR5A1/SF-1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. Binds phospholipids with a phosphatidylinositol (PI) headgroup, in particular PI(3,4)P2 and PI(3,4,5)P3 NR5A1 9q33 Nucleus None 7.73 51637.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7983 GenAtlas NR5A1 GenBank Gene Database U76388 IUPHAR 632 Guide to Pharmacology 112 UniProtKB Q13285 UniProt Accession STF1_HUMAN Adrenal 4-binding protein Fushi tarazu factor homolog 1 SF-1 Steroid hormone receptor Ad4BP STF-1 >Steroidogenic factor 1 MDYSYDEDLDELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKHYTCTESQSCKIDKT QRKRCPFCRFQKCLTVGMRLEAVRADRMRGGRNKFGPMYKRDRALKQQKKAQIRANGFKL ETGPPMGVPPPPPPAPDYVLPPSLHGPEPKGLAAGPPAGPLGDFGAPALPMAVPGAHGPL AGYLYPAFPGRAIKSEYPEPYASPPQPGLPYGYPEPFSGGPNVPELILQLLQLEPDEDQV RARILGCLQEPTKSRPDQPAAFGLLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQN CWSELLVFDHIYRQVQHGKEGSILLVTGQEVELTTVATQAGSLLHSLVLRAQELVLQLLA LQLDRQEFVCLKFIILFSLDLKFLNNHILVKDAQEKANAALLDYTLCHYPHCGDKFQQLL LCLVEVRALSMQAKEYLYHKHLGNEMPRNNLLIEMLQAKQT >1386 bp ATGGACTATTCGTACGACGAGGACCTGGACGAGCTGTGCCCCGTGTGCGGGGACAAGGTG TCCGGCTACCACTACGGACTGCTCACGTGTGAGAGCTGCAAGGGCTTCTTCAAGCGCACG GTGCAGAACAACAAGCACTACACGTGCACCGAGAGCCAGAGCTGCAAGATCGACAAGACG CAGCGCAAGCGCTGTCCCTTCTGCCGCTTCCAGAAATGCCTGACGGTGGGGATGCGCCTG GAAGCCGTGCGCGCTGACCGTATGAGGGGTGGCCGGAACAAGTTTGGGCCGATGTACAAG CGGGACCGGGCCCTGAAACAGCAGAAGAAGGCACAGATTCGGGCCAATGGCTTCAAGCTG GAGACAGGGCCCCCGATGGGGGTGCCCCCGCCGCCCCCTCCCGCACCGGACTACGTGCTG CCTCCCAGCCTGCATGGGCCTGAGCCCAAGGGCCTGGCCGCCGGTCCACCTGCTGGGCCA CTGGGCGACTTTGGGGCCCCAGCACTGCCCATGGCCGTGCCCGGTGCCCACGGGCCACTG GCTGGCTACCTCTACCCTGCCTTTCCTGGCCGTGCCATCAAGTCTGAGTACCCGGAGCCT TATGCCAGCCCCCCACAGCCTGGGCTGCCGTACGGCTACCCAGAGCCCTTCTCTGGAGGC CCCAACGTGCCTGAGCTCATCCTGCAGCTGCTGCAGCTGGAGCCGGATGAGGACCAGGTG CGGGCCCGCATCTTGGGCTGCCTGCAGGAGCCCACCAAAAGCCGCCCCGACCAGCCGGCG GCCTTCGGCCTCCTGTGCAGAATGGCCGACCAGACCTTCATCTCCATCGTGGACTGGGCA CGCAGGTGCATGGTCTTCAAGGAGCTGGAGGTGGCCGACCAGATGACGCTGCTGCAGAAC TGCTGGAGCGAGCTGCTGGTGTTCGACCACATCTACCGCCAGGTCCAGCACGGCAAGGAG GGCAGCATCCTGCTGGTCACCGGGCAGGAGGTGGAGCTGACCACAGTGGCCACCCAGGCG GGCTCGCTGCTGCACAGCCTGGTGTTGCGGGCGCAGGAGCTGGTGCTGCAGCTGCTTGCG CTGCAGCTGGACCGGCAGGAGTTTGTCTGCCTCAAGTTCATCATCCTCTTCAGCCTGGAT TTGAAGTTCCTGAATAACCACATCCTGGTGAAAGACGCTCAGGAGAAGGCCAACGCCGCC CTGCTTGACTACACCCTGTGCCACTACCCGCACTGCGGGGACAAATTCCAGCAGCTGCTG CTGTGCCTGGTGGAGGTGCGGGCCCTGAGCATGCAGGCCAAGGAGTACCTGTACCACAAG CACCTGGGCAACGAGATGCCCCGCAACAACCTGCTCATCGAAATGCTGCAAGCCAAGCAG ACTTGA PF00104 Hormone_recep PF00105 zf-C4 component membrane-bound organelle component intracellular membrane-bound organelle component nucleus component organelle function signal transducer activity function receptor activity function nucleic acid binding function steroid hormone receptor activity function transcription factor activity function ligand-dependent nuclear receptor activity function DNA binding function binding process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent process regulation of biological process process regulation of physiological process "
drug:(2R)-3-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-[(9E)-HEXADEC-9-ENOYLOXY]PROPYL (9E)-OCTADEC-9-ENOATErdfs:label"(2R)-3-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-[(9E)-HEXADEC-9-ENOYLOXY]PROPYL (9E)-OCTADEC-9-ENOATE"
drug:(2R)-3-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-2-[(9E)-HEXADEC-9-ENOYLOXY]PROPYL (9E)-OCTADEC-9-ENOATErdf:typedrugbank:drugs
drug:(2R)-4,4-dihydroxy-5-nitro-2-(phenylmethyl)pentanoic aciddrugbank:description" experimental This compound belongs to the phenylpropanoic acids. These are compounds whose structure contain a benzene ring conjugated to a propanoic acid. Phenylpropanoic Acids Organic Compounds Phenylpropanoids and Polyketides Phenylpropanoic Acids Benzene and Substituted Derivatives Nitro Compounds Polyols Nitronic Acids Enolates Polyamines Carboxylic Acids Carbonyl Hydrates Organic Oxoazanium Compounds benzene nitronic acid nitro compound polyol carbonyl hydrate enolate carboxylic acid derivative carboxylic acid organic oxoazanium polyamine organonitrogen compound amine logP 0.24 ALOGPS logS -2.4 ALOGPS Water Solubility 9.74e-01 g/l ALOGPS logP 1.1 ChemAxon IUPAC Name (2R)-2-benzyl-4,4-dihydroxy-5-nitropentanoic acid ChemAxon Traditional IUPAC Name (2R)-2-benzyl-4,4-dihydroxy-5-nitropentanoic acid ChemAxon Molecular Weight 269.2506 ChemAxon Monoisotopic Weight 269.089937217 ChemAxon SMILES [H][C@@](CC1=CC=CC=C1)(CC(O)(O)C[N+]([O-])=O)C(O)=O ChemAxon Molecular Formula C12H15NO6 ChemAxon InChI InChI=1S/C12H15NO6/c14-11(15)10(6-9-4-2-1-3-5-9)7-12(16,17)8-13(18)19/h1-5,10,16-17H,6-8H2,(H,14,15)/t10-/m1/s1 ChemAxon InChIKey InChIKey=CGGNZMVODZPHHK-SNVBAGLBSA-N ChemAxon Polar Surface Area (PSA) 123.58 ChemAxon Refractivity 64.94 ChemAxon Polarizability 24.95 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 3.9 ChemAxon pKa (strongest basic) -4.4 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 44176354 PubChem Substance 99443955 PDB BPX BE0003753 Carboxypeptidase A1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Carboxypeptidase A1 Amino acid transport and metabolism Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro CPA1 7q32 Secreted None 5.55 47139.9 Human HUGO Gene Nomenclature Committee (HGNC) GNC:2296 GeneCards CPA1 GenBank Gene Database X67318 GenBank Protein Database 35330 UniProtKB P15085 UniProt Accession CBPA1_HUMAN >Carboxypeptidase A1 MRGLLVLSVLLGAVFGKEDFVGHQVLRISVADEAQVQKVKELEDLEHLQLDFWRGPAHPG SPIDVRVPFPSIQAVKIFLESHGISYETMIEDVQSLLDEEQEQMFAFRSRARSTDTFNYA TYHTLEEIYDFLDLLVAENPHLVSKIQIGNTYEGRPIYVLKFSTGGSKRPAIWIDTGIHS REWVTQASGVWFAKKITQDYGQDAAFTAILDTLDIFLEIVTNPDGFAFTHSTNRMWRKTR SHTAGSLCIGVDPNRNWDAGFGLSGASSNPCSETYHGKFANSEVEVKSIVDFVKDHGNIK AFISIHSYSQLLMYPYGYKTEPVPDQDELDQLSKAAVTALASLYGTKFNYGSIIKAIYQA SGSTIDWTYSQGIKYSFTFELRDTGRYGFLLPASQIIPTAKETWLALLTIMEHTLNHPY >1260 bp ATGCGGGGGTTGCTGGTGTTGAGTGTCCTGTTGGGGGCTGTCTTTGGCAAGGAGGACTTT GTGGGGCATCAGGTGCTCCGAATCTCTGTAGCCGATGAGGCCCAGGTACAGAAGGTGAAG GAGCTGGAGGACCTGGAGCACCTGCAGCTGGACTTCTGGCGGGGGCCTGCCCACCCTGGC TCCCCCATCGACGTCCGAGTGCCCTTCCCCAGCATCCAGGCGGTCAAGATCTTTCTGGAG TCCCACGGCATCAGCTATGAGACCATGATCGAGGACGTGCAGTCGCTGCTGGACGAGGAG CAGGAGCAGATGTTCGCCTTCCGGTCCCGGGCGCGCTCCACCGACACTTTTAACTACGCC ACCTACCACACCCTGGAGGAGATCTATGACTTCCTGGACCTGCTGGTGGCGGAGAACCCG CACCTTGTCAGCAAGATCCAGATTGGCAACACCTATGAAGGGCGTCCCATTTATGTGCTG AAGTTCAGCACGGGGGGCAGTAAGCGTCCAGCCATCTGGATCGACACGGGCATCCATTCC CGGGAGTGGGTCACCCAGGCCAGTGGGGTCTGGTTTGCAAAGAAGATCACTCAAGACTAT GGGCAGGATGCAGCTTTCACCGCCATTCTCGACACCTTGGACATCTTCCTGGAGATCGTC ACCAACCCTGATGGCTTTGCCTTCACGCACAGCACGAATCGCATGTGGCGCAAGACTCGG TCCCACACAGCAGGCTCCCTCTGTATTGGCGTGGACCCCAACAGGAACTGGGACGCTGGC TTTGGGTTGTCCGGAGCCAGCAGTAACCCCTGCTCGGAGACTTACCACGGCAAGTTTGCC AATTCCGAAGTGGAGGTCAAGTCCATTGTAGACTTTGTGAAGGACCATGGGAACATCAAG GCCTTCATCTCCATCCACAGCTACTCCCAGCTCCTCATGTATCCCTATGGCTACAAAACA GAACCAGTCCCTGACCAGGATGAGCTGGATCAGCTTTCCAAGGCTGCTGTGACAGCCCTG GCCTCTCTCTACGGGACCAAGTTCAACTATGGCAGCATCATCAAGGCAATTTATCAAGCC AGTGGAAGCACTATTGACTGGACCTACAGCCAGGGCATCAAGTACTCCTTCACCTTCGAG CTCCGGGACACTGGGCGCTATGGCTTCCTGCTGCCAGCCTCCCAGATCATCCCCACAGCC AAGGAGACGTGGCTGGCGCTTCTGACCATCATGGAGCACACCCTGAATCACCCCTACTGA PF00246 Peptidase_M14 PF02244 Propep_M14 function peptidase activity function exopeptidase activity function carboxypeptidase activity function metallocarboxypeptidase activity function catalytic activity function carboxypeptidase A activity function hydrolase activity process protein metabolism process cellular protein metabolism process proteolysis process physiological process process metabolism process macromolecule metabolism "
drug:(2R)-4,4-dihydroxy-5-nitro-2-(phenylmethyl)pentanoic acidrdfs:label"(2R)-4,4-dihydroxy-5-nitro-2-(phenylmethyl)pentanoic acid"
drug:(2R)-4,4-dihydroxy-5-nitro-2-(phenylmethyl)pentanoic acidrdf:typedrugbank:drugs
drug:(2R)-4-(2-BENZOYL-1,2-DIAZEPAN-1-YL)-4-OXO-1-(2,4,5-TRIFLUOROPHENYL)BUTAN-2-AMINEdrugbank:description" experimental This compound belongs to the beta amino acids and derivatives. These are amino acids having a (-NH2) group attached to the beta carbon atom. Beta Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Amphetamines and Derivatives Benzamides Benzoyl Derivatives Fluorobenzenes Aryl Fluorides Carboxylic Acid Hydrazides Enolates Carboxylic Acid Amides Polyamines Hydrazines and Derivatives Organofluorides Monoalkylamines benzamide benzoyl fluorobenzene aryl fluoride aryl halide benzene carboxamide group carboxylic acid hydrazide polyamine enolate organofluoride organohalogen hydrazine derivative amine primary amine primary aliphatic amine organonitrogen compound logP 2.33 ALOGPS logS -4.2 ALOGPS Water Solubility 2.36e-02 g/l ALOGPS logP 3.35 ChemAxon IUPAC Name (3R)-3-amino-1-(2-benzoyl-1,2-diazepan-1-yl)-4-(2,4,5-trifluorophenyl)butan-1-one ChemAxon Traditional IUPAC Name (3R)-3-amino-1-(2-benzoyl-1,2-diazepan-1-yl)-4-(2,4,5-trifluorophenyl)butan-1-one ChemAxon Molecular Weight 419.4401 ChemAxon Monoisotopic Weight 419.182061642 ChemAxon SMILES [H][C@](N)(CC(=O)N1CCCCCN1C(=O)C1=CC=CC=C1)CC1=C(F)C=C(F)C(F)=C1 ChemAxon Molecular Formula C22H24F3N3O2 ChemAxon InChI InChI=1S/C22H24F3N3O2/c23-18-14-20(25)19(24)12-16(18)11-17(26)13-21(29)27-9-5-2-6-10-28(27)22(30)15-7-3-1-4-8-15/h1,3-4,7-8,12,14,17H,2,5-6,9-11,13,26H2/t17-/m1/s1 ChemAxon InChIKey InChIKey=XXRHRPGYYNOBHO-QGZVFWFLSA-N ChemAxon Polar Surface Area (PSA) 66.64 ChemAxon Refractivity 107.68 ChemAxon Polarizability 40.76 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 8.48 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 16739331 PubChem Substance 99444522 ChemSpider 20570732 PDB KR2 BE0000854 Dipeptidyl peptidase 4 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dipeptidyl peptidase 4 Amino acid transport and metabolism Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Plays a role in T-cell activation DPP4 2q24.3 Cell membrane; single-pass type II membrane protein. Processed form:Secreted protein. Note=Also exis 7-28 5.92 88279.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3009 GenAtlas DPP4 GeneCards DPP4 GenBank Gene Database U13735 GenBank Protein Database 535388 UniProtKB P27487 UniProt Accession DPP4_HUMAN ADABP Adenosine deaminase complexing protein 2 Dipeptidyl peptidase IV DPP IV EC 3.4.14.5 T-cell activation antigen CD26 TP103 >Dipeptidyl peptidase 4 MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSL RWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNY VKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNL PSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYL CDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPS EPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISN EYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKY PLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGT FEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWE YYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP >2301 bp ATGAAGACACCGTGGAAGGTTCTTCTGGGACTGCTGGGTGCTGCTGCGCTTGTCACCATC ATCACCGTGCCCGTGGTTCTGCTGAACAAAGGCACAGATGATGCTACAGCTGACAGTCGC AAAACTTACACTCTAACTGATTACTTAAAAAATACTTATAGACTGAAGTTATACTCCTTA AGATGGATTTCAGATCATGAATATCTCTACAAACAAGAAAATAATATCTTGGTATTCAAT GCTGAATATGGAAACAGCTCAGTTTTCTTGGAGAACAGTACATTTGATGAGTTTGGACAT TCTATCAATGATTATTCAATATCTCCTGATGGGCAGTTTATTCTCTTAGAATACAACTAC GTGAAGCAATGGAGGCATTCCTACACAGCTTCATATGACATTTATGATTTAAATAAAAGG CAGCTGATTACAGAAGAGAGGATTCCAAACAACACACAGTGGGTCACATGGTCACCAGTG GGTCATAAATTGGCATATGTTTGGAACAATGACATTTATGTTAAAATTGAACCAAATTTA CCAAGTTACAGAATCACATGGACGGGGAAAGAAGATATAATATATAATGGAATAACTGAC TGGGTTTATGAAGAGGAAGTCTTCAGTGCCTACTCTGCTCTGTGGTGGTCTCCAAACGGC ACTTTTTTAGCATATGCCCAATTTAACGACACAGAAGTCCCACTTATTGAATACTCCTTC TACTCTGATGAGTCACTGCAGTACCCAAAGACTGTACGGGTTCCATATCCAAAGGCAGGA GCTGTGAATCCAACTGTAAAGTTCTTTGTTGTAAATACAGACTCTCTCAGCTCAGTCACC AATGCAACTTCCATACAAATCACTGCTCCTGCTTCTATGTTGATAGGGGATCACTACTTG TGTGATGTGACATGGGCAACACAAGAAAGAATTTCTTTGCAGTGGCTCAGGAGGATTCAG AACTATTCGGTCATGGATATTTGTGACTATGATGAATCCAGTGGAAGATGGAACTGCTTA GTGGCACGGCAACACATTGAAATGAGTACTACTGGCTGGGTTGGAAGATTTAGGCCTTCA GAACCTCATTTTACCCTTGATGGTAATAGCTTCTACAAGATCATCAGCAATGAAGAAGGT TACAGACACATTTGCTATTTCCAAATAGATAAAAAAGACTGCACATTTATTACAAAAGGC ACCTGGGAAGTCATCGGGATAGAAGCTCTAACCAGTGATTATCTATACTACATTAGTAAT GAATATAAAGGAATGCCAGGAGGAAGGAATCTTTATAAAATCCAACTTAGTGACTATACA AAAGTGACATGCCTCAGTTGTGAGCTGAATCCGGAAAGGTGTCAGTACTATTCTGTGTCA TTCAGTAAAGAGGCGAAGTATTATCAGCTGAGATGTTCCGGTCCTGGTCTGCCCCTCTAT ACTCTACACAGCAGCGTGAATGATAAAGGGCTGAGAGTCCTGGAAGACAATTCAGCTTTG GATAAAATGCTGCAGAATGTCCAGATGCCCTCCAAAAAACTGGACTTCATTATTTTGAAT GAAACAAAATTTTGGTATCAGATGATCTTGCCTCCTCATTTTGATAAATCCAAGAAATAT CCTCTACTATTAGATGTGTATGCAGGCCCATGTAGTCAAAAAGCAGACACTGTCTTCAGA CTGAACTGGGCCACTTACCTTGCAAGCACAGAAAACATTATAGTAGCTAGCTTTGATGGC AGAGGAAGTGGTTACCAAGGAGATAAGATCATGCATGCAATCAACAGAAGACTGGGAACA TTTGAAGTTGAAGATCAAATTGAAGCAGCCAGACAATTTTCAAAAATGGGATTTGTGGAC AACAAACGAATTGCAATTTGGGGCTGGTCATATGGAGGGTACGTAACCTCAATGGTCCTG GGATCGGGAAGTGGCGTGTTCAAGTGTGGAATAGCCGTGGCGCCTGTATCCCGGTGGGAG TACTATGACTCAGTGTACACAGAACGTTACATGGGTCTCCCAACTCCAGAAGACAACCTT GACCATTACAGAAATTCAACAGTCATGAGCAGAGCTGAAAATTTTAAACAAGTTGAGTAC CTCCTTATTCATGGAACAGCAGATGATAACGTTCACTTTCAGCAGTCAGCTCAGATCTCC AAAGCCCTGGTCGATGTTGGAGTGGATTTCCAGGCAATGTGGTATACTGATGAAGACCAT GGAATAGCTAGCAGCACAGCACACCAACATATATATACCCACATGAGCCACTTCATAAAA CAATGTTTCTCTTTACCTTAG PF00930 DPPIV_N PF00326 Peptidase_S9 component cell component membrane function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function serine-type peptidase activity function hydrolase activity function dipeptidyl-peptidase IV activity function prolyl oligopeptidase activity process protein metabolism process cellular protein metabolism process physiological process process proteolysis process metabolism process macromolecule metabolism "
drug:(2R)-4-(2-BENZOYL-1,2-DIAZEPAN-1-YL)-4-OXO-1-(2,4,5-TRIFLUOROPHENYL)BUTAN-2-AMINErdfs:label"(2R)-4-(2-BENZOYL-1,2-DIAZEPAN-1-YL)-4-OXO-1-(2,4,5-TRIFLUOROPHENYL)BUTAN-2-AMINE"
drug:(2R)-4-(2-BENZOYL-1,2-DIAZEPAN-1-YL)-4-OXO-1-(2,4,5-TRIFLUOROPHENYL)BUTAN-2-AMINErdf:typedrugbank:drugs
drug:(2R)-4-[(8R)-8-METHYL-2-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[1,5-A]PYRAZIN-7(8H)-YL]-4-OXO-1-(2,4,5-TRIFLUOROPHENYL)BUTAN-2-AMINEdrugbank:description" experimental This compound belongs to the beta amino acids and derivatives. These are amino acids having a (-NH2) group attached to the beta carbon atom. Beta Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Amphetamines and Derivatives Fluorobenzenes Aryl Fluorides Triazoles Tertiary Carboxylic Acid Amides Tertiary Amines Polyamines Enolates Carboxylic Acids Monoalkylamines Organofluorides Alkyl Fluorides fluorobenzene aryl fluoride benzene aryl halide azole 1,2,4-triazole tertiary carboxylic acid amide tertiary amine carboxamide group enolate polyamine carboxylic acid amine organohalogen organofluoride primary aliphatic amine primary amine alkyl halide alkyl fluoride organonitrogen compound logP 2.16 ALOGPS logS -4.2 ALOGPS Water Solubility 2.79e-02 g/l ALOGPS logP 2.8 ChemAxon IUPAC Name (3R)-3-amino-1-[(4R)-4-methyl-2-(trifluoromethyl)-4H,5H,6H,7H-[1,2,4]triazolo[1,5-a]pyrazin-5-yl]-4-(2,4,5-trifluorophenyl)butan-1-one ChemAxon Traditional IUPAC Name (3R)-3-amino-1-[(4R)-4-methyl-2-(trifluoromethyl)-4H,6H,7H-[1,2,4]triazolo[1,5-a]pyrazin-5-yl]-4-(2,4,5-trifluorophenyl)butan-1-one ChemAxon Molecular Weight 421.3402 ChemAxon Monoisotopic Weight 421.133729421 ChemAxon SMILES [H][C@](N)(CC(=O)N1CCN2N=C(N=C2[C@@]1([H])C)C(F)(F)F)CC1=C(F)C=C(F)C(F)=C1 ChemAxon Molecular Formula C17H17F6N5O ChemAxon InChI InChI=1S/C17H17F6N5O/c1-8-15-25-16(17(21,22)23)26-28(15)3-2-27(8)14(29)6-10(24)4-9-5-12(19)13(20)7-11(9)18/h5,7-8,10H,2-4,6,24H2,1H3/t8-,10-/m1/s1 ChemAxon InChIKey InChIKey=FDEXEPZGMKFCTG-PSASIEDQSA-N ChemAxon Polar Surface Area (PSA) 77.04 ChemAxon Refractivity 102.18 ChemAxon Polarizability 34.86 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 8.78 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 23661697 PubChem Substance 99443552 ChemSpider 24682467 PDB 448 BE0000854 Dipeptidyl peptidase 4 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dipeptidyl peptidase 4 Amino acid transport and metabolism Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Plays a role in T-cell activation DPP4 2q24.3 Cell membrane; single-pass type II membrane protein. Processed form:Secreted protein. Note=Also exis 7-28 5.92 88279.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3009 GenAtlas DPP4 GeneCards DPP4 GenBank Gene Database U13735 GenBank Protein Database 535388 UniProtKB P27487 UniProt Accession DPP4_HUMAN ADABP Adenosine deaminase complexing protein 2 Dipeptidyl peptidase IV DPP IV EC 3.4.14.5 T-cell activation antigen CD26 TP103 >Dipeptidyl peptidase 4 MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSL RWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNY VKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNL PSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYL CDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPS EPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISN EYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKY PLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGT FEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWE YYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP >2301 bp ATGAAGACACCGTGGAAGGTTCTTCTGGGACTGCTGGGTGCTGCTGCGCTTGTCACCATC ATCACCGTGCCCGTGGTTCTGCTGAACAAAGGCACAGATGATGCTACAGCTGACAGTCGC AAAACTTACACTCTAACTGATTACTTAAAAAATACTTATAGACTGAAGTTATACTCCTTA AGATGGATTTCAGATCATGAATATCTCTACAAACAAGAAAATAATATCTTGGTATTCAAT GCTGAATATGGAAACAGCTCAGTTTTCTTGGAGAACAGTACATTTGATGAGTTTGGACAT TCTATCAATGATTATTCAATATCTCCTGATGGGCAGTTTATTCTCTTAGAATACAACTAC GTGAAGCAATGGAGGCATTCCTACACAGCTTCATATGACATTTATGATTTAAATAAAAGG CAGCTGATTACAGAAGAGAGGATTCCAAACAACACACAGTGGGTCACATGGTCACCAGTG GGTCATAAATTGGCATATGTTTGGAACAATGACATTTATGTTAAAATTGAACCAAATTTA CCAAGTTACAGAATCACATGGACGGGGAAAGAAGATATAATATATAATGGAATAACTGAC TGGGTTTATGAAGAGGAAGTCTTCAGTGCCTACTCTGCTCTGTGGTGGTCTCCAAACGGC ACTTTTTTAGCATATGCCCAATTTAACGACACAGAAGTCCCACTTATTGAATACTCCTTC TACTCTGATGAGTCACTGCAGTACCCAAAGACTGTACGGGTTCCATATCCAAAGGCAGGA GCTGTGAATCCAACTGTAAAGTTCTTTGTTGTAAATACAGACTCTCTCAGCTCAGTCACC AATGCAACTTCCATACAAATCACTGCTCCTGCTTCTATGTTGATAGGGGATCACTACTTG TGTGATGTGACATGGGCAACACAAGAAAGAATTTCTTTGCAGTGGCTCAGGAGGATTCAG AACTATTCGGTCATGGATATTTGTGACTATGATGAATCCAGTGGAAGATGGAACTGCTTA GTGGCACGGCAACACATTGAAATGAGTACTACTGGCTGGGTTGGAAGATTTAGGCCTTCA GAACCTCATTTTACCCTTGATGGTAATAGCTTCTACAAGATCATCAGCAATGAAGAAGGT TACAGACACATTTGCTATTTCCAAATAGATAAAAAAGACTGCACATTTATTACAAAAGGC ACCTGGGAAGTCATCGGGATAGAAGCTCTAACCAGTGATTATCTATACTACATTAGTAAT GAATATAAAGGAATGCCAGGAGGAAGGAATCTTTATAAAATCCAACTTAGTGACTATACA AAAGTGACATGCCTCAGTTGTGAGCTGAATCCGGAAAGGTGTCAGTACTATTCTGTGTCA TTCAGTAAAGAGGCGAAGTATTATCAGCTGAGATGTTCCGGTCCTGGTCTGCCCCTCTAT ACTCTACACAGCAGCGTGAATGATAAAGGGCTGAGAGTCCTGGAAGACAATTCAGCTTTG GATAAAATGCTGCAGAATGTCCAGATGCCCTCCAAAAAACTGGACTTCATTATTTTGAAT GAAACAAAATTTTGGTATCAGATGATCTTGCCTCCTCATTTTGATAAATCCAAGAAATAT CCTCTACTATTAGATGTGTATGCAGGCCCATGTAGTCAAAAAGCAGACACTGTCTTCAGA CTGAACTGGGCCACTTACCTTGCAAGCACAGAAAACATTATAGTAGCTAGCTTTGATGGC AGAGGAAGTGGTTACCAAGGAGATAAGATCATGCATGCAATCAACAGAAGACTGGGAACA TTTGAAGTTGAAGATCAAATTGAAGCAGCCAGACAATTTTCAAAAATGGGATTTGTGGAC AACAAACGAATTGCAATTTGGGGCTGGTCATATGGAGGGTACGTAACCTCAATGGTCCTG GGATCGGGAAGTGGCGTGTTCAAGTGTGGAATAGCCGTGGCGCCTGTATCCCGGTGGGAG TACTATGACTCAGTGTACACAGAACGTTACATGGGTCTCCCAACTCCAGAAGACAACCTT GACCATTACAGAAATTCAACAGTCATGAGCAGAGCTGAAAATTTTAAACAAGTTGAGTAC CTCCTTATTCATGGAACAGCAGATGATAACGTTCACTTTCAGCAGTCAGCTCAGATCTCC AAAGCCCTGGTCGATGTTGGAGTGGATTTCCAGGCAATGTGGTATACTGATGAAGACCAT GGAATAGCTAGCAGCACAGCACACCAACATATATATACCCACATGAGCCACTTCATAAAA CAATGTTTCTCTTTACCTTAG PF00930 DPPIV_N PF00326 Peptidase_S9 component cell component membrane function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function serine-type peptidase activity function hydrolase activity function dipeptidyl-peptidase IV activity function prolyl oligopeptidase activity process protein metabolism process cellular protein metabolism process physiological process process proteolysis process metabolism process macromolecule metabolism "
drug:(2R)-4-[(8R)-8-METHYL-2-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[1,5-A]PYRAZIN-7(8H)-YL]-4-OXO-1-(2,4,5-TRIFLUOROPHENYL)BUTAN-2-AMINErdfs:label"(2R)-4-[(8R)-8-METHYL-2-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[1,5-A]PYRAZIN-7(8H)-YL]-4-OXO-1-(2,4,5-TRIFLUOROPHENYL)BUTAN-2-AMINE"
drug:(2R)-4-[(8R)-8-METHYL-2-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,4]TRIAZOLO[1,5-A]PYRAZIN-7(8H)-YL]-4-OXO-1-(2,4,5-TRIFLUOROPHENYL)BUTAN-2-AMINErdf:typedrugbank:drugs
drug:(2R)-N-HYDROXY-2-[(3S)-3-METHYL-3-{4-[(2-METHYLQUINOLIN-4-YL)METHOXY]PHENYL}-2-OXOPYRROLIDIN-1-YL]PROPANAMIDEdrugbank:description" experimental This compound belongs to the phenylpyrrolidines. These are polycyclic aromatic compounds containing a benzene ring linked to a pyrrolidine ring through a CC or CN bond. Phenylpyrrolidines Organic Compounds Heterocyclic Compounds Pyrrolidines Phenylpyrrolidines Quinolines and Derivatives Phenol Ethers Alkyl Aryl Ethers Pyrrolidones Pyridines and Derivatives Tertiary Carboxylic Acid Amides Pyrroles Hydroxamic Acids Lactams Tertiary Amines Enolates Carboxylic Acids Polyamines phenol ether alkyl aryl ether pyrrolidone pyridine benzene pyrrole tertiary carboxylic acid amide tertiary amine carboxamide group hydroxamic acid lactam carboxylic acid derivative polyamine enolate ether carboxylic acid amine organonitrogen compound logP 3.8 ALOGPS logS -5 ALOGPS Water Solubility 4.14e-03 g/l ALOGPS logP 2.97 ChemAxon IUPAC Name (2R)-N-hydroxy-2-[(3S)-3-methyl-3-{4-[(2-methylquinolin-4-yl)methoxy]phenyl}-2-oxopyrrolidin-1-yl]propanamide ChemAxon Traditional IUPAC Name (2R)-N-hydroxy-2-[(3S)-3-methyl-3-{4-[(2-methylquinolin-4-yl)methoxy]phenyl}-2-oxopyrrolidin-1-yl]propanamide ChemAxon Molecular Weight 433.4996 ChemAxon Monoisotopic Weight 433.200156367 ChemAxon SMILES [H][C@](C)(N1CC[C@](C)(C1=O)C1=CC=C(OCC2=CC(C)=NC3=CC=CC=C23)C=C1)C(=O)NO ChemAxon Molecular Formula C25H27N3O4 ChemAxon InChI InChI=1S/C25H27N3O4/c1-16-14-18(21-6-4-5-7-22(21)26-16)15-32-20-10-8-19(9-11-20)25(3)12-13-28(24(25)30)17(2)23(29)27-31/h4-11,14,17,31H,12-13,15H2,1-3H3,(H,27,29)/t17-,25+/m1/s1 ChemAxon InChIKey InChIKey=YDMIPBHQKFOFQW-NSYGIPOTSA-N ChemAxon Polar Surface Area (PSA) 91.76 ChemAxon Refractivity 120.08 ChemAxon Polarizability 47.66 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 8.72 ChemAxon pKa (strongest basic) 5.02 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon ChEBI 40083 PubChem Compound 6914621 PubChem Substance 99443616 ChemSpider 5290501 PDB 541 BE0003754 Disintegrin and metalloproteinase domain-containing protein 17 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Disintegrin and metalloproteinase domain-containing protein 17 Involved in integrin binding Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Also involved in the activation of Notch pathway (By similarity) ADAM17 2p25 Membrane 672-692 5.5 93020.2 Human HUGO Gene Nomenclature Committee (HGNC) GNC:195 GeneCards ADAM17 GenBank Gene Database U86755 GenBank Protein Database 1857673 UniProtKB P78536 UniProt Accession ADA17_HUMAN ADAM 17 CD156b antigen Snake venom-like protease TNF-alpha convertase TNF-alpha-converting enzyme >Disintegrin and metalloproteinase domain-containing protein 17 MRQSLLFLTSVVPFVLAPRPPDDPGFGPHQRLEKLDSLLSDYDILSLSNIQQHSVRKRDL QTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQDFFTGHVV GEPDSRVLAHIRDDDVIIRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKNVSRLQS PKVCGYLKVDNEELLPKGLVDREPPEELVHRVKRRADPDPMKNTCKLLVVADHRFYRYMG RGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNM AKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANS HGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGL AECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGN SRVDEGEECDPGIMYLNNDTCCNSDCTLKEGVQCSDRNSPCCKNCQFETAQKKCQEAINA TCKGVSYCTGNSSECPPPGNAEDDTVCLDLGKCKDGKCIPFCEREQQLESCACNETDNSC KVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWDFIDQLS INTFGKFLADNIVGSVLVFSLIFWIPFSILVHCVDKKLDKQYESLSLFHPSNVEMLSSMD SASVRIIKPFPAPQTPGRLQPAPVIPSAPAAPKLDHQRMDTIQEDPSTDSHMDEDGFEKD PFPNSSTAAKSFEDLTDHPVTRSEKAASFKLQRQNRVDSKETEC >2475 bp ATGAGGCAGTCTCTCCTATTCCTGACCAGCGTGGTTCCTTTCGTGCTGGCGCCGCGACCT CCGGATGACCCGGGCTTCGGCCCCCACCAGAGACTCGAGAAGCTTGATTCTTTGCTCTCA GACTACGATATTCTCTCTTTATCTAATATCCAGCAGCATTCGGTAAGAAAAAGAGATCTA CAGACTTCAACACATGTAGAAACACTACTAACTTTTTCAGCTTTGAAAAGGCATTTTAAA TTATACCTGACATCAAGTACTGAACGTTTTTCACAAAATTTCAAGGTCGTGGTGGTGGAT GGTAAAAACGAAAGCGAGTACACTGTAAAATGGCAGGACTTCTTCACTGGACACGTGGTT GGTGAGCCTGACTCTAGGGTTCTAGCCCACATAAGAGATGATGATGTTATAATCAGAATC AACACAGATGGGGCCGAATATAACATAGAGCCACTTTGGAGATTTGTTAATGATACCAAA GACAAAAGAATGTTAGTTTATAAATCTGAAGATATCAAGAATGTTTCACGTTTGCAGTCT CCAAAAGTGTGTGGTTATTTAAAAGTGGATAATGAAGAGTTGCTCCCAAAAGGGTTAGTA GACAGAGAACCACCTGAAGAGCTTGTTCATCGAGTGAAAAGAAGAGCTGACCCAGATCCC ATGAAGAACACGTGTAAATTATTGGTGGTAGCAGATCATCGCTTCTACAGATACATGGGC AGAGGGGAAGAGAGTACAACTACAAATTACTTAATAGAGCTAATTGACAGAGTTGATGAC ATCTATCGGAACACTTCATGGGATAATGCAGGTTTTAAAGGCTATGGAATACAGATAGAG CAGATTCGCATTCTCAAGTCTCCACAAGAGGTAAAACCTGGTGAAAAGCACTACAACATG GCAAAAAGTTACCCAAATGAAGAAAAGGATGCTTGGGATGTGAAGATGTTGCTAGAGCAA TTTAGCTTTGATATAGCTGAGGAAGCATCTAAAGTTTGCTTGGCACACCTTTTCACATAC CAAGATTTTGATATGGGAACTCTTGGATTAGCTTATGTTGGCTCTCCCAGAGCAAACAGC CATGGAGGTGTTTGTCCAAAGGCTTATTATAGCCCAGTTGGGAAGAAAAATATCTATTTG AATAGTGGTTTGACGAGCACAAAGAATTATGGTAAAACCATCCTTACAAAGGAAGCTGAC CTGGTTACAACTCATGAATTGGGACATAATTTTGGAGCAGAACATGATCCGGATGGTCTA GCAGAATGTGCCCCGAATGAGGACCAGGGAGGGAAATATGTCATGTATCCCATAGCTGTG AGTGGCGATCACGAGAACAATAAGATGTTTTCAAACTGCAGTAAACAATCAATCTATAAG ACCATTGAAAGTAAGGCCCAGGAGTGTTTTCAAGAACGCAGCAATAAAGTTTGTGGGAAC TCGAGGGTGGATGAAGGAGAAGAGTGTGATCCTGGCATCATGTATCTGAACAACGACACC TGCTGCAACAGCGACTGCACGTTGAAGGAAGGTGTCCAGTGCAGTGACAGGAACAGTCCT TGCTGTAAAAACTGTCAGTTTGAGACTGCCCAGAAGAAGTGCCAGGAGGCGATTAATGCT ACTTGCAAAGGCGTGTCCTACTGCACAGGTAATAGCAGTGAGTGCCCGCCTCCAGGAAAT GCTGAAGATGACACTGTTTGCTTGGATCTTGGCAAGTGTAAGGATGGGAAATGCATCCCT TTCTGCGAGAGGGAACAGCAGCTGGAGTCCTGTGCATGTAATGAAACTGACAACTCCTGC AAGGTGTGCTGCAGGGACCTTTCTGGCCGCTGTGTGCCCTATGTCGATGCTGAACAAAAG AACTTATTTTTGAGGAAAGGAAAGCCCTGTACAGTAGGATTTTGTGACATGAATGGCAAA TGTGAGAAACGAGTACAGGATGTAATTGAACGATTTTGGGATTTCATTGACCAGCTGAGC ATCAATACTTTTGGAAAGTTTTTAGCAGACAACATCGTTGGGTCTGTCCTGGTTTTCTCC TTGATATTTTGGATTCCTTTCAGCATTCTTGTCCATTGTGTGGATAAGAAATTGGATAAA CAGTATGAATCTCTGTCTCTGTTTCACCCCAGTAACGTCGAAATGCTGAGCAGCATGGAT TCTGCATCGGTTCGCATTATCAAACCCTTTCCTGCGCCCCAGACTCCAGGCCGCCTGCAG CCTGCCCCTGTGATCCCTTCGGCGCCAGCAGCTCCAAAACTGGACCACCAGAGAATGGAC ACCATCCAGGAAGACCCCAGCACAGACTCACATATGGACGAGGATGGGTTTGAGAAGGAC CCCTTCCCAAATAGCAGCACAGCTGCCAAGTCATTTGAGGATCTCACGGACCATCCGGTC ACCAGAAGTGAAAAGGCTGCCTCCTTTAAACTGCAGCGTCAGAATCGTGTTGACAGCAAA GAAACAGAGTGCTAA PF01421 Reprolysin PF00200 Disintegrin component extracellular matrix component extracellular matrix (sensu Metazoa) function catalytic activity function peptidase activity function hydrolase activity function endopeptidase activity function ion binding function metallopeptidase activity function cation binding function metalloendopeptidase activity function transition metal ion binding function zinc ion binding function binding process cellular protein metabolism process metabolism process macromolecule metabolism process proteolysis process physiological process process protein metabolism "
drug:(2R)-N-HYDROXY-2-[(3S)-3-METHYL-3-{4-[(2-METHYLQUINOLIN-4-YL)METHOXY]PHENYL}-2-OXOPYRROLIDIN-1-YL]PROPANAMIDErdfs:label"(2R)-N-HYDROXY-2-[(3S)-3-METHYL-3-{4-[(2-METHYLQUINOLIN-4-YL)METHOXY]PHENYL}-2-OXOPYRROLIDIN-1-YL]PROPANAMIDE"
drug:(2R)-N-HYDROXY-2-[(3S)-3-METHYL-3-{4-[(2-METHYLQUINOLIN-4-YL)METHOXY]PHENYL}-2-OXOPYRROLIDIN-1-YL]PROPANAMIDErdf:typedrugbank:drugs
drug:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDEdrugbank:description" experimental This compound belongs to the alpha amino acid amides. These are amide derivatives of alpha amino acids. Alpha Amino Acid Amides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Pyrrolidinecarboxamides Boronic Acids Tertiary Carboxylic Acid Amides Tertiary Amines Polyamines Carboxylic Acids Dialkylamines Enolates Organoboron Compounds pyrrolidine-2-carboxamide pyrrolidine carboxylic acid or derivative boronic acid pyrrolidine tertiary carboxylic acid amide tertiary amine boronic acid derivative carboxamide group polyamine secondary amine secondary aliphatic amine enolate carboxylic acid amine organic metalloid moeity organonitrogen compound organoboron compound logP -0.52 ALOGPS logS -0.85 ALOGPS Water Solubility 3.02e+01 g/l ALOGPS logP -0.062 ChemAxon IUPAC Name [(2R)-1-{[(2S)-pyrrolidin-2-yl]carbonyl}pyrrolidin-2-yl]boronic acid ChemAxon Traditional IUPAC Name (2R)-1-{[(2S)-pyrrolidin-2-yl]carbonyl}pyrrolidin-2-ylboronic acid ChemAxon Molecular Weight 212.054 ChemAxon Monoisotopic Weight 212.133222886 ChemAxon SMILES [H][C@]1(CCCN1C(=O)[C@]1([H])CCCN1)B(O)O ChemAxon Molecular Formula C9H17BN2O3 ChemAxon InChI InChI=1S/C9H17BN2O3/c13-9(7-3-1-5-11-7)12-6-2-4-8(12)10(14)15/h7-8,11,14-15H,1-6H2/t7-,8-/m0/s1 ChemAxon InChIKey InChIKey=XSBZZZGVAIXJLD-YUMQZZPRSA-N ChemAxon Polar Surface Area (PSA) 72.8 ChemAxon Refractivity 50.91 ChemAxon Polarizability 22.55 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest basic) 9.82 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 10198228 PubChem Substance 99443953 ChemSpider 8373728 PDB BPR BE0000854 Dipeptidyl peptidase 4 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dipeptidyl peptidase 4 Amino acid transport and metabolism Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Plays a role in T-cell activation DPP4 2q24.3 Cell membrane; single-pass type II membrane protein. Processed form:Secreted protein. Note=Also exis 7-28 5.92 88279.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3009 GenAtlas DPP4 GeneCards DPP4 GenBank Gene Database U13735 GenBank Protein Database 535388 UniProtKB P27487 UniProt Accession DPP4_HUMAN ADABP Adenosine deaminase complexing protein 2 Dipeptidyl peptidase IV DPP IV EC 3.4.14.5 T-cell activation antigen CD26 TP103 >Dipeptidyl peptidase 4 MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSL RWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNY VKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNL PSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYL CDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPS EPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISN EYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKY PLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGT FEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWE YYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP >2301 bp ATGAAGACACCGTGGAAGGTTCTTCTGGGACTGCTGGGTGCTGCTGCGCTTGTCACCATC ATCACCGTGCCCGTGGTTCTGCTGAACAAAGGCACAGATGATGCTACAGCTGACAGTCGC AAAACTTACACTCTAACTGATTACTTAAAAAATACTTATAGACTGAAGTTATACTCCTTA AGATGGATTTCAGATCATGAATATCTCTACAAACAAGAAAATAATATCTTGGTATTCAAT GCTGAATATGGAAACAGCTCAGTTTTCTTGGAGAACAGTACATTTGATGAGTTTGGACAT TCTATCAATGATTATTCAATATCTCCTGATGGGCAGTTTATTCTCTTAGAATACAACTAC GTGAAGCAATGGAGGCATTCCTACACAGCTTCATATGACATTTATGATTTAAATAAAAGG CAGCTGATTACAGAAGAGAGGATTCCAAACAACACACAGTGGGTCACATGGTCACCAGTG GGTCATAAATTGGCATATGTTTGGAACAATGACATTTATGTTAAAATTGAACCAAATTTA CCAAGTTACAGAATCACATGGACGGGGAAAGAAGATATAATATATAATGGAATAACTGAC TGGGTTTATGAAGAGGAAGTCTTCAGTGCCTACTCTGCTCTGTGGTGGTCTCCAAACGGC ACTTTTTTAGCATATGCCCAATTTAACGACACAGAAGTCCCACTTATTGAATACTCCTTC TACTCTGATGAGTCACTGCAGTACCCAAAGACTGTACGGGTTCCATATCCAAAGGCAGGA GCTGTGAATCCAACTGTAAAGTTCTTTGTTGTAAATACAGACTCTCTCAGCTCAGTCACC AATGCAACTTCCATACAAATCACTGCTCCTGCTTCTATGTTGATAGGGGATCACTACTTG TGTGATGTGACATGGGCAACACAAGAAAGAATTTCTTTGCAGTGGCTCAGGAGGATTCAG AACTATTCGGTCATGGATATTTGTGACTATGATGAATCCAGTGGAAGATGGAACTGCTTA GTGGCACGGCAACACATTGAAATGAGTACTACTGGCTGGGTTGGAAGATTTAGGCCTTCA GAACCTCATTTTACCCTTGATGGTAATAGCTTCTACAAGATCATCAGCAATGAAGAAGGT TACAGACACATTTGCTATTTCCAAATAGATAAAAAAGACTGCACATTTATTACAAAAGGC ACCTGGGAAGTCATCGGGATAGAAGCTCTAACCAGTGATTATCTATACTACATTAGTAAT GAATATAAAGGAATGCCAGGAGGAAGGAATCTTTATAAAATCCAACTTAGTGACTATACA AAAGTGACATGCCTCAGTTGTGAGCTGAATCCGGAAAGGTGTCAGTACTATTCTGTGTCA TTCAGTAAAGAGGCGAAGTATTATCAGCTGAGATGTTCCGGTCCTGGTCTGCCCCTCTAT ACTCTACACAGCAGCGTGAATGATAAAGGGCTGAGAGTCCTGGAAGACAATTCAGCTTTG GATAAAATGCTGCAGAATGTCCAGATGCCCTCCAAAAAACTGGACTTCATTATTTTGAAT GAAACAAAATTTTGGTATCAGATGATCTTGCCTCCTCATTTTGATAAATCCAAGAAATAT CCTCTACTATTAGATGTGTATGCAGGCCCATGTAGTCAAAAAGCAGACACTGTCTTCAGA CTGAACTGGGCCACTTACCTTGCAAGCACAGAAAACATTATAGTAGCTAGCTTTGATGGC AGAGGAAGTGGTTACCAAGGAGATAAGATCATGCATGCAATCAACAGAAGACTGGGAACA TTTGAAGTTGAAGATCAAATTGAAGCAGCCAGACAATTTTCAAAAATGGGATTTGTGGAC AACAAACGAATTGCAATTTGGGGCTGGTCATATGGAGGGTACGTAACCTCAATGGTCCTG GGATCGGGAAGTGGCGTGTTCAAGTGTGGAATAGCCGTGGCGCCTGTATCCCGGTGGGAG TACTATGACTCAGTGTACACAGAACGTTACATGGGTCTCCCAACTCCAGAAGACAACCTT GACCATTACAGAAATTCAACAGTCATGAGCAGAGCTGAAAATTTTAAACAAGTTGAGTAC CTCCTTATTCATGGAACAGCAGATGATAACGTTCACTTTCAGCAGTCAGCTCAGATCTCC AAAGCCCTGGTCGATGTTGGAGTGGATTTCCAGGCAATGTGGTATACTGATGAAGACCAT GGAATAGCTAGCAGCACAGCACACCAACATATATATACCCACATGAGCCACTTCATAAAA CAATGTTTCTCTTTACCTTAG PF00930 DPPIV_N PF00326 Peptidase_S9 component cell component membrane function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function serine-type peptidase activity function hydrolase activity function dipeptidyl-peptidase IV activity function prolyl oligopeptidase activity process protein metabolism process cellular protein metabolism process physiological process process proteolysis process metabolism process macromolecule metabolism "
drug:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDErdfs:label"(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE"
drug:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDErdf:typedrugbank:drugs
drug:(2R)-N-hydroxy-3-naphthalen-2-yl-2-[(naphthalen-2-ylsulfonyl)amino]propanamidedrugbank:description" experimental This compound belongs to the alpha amino acid amides. These are amide derivatives of alpha amino acids. Alpha Amino Acid Amides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Amphetamines and Derivatives Benzenesulfonamides Naphthalenes Sulfonyls Sulfonamides Hydroxamic Acids Enolates Polyamines acene amphetamine or derivative naphthalene benzenesulfonamide benzene sulfonic acid derivative sulfonyl sulfonamide carboxamide group hydroxamic acid polyamine enolate amine organonitrogen compound logP 3.14 ALOGPS logS -6 ALOGPS Water Solubility 4.31e-04 g/l ALOGPS logP 3.67 ChemAxon IUPAC Name (2R)-N-hydroxy-3-(naphthalen-2-yl)-2-(naphthalene-2-sulfonamido)propanamide ChemAxon Traditional IUPAC Name (2R)-N-hydroxy-3-(naphthalen-2-yl)-2-(naphthalene-2-sulfonamido)propanamide ChemAxon Molecular Weight 420.481 ChemAxon Monoisotopic Weight 420.114377828 ChemAxon SMILES [H][C@](CC1=CC2=C(C=CC=C2)C=C1)(NS(=O)(=O)C1=CC2=C(C=CC=C2)C=C1)C(=O)NO ChemAxon Molecular Formula C23H20N2O4S ChemAxon InChI InChI=1S/C23H20N2O4S/c26-23(24-27)22(14-16-9-10-17-5-1-3-7-19(17)13-16)25-30(28,29)21-12-11-18-6-2-4-8-20(18)15-21/h1-13,15,22,25,27H,14H2,(H,24,26)/t22-/m1/s1 ChemAxon InChIKey InChIKey=MMOUXLMPQFMDRD-JOCHJYFZSA-N ChemAxon Polar Surface Area (PSA) 95.5 ChemAxon Refractivity 114.8 ChemAxon Polarizability 43.4 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 8.69 ChemAxon pKa (strongest basic) -5.5 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 9823454 PubChem Substance 99444332 ChemSpider 7999201 PDB GVR BE0004110 UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase Cell wall/membrane/envelope biogenesis Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell lpxC Cytoplasmic None 5.0 33434.8 Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) GeneCards lpxC GenBank Gene Database U19797 GenBank Protein Database 6715617 UniProtKB P47205 UniProt Accession LPXC_PSEAE Protein envA UDP-3-O-acyl-GlcNAc deacetylase >UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase MIKQRTLKNIIRATGVGLHSGEKVYLTLKPAPVDTGIVFCRTDLDPVVEIPARAENVGET TMSTTLVKGDVKVDTVEHLLSAMAGLGIDNAYVELSASEVPIMDGSAGPFVFLIQSAGLQ EQEAAKKFIRIKREVSVEEGDKRAVFVPFDGFKVSFEIDFDHPVFRGRTQQASVDFSSTS FVKEVSRARTFGFMRDIEYLRSQNLALGGSVENAIVVDENRVLNEDGLRYEDEFVKHKIL DAIGDLYLLGNSLIGEFRGFKSGHALNNQLLRTLIADKDAWEVVTFEDARTAPISYMRPA AAV >960 bp ATGAACCTTTGCCTCGATAGCCTGCTGAACGGCACCCAGGATCCCAAGGCGTTCGGCCGT GTCGCCGTGCTGTTCGGCGGCAAGAGCGCCGAGCGCGAGGTGTCGCTGAAGTCCGGCGCG ATGGTCCTGCAATCCCTGCTGGCCGCCGGGGTCGATGCCTTCGGCATCGATGTCGGCGAA GACCTGCTGCAACGCCTGGTCGAGGAGAAGATCGACCGTGCCTTCATCATTCTCCACGGT CGTGGCGGCGAGGATGGCAGCATGCAGGGCCTGCTCGAGTGCGCGGGCATTCCCTACACC GGCAGCGGCGTGCTGGCCTCGGCGCTGGCGATGGACAAGCTGCGGACCAAGCGGGTCTGG CTCAGCCTCGGCCTGCCGACCCCGGACTACGCGGTGCTGGCCAGCGAGGATGACTGCCGC GAAGCGGCGCAGCGACTGGGTTTCCCGCTGATCGTCAAGCCGGCTCACGAAGGCTCGAGC ATCGGCATGGCCAAGGTCGGCGGGCTCGACGAATTGATCGCGGCGTGGCGCGAAGCGGCC CGCTACGACTCGCAGGTGCTGGTCGAGCAGTGGATCAGCGGCCCGGAATTCACCGTGGCG ACCTTGCGCGGGCAGGTGCTGCCGGCGATCCGCCTGGGCACGCCGCACACCTTCTACGAC TACGACGCCAAGTACCTGGCCAGCGATACCCGCTACCAGGTGCCCTGCGGTCTCGACGAG GCCAAGGAACGCGAGCTGAAGGAACTCACCGCGCGCGCCTGCGACGCCCTGGGCATCCAG GGCTGGGGGCGGGCGGACGTGATGCAGGACGCCGAAGGGCGTTTCTGGCTGCTTGAAGTC AACACCGCACCGGGCATGACCGACCACAGCCTGGTGCCTATGGCCGCGCGGGCCGCCGGC CTGGATTTCCAGCAACTGGTGCTGGCGATCCTGGCCGATAGCCGCGAGGCGAGGGGATAA PF03331 LpxC function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides function UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity function catalytic activity process metabolism process primary metabolism process lipid metabolism process cellular lipid metabolism process lipid A metabolism process physiological process process lipid A biosynthesis "
drug:(2R)-N-hydroxy-3-naphthalen-2-yl-2-[(naphthalen-2-ylsulfonyl)amino]propanamiderdfs:label"(2R)-N-hydroxy-3-naphthalen-2-yl-2-[(naphthalen-2-ylsulfonyl)amino]propanamide"
drug:(2R)-N-hydroxy-3-naphthalen-2-yl-2-[(naphthalen-2-ylsulfonyl)amino]propanamiderdf:typedrugbank:drugs
drug:(2R)-N~4~-hydroxy-2-(3-hydroxybenzyl)-N~1~-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamidedrugbank:description" experimental This compound belongs to the phenylpropylamines. These are compounds containing a phenylpropylamine moiety, which consists of a phenyl group substituted at the third carbon by an propan-1-amine. Phenylpropylamines Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenylpropylamines Indanes Phenols and Derivatives Secondary Carboxylic Acid Amides Secondary Alcohols Hydroxamic Acids Polyamines Enols Enolates Carboxylic Acids phenol derivative secondary alcohol hydroxamic acid secondary carboxylic acid amide carboxamide group carboxylic acid derivative carboxylic acid polyamine enolate enol alcohol amine organonitrogen compound logP 0.7 ALOGPS logS -3.4 ALOGPS Water Solubility 1.62e-01 g/l ALOGPS logP 1.22 ChemAxon IUPAC Name (2R)-N-hydroxy-N'-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-2-[(3-hydroxyphenyl)methyl]butanediamide ChemAxon Traditional IUPAC Name (2R)-N-hydroxy-N'-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-2-[(3-hydroxyphenyl)methyl]butanediamide ChemAxon Molecular Weight 370.3991 ChemAxon Monoisotopic Weight 370.152871824 ChemAxon SMILES [H][C@](CC(=O)NO)(CC1=CC(O)=CC=C1)C(=O)N[C@@]1([H])C2=C(C[C@@]1([H])O)C=CC=C2 ChemAxon Molecular Formula C20H22N2O5 ChemAxon InChI InChI=1S/C20H22N2O5/c23-15-6-3-4-12(9-15)8-14(11-18(25)22-27)20(26)21-19-16-7-2-1-5-13(16)10-17(19)24/h1-7,9,14,17,19,23-24,27H,8,10-11H2,(H,21,26)(H,22,25)/t14-,17-,19+/m1/s1 ChemAxon InChIKey InChIKey=VXDKQRWTOJFQKH-BJZITVGISA-N ChemAxon Polar Surface Area (PSA) 118.89 ChemAxon Refractivity 98.65 ChemAxon Polarizability 38.08 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 8.79 ChemAxon pKa (strongest basic) -0.99 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 11143173 PubChem Substance 99443308 ChemSpider 9318285 PDB 099 BE0003730 A disintegrin and metalloproteinase with thrombospondin motifs 5 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown A disintegrin and metalloproteinase with thrombospondin motifs 5 Involved in integrin binding Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period ADAMTS5 21q21.3 Secreted, extracellular space, extracellular matrix (By similarity) None 9.01 101714.9 Human HUGO Gene Nomenclature Committee (HGNC) GNC:221 GeneCards ADAMTS5 GenBank Gene Database AF142099 GenBank Protein Database 5733438 UniProtKB Q9UNA0 UniProt Accession ATS5_HUMAN A disintegrin and metalloproteinase with thrombospondin motifs 11 ADAM-TS 11 ADAM-TS 5 ADAM-TS5 ADAMTS-11 ADAMTS-5 ADMP-2 Aggrecanase-2 >A disintegrin and metalloproteinase with thrombospondin motifs 5 MLLGWASLLLCAFRLPLAAVGPAATPAQDKAGQPPTAAAAAQPRRRQGEEVQERAEPPGH PHPLAQRRRSKGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDGSVGIAGFVPAGGGT SAPWRHRSHCFYRGTVDASPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEKGR VYGDGSARILHVYTREGFSFEALPPRASCETPASTPEAHEHAPAHSNPSGRAALASQLLD QSALSPAGGSGPQTWWRRRRRSISRARQVELLLVADASMARLYGRGLQHYLLTLASIANR LYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYD AAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSH DDSKFCEETFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQI LGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGT PCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPR NNGRYCTGKRAIYRSCSLMPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVL PADVCKLTCRAKGTGYYVVFSPKVTDGTECRPYSNSVCVRGKCVRTGCDGIIGSKLQYDK CGVCGGDNSSCTKIVGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKK NGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPT KPLDVRYSFFVPKKSTPKVNSVTSHGSNKVGSHTSQPQWVTGPWLACSRTCDTGWHTRTV QCQDGNRKLAKGCPLSQRPSAFKQCLLKKC >2793 bp ATGCTGCTCGGGTGGGCGTCCCTGCTGCTGTGCGCGTTCCGCCTGCCCCTGGCCGCGGTC GGCCCCGCCGCGACACCTGCCCAGGATAAAGCCGGGCAGCCTCCGACTGCTGCAGCAGCC GCCCAGCCCCGCCGGCGGCAGGGGGAGGAGGTGCAGGAGCGAGCCGAGCCTCCCGGCCAC CCGCACCCCCTGGCGCAGCGGCGCAGGAGCAAGGGGCTGGTGCAGAACATCGACCAACTC TACTCCGGCGGCGGCAAGGTGGGCTACCTCGTCTACGCGGGCGGCCGGAGGTTCCTCTTG GACCTGGAGCGAGATGGTTCGGTGGGCATTGCTGGCTTCGTGCCCGCAGGAGGCGGGACG AGTGCGCCCTGGCGCCACCGGAGCCACTGCTTCTATCGGGGCACAGTGGACGCTAGTCCC CGCTCTCTGGCTGTCTTTGACCTCTGTGGGGGTCTCGACGGCTTCTTCGCGGTCAAGCAC GCGCGCTACACCCTAAAGCCACTGCTGCGCGGACCCTGGGCGGAGGAAGAAAAGGGGCGC GTGTACGGGGATGGGTCCGCACGGATCCTGCACGTCTACACCCGCGAGGGCTTCAGCTTC GAGGCCCTGCCGCCGCGCGCCAGCTGCGAAACCCCCGCGTCCACACCGGAGGCCCACGAG CATGCTCCGGCGCACAGCAACCCGAGCGGACGCGCAGCACTGGCCTCGCAGCTCTTGGAC CAGTCCGCTCTCTCGCCCGCTGGGGGCTCAGGACCGCAGACGTGGTGGCGGCGGCGGCGC CGCTCCATCTCCCGGGCCCGCCAGGTGGAGCTGCTTCTGGTGGCTGACGCGTCCATGGCG CGGTTGTATGGCCGGGGCCTGCAGCATTACCTGCTGACCCTGGCCTCCATCGCCAATAGG CTGTACAGCCATGCTAGCATCGAGAACCACATCCGCCTGGCCGTGGTGAAGGTGGTGGTG CTAGGCGACAAGGACAAGAGCCTGGAAGTGAGCAAGAACGCTGCCACCACACTCAAGAAC TTTTGCAAGTGGCAGCACCAACACAACCAGCTGGGAGATGACCATGAGGAGCACTACGAT GCAGCTATCCTGTTTACTCGGGAGGATTTATGTGGGCATCATTCATGTGACACCCTGGGA ATGGCAGACGTTGGGACCATATGTTCTCCAGAGCGCAGCTGTGCTGTGATTGAAGACGAT GGCCTCCACGCAGCCTTCACTGTGGCTCACGAAATCGGACATTTACTTGGCCTCTCCCAT GACGATTCCAAATTCTGTGAAGAGACCTTTGGTTCCACAGAAGATAAGCGCTTAATGTCT TCCATCCTTACCAGCATTGATGCATCTAAGCCCTGGTCCAAATGCACTTCAGCCACCATC ACAGAATTCCTGGATGATGGCCATGGTAACTGTTTGCTGGACCTACCACGAAAGCAGATC CTGGGCCCCGAAGAACTCCCAGGACAGACCTACGATGCCACCCAGCAGTGCAACCTGACA TTCGGGCCTGAGTACTCCGTGTGTCCCGGCATGGATGTCTGTGCTCGCCTGTGGTGTGCT GTGGTACGCCAGGGCCAGATGGTCTGTCTGACCAAGAAGCTGCCTGCGGTGGAAGGGACG CCTTGTGGAAAGGGGAGAATCTGCCTGCAGGGCAAATGTGTGGACAAAACCAAGAAAAAA TATTATTCAACGTCAAGCCATGGCAACTGGGGATCTTGGGGATCCTGGGGCCAGTGTTCT CGCTCATGTGGAGGAGGAGTGCAGTTTGCCTATCGTCACTGTAATAACCCTGCTCCCAGA AACAACGGACGCTACTGCACAGGGAAGAGGGCCATCTACCGCTCCTGCAGTCTCATGCCC TGCCCACCCAATGGTAAATCATTTCGTCATGAACAGTGTGAGGCCAAAAATGGCTATCAG TCTGATGCAAAAGGAGTCAAAACTTTTGTGGAATGGGTTCCCAAATATGCAGGTGTCCTG CCAGCGGATGTGTGCAAGCTGACCTGCAGAGCCAAGGGCACTGGCTACTATGTGGTATTT TCTCCAAAGGTGACCGATGGCACTGAATGTAGGCCGTACAGTAATTCCGTCTGCGTCCGG GGGAAGTGTGTGAGAACTGGCTGTGACGGCATCATTGGCTCAAAGCTGCAGTATGACAAG TGCGGAGTATGTGGAGGAGACAACTCCAGCTGTACAAAGATTGTTGGAACCTTTAATAAG AAAAGTAAGGGTTACACTGACGTGGTGAGGATTCCTGAAGGGGCAACCCACATAAAAGTT CGACAGTTCAAAGCCAAAGACCAGACTAGATTCACTGCCTATTTAGCCCTGAAAAAGAAA AACGGTGAGTACCTTATCAATGGAAAGTACATGATCTCCACTTCAGAGACTATCATTGAC ATCAATGGAACAGTCATGAACTATAGCGGTTGGAGCCACAGGGATGACTTCCTGCATGGC ATGGGCTACTCTGCCACGAAGGAAATTCTAATAGTGCAGATTCTTGCAACAGACCCCACT AAACCATTAGATGTCCGTTATAGCTTTTTTGTTCCCAAGAAGTCCACTCCAAAAGTAAAC TCTGTCACTAGTCATGGCAGCAATAAAGTGGGATCACACACTTCGCAGCCGCAGTGGGTC ACGGGCCCATGGCTCGCCTGCTCTAGGACCTGTGACACAGGTTGGCACACCAGAACGGTG CAGTGCCAGGATGGAAACCGGAAGTTAGCAAAAGGATGTCCTCTCTCCCAAAGGCCTTCT GCGTTTAAGCAATGCTTGTTGAAGAAATGTTAG PF00090 TSP_1 PF01562 Pep_M12B_propep PF01421 Reprolysin PF05986 ADAM_spacer1 component extracellular matrix function cation binding function transition metal ion binding function zinc ion binding function binding function catalytic activity function peptidase activity function endopeptidase activity function hydrolase activity function metallopeptidase activity function ion binding function metalloendopeptidase activity process protein metabolism process physiological process process cellular protein metabolism process metabolism process proteolysis process macromolecule metabolism "
drug:(2R)-N~4~-hydroxy-2-(3-hydroxybenzyl)-N~1~-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamiderdfs:label"(2R)-N~4~-hydroxy-2-(3-hydroxybenzyl)-N~1~-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide"
drug:(2R)-N~4~-hydroxy-2-(3-hydroxybenzyl)-N~1~-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamiderdf:typedrugbank:drugs
drug:(2R,3R)-3-{[3,5-BIS(TRIFLUOROMETHYL)PHENYL]AMINO}-2-CYANO-3-THIOXOPROPANAMIDEdrugbank:description" experimental This compound belongs to the beta amino acids and derivatives. These are amino acids having a (-NH2) group attached to the beta carbon atom. Beta Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Benzene and Substituted Derivatives Primary Carboxylic Acid Amides Hemiaminals Secondary Amines Nitriles Alkylthiols Enolates Polyamines Carboxylic Acids Organofluorides Alkyl Fluorides benzene hemiaminal primary carboxylic acid amide carboxamide group alkylthiol carboxylic acid secondary amine polyamine enolate nitrile carbonitrile organofluoride organohalogen amine organonitrogen compound alkyl halide alkyl fluoride logP 3.57 ALOGPS logS -4.1 ALOGPS Water Solubility 3.04e-02 g/l ALOGPS logP 2.51 ChemAxon IUPAC Name (2S)-2-[(R)-{[3,5-bis(trifluoromethyl)phenyl]amino}(sulfanyl)methyl]-2-cyanoacetamide ChemAxon Traditional IUPAC Name (2S)-2-[(R)-{[3,5-bis(trifluoromethyl)phenyl]amino}(sulfanyl)methyl]-2-cyanoacetamide ChemAxon Molecular Weight 357.275 ChemAxon Monoisotopic Weight 357.037051845 ChemAxon SMILES [H][C@](S)(NC1=CC(=CC(=C1)C(F)(F)F)C(F)(F)F)[C@@]([H])(C#N)C(N)=O ChemAxon Molecular Formula C12H9F6N3OS ChemAxon InChI InChI=1S/C12H9F6N3OS/c13-11(14,15)5-1-6(12(16,17)18)3-7(2-5)21-10(23)8(4-19)9(20)22/h1-3,8,10,21,23H,(H2,20,22)/t8-,10+/m0/s1 ChemAxon InChIKey InChIKey=ZTUMRSFHUOBXAC-WCBMZHEXSA-N ChemAxon Polar Surface Area (PSA) 78.91 ChemAxon Refractivity 73.33 ChemAxon Polarizability 27.01 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 6.87 ChemAxon pKa (strongest basic) 1.58 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937036 PubChem Substance 99443384 PDB 221 BE0003752 Genome polyprotein Hepatitis C virus subtype 1b # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Genome polyprotein Involved in ATP binding Cytoplasmic None 8.14 327008.3 Hepatitis C virus subtype 1b GenBank Gene Database AF333324 GenBank Protein Database 12831193 UniProtKB Q99AU2 UniProt Accession Q99AU2_9HEPC >Genome polyprotein MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRG RRQPIPKARRPEGRTWAQPGYPWPLYGNEGMGWAGWLLSPRGSRPSWGPTDPRRRSRNLG KVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLA LLSCLTIPASAYEVRNVSGIYHVTNDCSNSSIVYEAADMIMHTPGCVPCVRESNFSRCWV ALTPTLAARNSSIPTTTIRRHVDLLVGAAALCSAMYVGDLCGSVFLVSQLFTFSPRRYET VQDCNCSIYPGHVSGHRMAWDMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLA YYSMVGNWAKVLIVMLLFAGVDGHTHVTGGRVASSTQSLVSWLSQGPSQKIQLVNTNGSW HINRTALNCNDSLQTGFIAALFYAHRFNASGCPERMASCRPIDKFAQGWGPITHVVPNIS DQRPYCWHYAPQPCGIVPASQVCGPVYCFTPSPVVVGTTDRSGVPTYSWGENETDVLLLN NTRPPQGNWFGCTWMNSTGFTKTCGGPPCNIGGVGNNTLICPTDCFRKHPEATYTKCGSG PWLTPRCLVDYPYRLWHYPCTINFTIFKVRMYVGGVEHRLNAACNWTRGERCDLEDRDRS ELSPLLLSTTEWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSVVVSVVIKWEYVL LLFLLLADARVCACLWMMLLIAQAEATLENLVVLNAASVAGAHGLLSFLVFFCAAWYIKG RLVPGAAYALYGVWPLLLLLLALPPRAYAMDREMAASCGGAVFVGLVLLTLSPYYKVFLA RLIWWLQYFITRAEAHLQVWVPPLNVRGGRDAIILLTCAVHPELIFDITKLLLAILGPLM VLQAGITRVPYFVRAQGLIHACMLVRKVAGGHYVQMAFMKLGALTGTYIYNHLTPLRDWA HAGLRDLAVAVEPVVFSDMETKIITWGADTAACGDIILGLPVSARRGKEILLGPADSLEG RGWRLLAPITAYSQQTRGLLGCIITSLTGRDKNQVEGEVQVVSTATQSFLATCVNGVCWT VYHGAGSKTLAGPKGPITQMYTNVDQDLVGWQAPPGARSLTPCTCGSSDLYLVTRHADVI PVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHAVGIFRAAVCTRGVAKAVDFVPVES METTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAA TLGFGAYMSKAHGIDPNIRTGVRTITTGAPVTYSTYGKFLADGGCSGGAYDIIICDECHS TDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSNTGEIPFYGKAI PIEAIRGGRHLIFCHSKKKCDELAAKLSGLGINAVAYYRGLDVSVIPTIGDVVVVATDAL MTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRRGIYR FVTPGERPSGMFDSSVLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWES VFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHG PTPLLYRLGAVQNEVTLTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSV VIVGRIILSGRPAIVPDRELLYQEFDEMEECATHLPYIEQGMQLAEQFKQKALGLLQTAT KQAEAAAPVVESKWRALETFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSP LTTQSTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVGSIGLGKVLVDILAGYGAGVA GALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLI AFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLRDV WDWICTVLTDFKTWLQSKLLPQLPGVPFFSCQRGYKGVWRGDGIMQTTCPCGAQITGHVK NGSMRIVGPKTCSNTWHGTFPINAYTTGPCTPSPAPNYSRALWRVAAEEYVEVTRVGDFH YVTGMTTDNVKCPCQVPAPEFFSEVDGVRLHRYAPACRPLLREEVTFQVGLNQYLVGSQL PCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHV SPDADLIEANLLWRQEMGGNITRVESENKVVVLDSFDPLRAEEDEREVSVPAEILRKSKK FPAAMPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPPIKAPPIPPPRRKRTVVLTESSV SSALAELATKTFGSSESSAVDSGTATALPDQASDDGDKGSDVESYSSMPPLEGEPGDPDL SDGSWSTVSEEASEDVVCCSMSYTWTGALITPCAAEESKLPINALSNSLLRHHNMVYATT SRSAGLRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKAKLLSVEEACKLTPPHSAKSKF GYGAKDVRNLSSKAVNHIHSVWKDLLEDTVTPIDTTIMAKNEVFCVQPEKGGRKPARLIV FPDLGVRVCEKMALYDVVSTLPQVVMGSSYGFQYSPGQRVEFLVNTWKSKKNPMGFSYDT RCFDSTVTENDIRVEESIYQCCDLAPEARQAIKSLTERLYIGGPLTNSKGQNCGYRRCRA SGVLTTSCGNTLTCYLKASAACRAAKLQDCTMLVNGDDLVVICESAGTQEDAASLRVFTE AMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETAR HTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQ IIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRARLLSQGGRAATC GKYLFNWAVKTKLKLTPIPAASQLDLSGWFVAGYSGGDIYHSLSRARPRWFMLCLLLLSV GVGIYLLPNR >9033 bp ATGAGCACAAATCCTAAACCTCAAAGAAAAACCAAACGTAACACCAACCGCCGCCCACAG GACGTTAAGTTCCCGGGCGGTGGTCAGATCGTTGGTGGAGTTTACCTGTTGCCGCGCAGG GGCCCCAGGTTGGGTGTGCGCGCGACTAGGAAGACTTCCGAGCGGTCGCAACCTCGTGGA AGGCGACAACCTATCCCCAAGGCTCGCCGGCCCGAGGGTAGGACCTGGGCTCAGCCCGGG TACCCTTGGCCCCTCTATGGCAACGAGGGTATGGGGTGGGCAGGATGGCTCCTGTCACCC CGTGGCTCTCGGCCTAGTTGGGGCCCCACAGACCCCCGGCGTAGGTCGCGTAATTTGGGT AAGGTCATCGATACCCTTACATGCGGCTTCGCCGACCTCATGGGGTACATTCCGCTTGTC GGCGCCCCCCTAGGAGGCGCTGCCAGGGCCCTGGCGCATGGCGTCCGGGTTCTGGAGGAC GGCGTGAACTATGCAACAGGGAATCTGCCCGGTTGCTCTTTCTCTATCTTCCTCTTAGCT TTGCTGTCTTGTTTGACCATCCCAGCTTCCGCTTACGAGGTGCGCAACGTGTCCGGGATA TACCATGTCACGAACGACTGCTCCAACTCAAGTATTGTGTATGAGGCAGCGGACATGATC ATGCACACCCCCGGGTGCGTGCCCTGCGTCCGGGAGAGTAATTTCTCCCGTTGCTGGGTA GCGCTCACTCCCACGCTCGCGGCCAGGAACAGCAGCATCCCCACCACGACAATACGACGC CACGTCGATTTGCTCGTTGGGGCGGCTGCTCTCTGTTCCGCTATGTACGTTGGGGATCTC TGCGGATCCGTTTTTCTCGTCTCCCAGCTGTTCACCTTCTCACCTCGCCGGTATGAGACG GTACAAGATTGCAATTGCTCAATCTATCCCGGCCACGTATCAGGTCACCGCATGGCTTGG GATATGATGATGAACTGGTCACCTACAACGGCCCTAGTGGTATCGCAGCTACTCCGGATC CCACAAGCCGTCGTGGACATGGTGGCGGGGGCCCACTGGGGTGTCCTAGCGGGCCTTGCC TACTATTCCATGGTGGGGAACTGGGCTAAGGTCTTGATTGTGATGCTACTCTTTGCTGGC GTTGACGGGCACACCCACGTGACAGGGGGAAGGGTAGCCTCCAGCACCCAGAGCCTCGTG TCCTGGCTCTCACAAGGGCCATCTCAGAAAATCCAACTCGTGAACACCAACGGCAGCTGG CACATCAACAGGACCGCTCTGAATTGCAATGACTCCCTCCAAACTGGGTTCATTGCTGCG CTGTTCTACGCACACAGGTTCAACGCGTCCGGATGTCCAGAGCGCATGGCCAGCTGCCGC CCCATCGACAAGTTCGCTCAGGGGTGGGGTCCCATCACTCACGTTGTGCCTAACATCTCG GACCAGAGGCCTTATTGCTGGCACTATGCACCCCAACCGTGCGGTATTGTACCCGCGTCG CAGGTGTGTGGCCCAGTGTATTGCTTCACCCCGAGTCCTGTTGTGGTGGGGACGACCGAC CGTTCCGGAGTCCCCACGTATAGCTGGGGGGAGAATGAGACAGACGTGCTGCTACTCAAC AACACGCGGCCGCCGCAAGGCAACTGGTTCGGCTGTACATGGATGAATAGCACCGGGTTC ACCAAGACGTGCGGGGGCCCCCCGTGTAACATCGGGGGGGTTGGCAACAACACCTTGATT TGCCCCACGGATTGCTTCCGAAAGCACCCCGAGGCCACTTACACCAAATGCGGCTCGGGT CCTTGGTTGACACCTAGGTGTCTAGTTGACTACCCATACAGACTTTGGCACTACCCCTGC ACTATCAATTTTACCATCTTCAAGGTCAGGATGTACGTGGGGGGCGTGGAGCACAGGCTC AACGCCGCGTGCAATTGGACCCGAGGAGAGCGCTGTGACCTGGAGGACAGGGATAGATCA GAGCTTAGCCCGCTGCTATTGTCTACAACGGAGTGGCAGGTACTGCCCTGTTCCTTTACC ACCCTACCGGCTCTGTCCACTGGATTGATCCACCTCCATCAGAATATCGTGGACGTGCAA TACCTGTACGGTGTAGGGTCAGTGGTTGTCTCCGTCGTAATCAAATGGGAGTATGTTCTG CTGCTCTTCCTTCTCCTGGCGGACGCGCGCGTCTGTGCCTGCTTGTGGATGATGCTGCTG ATAGCCCAGGCTGAGGCCACCTTAGAGAACCTGGTGGTCCTCAATGCGGCGTCTGTGGCC GGAGCGCATGGCCTTCTCTCCTTCCTCGTGTTCTTCTGCGCCGCCTGGTACATCAAAGGC AGGCTGGTCCCTGGGGCGGCATATGCTCTCTATGGCGTATGGCCGTTGCTCCTGCTCTTG CTGGCTTTACCACCACGAGCTTATGCCATGGACCGAGAGATGGCTGCATCGTGCGGAGGC GCGGTTTTTGTAGGTCTGGTACTCTTGACCTTGTCACCATACTATAAGGTGTTCCTCGCT AGGCTCATATGGTGGTTACAATATTTTATCACCAGGGCCGAGGCGCACTTGCAAGTGTGG GTCCCCCCTCTTAATGTTCGGGGAGGCCGCGATGCCATCATCCTCCTTACATGCGCGGTC CATCCAGAGCTAATCTTTGACATCACCAAACTCCTGCTCGCCATACTCGGTCCGCTCATG GTGCTCCAAGCTGGCATAACCAGAGTGCCGTACTTCGTGCGCGCTCAAGGGCTCATTCAT GCATGCATGTTAGTGCGGAAGGTCGCTGGGGGTCATTATGTCCAAATGGCCTTCATGAAG CTGGGCGCGCTGACAGGCACGTACATTTACAACCATCTTACCCCGCTACGGGATTGGGCC CACGCGGGCCTACGAGACCTTGCGGTGGCAGTGGAGCCCGTCGTCTTCTCCGACATGGAG ACCAAGATCATCACCTGGGGAGCAGACACCGCGGCGTGTGGGGACATCATCTTGGGTCTG CCCGTCTCCGCCCGAAGGGGAAAGGAGATACTCCTGGGCCCGGCCGATAGTCTTGAAGGG CGGGGGTGGCGACTCCTCGCGCCCATCACGGCCTACTCCCAACAGACGCGGGGCCTACTT GGTTGCATCATCACTAGCCTTACAGGCCGGGACAAGAACCAGGTCGAGGGAGAGGTTCAG GTGGTTTCCACCGCAACACAATCCTTCCTGGCGACCTGCGTCAACGGCGTGTGTTGGACC GTTTACCATGGTGCTGGCTCAAAGACCTTAGCCGGCCCAAAGGGGCCAATCACCCAGATG TACACTAATGTGGACCAGGACCTCGTCGGCTGGCAGGCGCCCCCCGGGGCGCGTTCCTTG ACACCATGCACCTGTGGCAGCTCAGACCTTTACTTGGTCACGAGACATGCTGACGTCATT CCGGTGCGCCGGCGGGGCGACAGTAGGGGGAGCCTGCTCTCCCCCAGGCCTGTCTCCTAC TTGAAGGGCTCTTCGGGTGGTCCACTGCTCTGCCCTTCGGGGCACGCTGTGGGCATCTTC CGGGCTGCCGTATGCACCCGGGGGGTTGCGAAGGCGGTGGACTTTGTGCCCGTAGAGTCC ATGGAAACTACTATGCGGTCTCCGGTCTTCACGGACAACTCATCCCCCCCGGCCGTACCG CAGTCATTTCAAGTGGCCCACCTACACGCTCCCACTGGCAGCGGCAAGAGTACTAAAGTG CCGGCTGCATATGCAGCCCAAGGGTACAAGGTGCTCGTCCTCAATCCGTCCGTTGCCGCT ACCTTAGGGTTTGGGGCGTATATGTCTAAGGCACACGGTATTGACCCCAACATCAGAACT GGGGTAAGGACCATTACCACAGGCGCCCCCGTCACATACTCTACCTATGGCAAGTTTCTT GCCGATGGTGGTTGCTCTGGGGGCGCTTATGACATCATAATATGTGATGAGTGCCATTCA ACTGACTCGACTACAATCTTGGGCATCGGCACAGTCCTGGACCAAGCGGAGACGGCTGGA GCGCGGCTTGTCGTGCTCGCCACCGCTACGCCTCCGGGATCGGTCACCGTGCCACACCCA AACATCGAGGAGGTGGCCCTGTCTAATACTGGAGAGATCCCCTTCTATGGCAAAGCCATC CCCATTGAAGCCATCAGGGGGGGAAGGCATCTCATTTTCTGTCATTCCAAGAAGAAGTGC GACGAGCTCGCCGCAAAGCTGTCAGGCCTCGGAATCAACGCTGTGGCGTATTACCGGGGG CTCGATGTGTCCGTCATACCAACTATCGGAGACGTCGTTGTCGTGGCAACAGACGCTCTG ATGACGGGCTATACGGGCGACTTTGACTCAGTGATCGACTGTAACACATGTGTCACCCAG ACAGTCGACTTCAGCTTGGATCCCACCTTCACCATTGAGACGACGACCGTGCCTCAAGAC GCAGTGTCGCGCTCGCAGCGGCGGGGTAGGACTGGCAGGGGTAGGAGAGGCATCTACAGG TTTGTGACTCCGGGAGAACGGCCCTCGGGCATGTTCGATTCCTCGGTCCTGTGTGAGTGC TATGACGCGGGCTGTGCTTGGTACGAGCTCACCCCCGCCGAGACCTCGGTTAGGTTGCGG GCCTACCTGAACACACCAGGGTTGCCCGTTTGCCAGGACCACCTGGAGTTCTGGGAGAGT GTCTTCACAGGCCTCACCCACATAGATGCACACTTCTTGTCCCAGACCAAGCAGGCAGGA GACAACTTCCCCTACCTGGTAGCATACCAAGCCACGGTGTGCGCCAGGGCTCAGGCCCCA CCTCCATCATGGGATCAAATGTGGAAGTGTCTCATACGGCTGAAACCTACGCTGCACGGG CCAACACCCTTGCTGTACAGGCTGGGAGCCGTCCAAAATGAGGTCACCCTCACCCACCCC ATAACCAAATACATCATGGCATGCATGTCGGCTGACCTGGAGGTCGTCACTAGCACCTGG GTGCTGGTGGGCGGAGTCCTTGCAGCTCTGGCCGCGTATTGCCTGACAACAGGCAGTGTG GTCATTGTGGGTAGGATTATCTTGTCCGGGAGGCCGGCTATTGTTCCCGACAGGGAGCTT CTCTACCAGGAGTTCGATGAAATGGAAGAGTGCGCCACGCACCTCCCTTACATTGAGCAG GGAATGCAGCTCGCCGAGCAGTTCAAGCAGAAAGCGCTCGGGTTACTGCAAACAGCCACC AAACAAGCGGAGGCTGCTGCTCCCGTGGTGGAGTCCAAGTGGCGAGCCCTTGAGACATTC TGGGCGAAGCACATGTGGAATTTCATCAGCGGGATACAGTACTTAGCAGGCTTATCCACT CTGCCTGGGAACCCCGCAATAGCATCATTGATGGCATTCACAGCCTCTATCACCAGCCCG CTCACCACCCAAAGTACCCTCCTGTTTAACATCTTGGGGGGGTGGGTGGCTGCCCAACTC GCCCCCCCCAGCGCCGCTTCGGCTTTCGTGGGCGCCGGCATCGCCGGTGCGGCTGTTGGC AGCATAGGCCTTGGGAAGGTGCTTGTGGACATTCTGGCGGGTTATGGAGCAGGAGTGGCC GGCGCGCTCGTGGCCTTTAAGGTCATGAGCGGCGAGATGCCCTCTACCGAGGACCTGGTC AATCTACTTCCTGCCATCCTCTCTCCTGGCGCCCTGGTCGTCGGGGTCGTGTGTGCAGCA ATACTGCGTCGGCACGTGGGTCCGGGAGAGGGGGCTGTGCAGTGGATGAACCGGCTGATA GCGTTCGCCTCGCGGGGTAATCACGTTTCCCCCACGCACTATGTGCCTGAGAGCGACGCC GCAGCGCGTGTTACTCAGATCCTCTCCAGCCTTACCATCACTCAGCTGCTGAAAAGGCTC CACCAGTGGATTAATGAGGACTGCTCCACACCGTGTTCCGGCTCGTGGCTAAGGGATGTT TGGGACTGGATATGCACGGTGTTGACTGACTTCAAGACCTGGCTCCAGTCCAAGCTCCTG CCGCAGCTACCGGGAGTCCCTTTTTTCTCGTGCCAACGCGGGTACAAGGGAGTCTGGCGG GGAGACGGCATCATGCAAACCACCTGCCCATGTGGAGCACAGATCACCGGACATGTCAAA AACGGTTCCATGAGGATCGTCGGGCCTAAGACCTGCAGCAACACGTGGCATGGAACATTC CCCATCAACGCATACACCACGGGCCCCTGCACACCCTCTCCAGCGCCAAACTATTCTAGG GCGCTGTGGCGGGTGGCCGCTGAGGAGTACGTGGAGGTCACGCGGGTGGGGGATTTCCAC TACGTGACGGGCATGACCACTGACAACGTAAAGTGCCCATGCCAGGTTCCGGCTCCTGAA TTCTTCTCGGAGGTGGACGGAGTGCGGTTGCACAGGTACGCTCCGGCGTGCAGGCCTCTC CTACGGGAGGAGGTTACATTCCAGGTCGGGCTCAACCAATACCTGGTTGGGTCACAGCTA CCATGCGAGCCCGAACCGGATGTAGCAGTGCTCACTTCCATGCTCACCGACCCCTCCCAC ATCACAGCAGAAACGGCTAAGCGTAGGTTGGCCAGGGGGTCTCCCCCCTCCTTGGCCAGC TCTTCAGCTAGCCAGTTGTCTGCGCCTTCCTTGAAGGCGACATGCACTACCCACCATGTC TCTCCGGACGCTGACCTCATCGAGGCCAACCTCCTGTGGCGGCAGGAGATGGGCGGGAAC ATCACCCGCGTGGAGTCGGAGAACAAGGTGGTAGTCCTGGACTCTTTCGACCCGCTTCGA GCGGAGGAGGATGAGAGGGAAGTATCCGTTCCGGCGGAGATCCTGCGGAAATCCAAGAAG TTCCCCGCAGCGATGCCCATCTGGGCGCGCCCGGATTACAACCCTCCACTGTTAGAGTCC TGGAAGGACCCGGACTACGTCCCTCCGGTGGTGCACGGGTGCCCGTTGCCACCTATCAAG GCCCCTCCAATACCACCTCCACGGAGAAAGAGGACGGTTGTCCTAACAGAGTCCTCCGTG TCTTCTGCCTTAGCGGAGCTCGCTACTAAGACCTTCGGCAGCTCCGAATCATCGGCCGTC GACAGCGGCACGGCGACCGCCCTTCCTGACCAGGCCTCCGACGACGGTGACAAAGGATCC GACGTTGAGTCGTACTCCTCCATGCCCCCCCTTGAGGGGGAACCGGGGGACCCCGATCTC AGTGACGGGTCTTGGTCTACCGTGAGCGAGGAAGCTAGTGAGGATGTCGTCTGCTGCTCA ATGTCCTACACATGGACAGGCGCCTTGATCACGCCATGCGCTGCGGAGGAAAGCAAGCTG CCCATCAACGCGTTGAGCAACTCTTTGCTGCGCCACCATAACATGGTTTATGCCACAACA TCTCGCAGCGCAGGCCTGCGGCAGAAGAAGGTCACCTTTGACAGACTGCAAGTCCTGGAC GACCACTACCGGGACGTGCTCAAGGAGATGAAGGCGAAGGCGTCCACAGTTAAGGCTAAA CTCCTATCCGTAGAGGAAGCCTGCAAGCTGACGCCCCCACATTCGGCCAAATCCAAGTTT GGCTATGGGGCAAAGGACGTCCGGAACCTATCCAGCAAGGCCGTTAACCACATCCACTCC GTGTGGAAGGACTTGCTGGAAGACACTGTGACACCAATTGACACCACCATCATGGCAAAA AATGAGGTTTTCTGTGTCCAACCAGAGAAAGGAGGCCGTAAGCCAGCCCGCCTTATCGTA TTCCCAGATCTGGGAGTCCGTGTATGCGAGAAGATGGCCCTCTATGATGTGGTCTCCACC CTTCCTCAGGTCGTGATGGGCTCCTCATACGGATTCCAGTACTCTCCTGGGCAGCGAGTC GAGTTCCTGGTGAATACCTGGAAATCAAAGAAAAACCCCATGGGCTTTTCATATGACACT CGCTGTTTCGACTCAACGGTCACCGAGAACGACATCCGTGTTGAGGAGTCAATTTACCAA TGTTGTGACTTGGCCCCCGAAGCCAGACAGGCCATAAAATCGCTCACAGAGCGGCTTTAT ATCGGGGGTCCTCTGACTAATTCAAAAGGGCAGAACTGCGGTTATCGCCGGTGCCGCGCG AGCGGCGTGCTGACGACTAGCTGCGGTAACACCCTCACATGTTACTTGAAGGCCTCTGCA GCCTGTCGAGCTGCGAAGCTCCAGGACTGCACGATGCTCGTGAACGGAGACGACCTTGTC GTTATCTGTGAAAGCGCGGGAACCCAAGAGGACGCGGCGAGCCTACGAGTCTTCACGGAG GCTATGACTAGGTACTCTGCCCCCCCCGGGGACCCGCCCCAACCAGAATACGACTTGGAG CTGATAACATCATGTTCCTCCAATGTGTCGGTCGCCCACGATGCATCAGGCAAAAGGGTG TACTACCTCACCCGTGATCCCACCACCCCCCTCGCACGGGCTGCGTGGGAAACAGCTAGA CACACTCCAGTTAACTCCTGGCTAGGCAACATTATCATGTATGCGCCCACTTTGTGGGCA AGGATGATTCTGATGACTCACTTCTTCTCCATCCTTCTAGCACAGGAGCAACTTGAAAAA GCCCTGGACTGCCAGATCTACGGGGCCTGTTACTCCATTGAGCCACTTGACCTACCTCAG ATCATTGAACGACTCCATGGCCTTAGCGCATTTTCACTCCATAGTTACTCTCCAGGTGAG ATCAATAGGGTGGCTTCATGCCTCAGGAAACTTGGGGTACCACCCTTGCGAGTCTGGAGA CATCGGGCCAGGAGCGTCCGCGCTAGGCTACTGTCCCAGGGGGGGAGGGCCGCCACTTGT GGCAAGTACCTCTTCAACTGGGCAGTGAAGACCAAACTCAAACTCACTCCAATCCCGGCT GCGTCCCAGCTGGACTTGTCCGGCTGGTTCGTTGCTGGTTACAGCGGGGGAGACATATAT CACAGCCTGTCTCGTGCCCGACCCCGCTGGTTCATGCTGTGCCTACTCCTACTTTCTGTA GGGGTAGGCATCTACCTGCTCCCCAACCGATGA PF01543 HCV_capsid PF01542 HCV_core PF01539 HCV_env PF01560 HCV_NS1 PF01538 HCV_NS2 PF01006 HCV_NS4a PF01001 HCV_NS4b PF01506 HCV_NS5a PF08300 HCV_NS5a_1a PF08301 HCV_NS5a_1b PF02907 Peptidase_S29 PF00998 RdRP_3 component viral capsid component virion component viral envelope function hydrolase activity function nucleotide binding function purine nucleotide binding function peptidase activity function helicase activity function adenyl nucleotide binding function transferase activity function nucleotidyltransferase activity function binding function ATP binding function transferase activity, transferring phosphorus-containing groups function serine-type peptidase activity function catalytic activity function nucleic acid binding function RNA-directed RNA polymerase activity function RNA binding function structural molecule activity process viral infectious cycle process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process viral genome replication process macromolecule metabolism process protein metabolism process cellular protein metabolism process proteolysis process interaction between organisms process interspecies interaction between organisms process transcription process physiological process process symbiosis, encompassing mutualism through parasitism process interaction with host process metabolism process virus-host interaction process viral life cycle process cellular metabolism process transformation of host cell by virus "
drug:(2R,3R)-3-{[3,5-BIS(TRIFLUOROMETHYL)PHENYL]AMINO}-2-CYANO-3-THIOXOPROPANAMIDErdfs:label"(2R,3R)-3-{[3,5-BIS(TRIFLUOROMETHYL)PHENYL]AMINO}-2-CYANO-3-THIOXOPROPANAMIDE"
drug:(2R,3R)-3-{[3,5-BIS(TRIFLUOROMETHYL)PHENYL]AMINO}-2-CYANO-3-THIOXOPROPANAMIDErdf:typedrugbank:drugs
drug:(2R,3R)-7-(methylsulfonyl)-3-(2,4,5-trifluorophenyl)-1,2,3,4-tetrahydropyrido[1,2-a]benzimidazol-2-aminedrugbank:description" experimental This compound belongs to the benzimidazoles. These are organic compounds containing a benzene ring fused to an imidazole ring (five member ring containing a nitrogen atom, 4 carbon atoms, and two double bonds). Benzimidazoles Organic Compounds Heterocyclic Compounds Benzimidazoles Fluorobenzenes Aryl Fluorides N-substituted Imidazoles Sulfones Sulfoxides Polyamines Monoalkylamines Organofluorides fluorobenzene aryl fluoride aryl halide benzene n-substituted imidazole sulfonyl imidazole sulfone azole sulfoxide polyamine organofluoride organohalogen amine primary amine primary aliphatic amine organonitrogen compound logP 1.8 ALOGPS logS -4 ALOGPS Water Solubility 3.89e-02 g/l ALOGPS logP 1.86 ChemAxon IUPAC Name (11R,12R)-5-methanesulfonyl-11-(2,4,5-trifluorophenyl)-1,8-diazatricyclo[7.4.0.0^{2,7}]trideca-2,4,6,8-tetraen-12-amine ChemAxon Traditional IUPAC Name (11R,12R)-5-methanesulfonyl-11-(2,4,5-trifluorophenyl)-1,8-diazatricyclo[7.4.0.0^{2,7}]trideca-2,4,6,8-tetraen-12-amine ChemAxon Molecular Weight 395.399 ChemAxon Monoisotopic Weight 395.091532076 ChemAxon SMILES [H][C@]1(N)CN2C(C[C@]1([H])C1=C(F)C=C(F)C(F)=C1)=NC1=CC(=CC=C21)S(C)(=O)=O ChemAxon Molecular Formula C18H16F3N3O2S ChemAxon InChI InChI=1S/C18H16F3N3O2S/c1-27(25,26)9-2-3-17-16(4-9)23-18-6-11(15(22)8-24(17)18)10-5-13(20)14(21)7-12(10)19/h2-5,7,11,15H,6,8,22H2,1H3/t11-,15+/m1/s1 ChemAxon InChIKey InChIKey=HJJAYSSCWGUPKO-ABAIWWIYSA-N ChemAxon Polar Surface Area (PSA) 77.98 ChemAxon Refractivity 94.04 ChemAxon Polarizability 37.98 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 19.67 ChemAxon pKa (strongest basic) 8.86 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11710963 PubChem Substance 99443664 ChemSpider 9885685 PDB 677 BE0000854 Dipeptidyl peptidase 4 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dipeptidyl peptidase 4 Amino acid transport and metabolism Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Plays a role in T-cell activation DPP4 2q24.3 Cell membrane; single-pass type II membrane protein. Processed form:Secreted protein. Note=Also exis 7-28 5.92 88279.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3009 GenAtlas DPP4 GeneCards DPP4 GenBank Gene Database U13735 GenBank Protein Database 535388 UniProtKB P27487 UniProt Accession DPP4_HUMAN ADABP Adenosine deaminase complexing protein 2 Dipeptidyl peptidase IV DPP IV EC 3.4.14.5 T-cell activation antigen CD26 TP103 >Dipeptidyl peptidase 4 MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSL RWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNY VKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNL PSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSF YSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYL CDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPS EPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISN EYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLY TLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKY PLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGT FEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWE YYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQIS KALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP >2301 bp ATGAAGACACCGTGGAAGGTTCTTCTGGGACTGCTGGGTGCTGCTGCGCTTGTCACCATC ATCACCGTGCCCGTGGTTCTGCTGAACAAAGGCACAGATGATGCTACAGCTGACAGTCGC AAAACTTACACTCTAACTGATTACTTAAAAAATACTTATAGACTGAAGTTATACTCCTTA AGATGGATTTCAGATCATGAATATCTCTACAAACAAGAAAATAATATCTTGGTATTCAAT GCTGAATATGGAAACAGCTCAGTTTTCTTGGAGAACAGTACATTTGATGAGTTTGGACAT TCTATCAATGATTATTCAATATCTCCTGATGGGCAGTTTATTCTCTTAGAATACAACTAC GTGAAGCAATGGAGGCATTCCTACACAGCTTCATATGACATTTATGATTTAAATAAAAGG CAGCTGATTACAGAAGAGAGGATTCCAAACAACACACAGTGGGTCACATGGTCACCAGTG GGTCATAAATTGGCATATGTTTGGAACAATGACATTTATGTTAAAATTGAACCAAATTTA CCAAGTTACAGAATCACATGGACGGGGAAAGAAGATATAATATATAATGGAATAACTGAC TGGGTTTATGAAGAGGAAGTCTTCAGTGCCTACTCTGCTCTGTGGTGGTCTCCAAACGGC ACTTTTTTAGCATATGCCCAATTTAACGACACAGAAGTCCCACTTATTGAATACTCCTTC TACTCTGATGAGTCACTGCAGTACCCAAAGACTGTACGGGTTCCATATCCAAAGGCAGGA GCTGTGAATCCAACTGTAAAGTTCTTTGTTGTAAATACAGACTCTCTCAGCTCAGTCACC AATGCAACTTCCATACAAATCACTGCTCCTGCTTCTATGTTGATAGGGGATCACTACTTG TGTGATGTGACATGGGCAACACAAGAAAGAATTTCTTTGCAGTGGCTCAGGAGGATTCAG AACTATTCGGTCATGGATATTTGTGACTATGATGAATCCAGTGGAAGATGGAACTGCTTA GTGGCACGGCAACACATTGAAATGAGTACTACTGGCTGGGTTGGAAGATTTAGGCCTTCA GAACCTCATTTTACCCTTGATGGTAATAGCTTCTACAAGATCATCAGCAATGAAGAAGGT TACAGACACATTTGCTATTTCCAAATAGATAAAAAAGACTGCACATTTATTACAAAAGGC ACCTGGGAAGTCATCGGGATAGAAGCTCTAACCAGTGATTATCTATACTACATTAGTAAT GAATATAAAGGAATGCCAGGAGGAAGGAATCTTTATAAAATCCAACTTAGTGACTATACA AAAGTGACATGCCTCAGTTGTGAGCTGAATCCGGAAAGGTGTCAGTACTATTCTGTGTCA TTCAGTAAAGAGGCGAAGTATTATCAGCTGAGATGTTCCGGTCCTGGTCTGCCCCTCTAT ACTCTACACAGCAGCGTGAATGATAAAGGGCTGAGAGTCCTGGAAGACAATTCAGCTTTG GATAAAATGCTGCAGAATGTCCAGATGCCCTCCAAAAAACTGGACTTCATTATTTTGAAT GAAACAAAATTTTGGTATCAGATGATCTTGCCTCCTCATTTTGATAAATCCAAGAAATAT CCTCTACTATTAGATGTGTATGCAGGCCCATGTAGTCAAAAAGCAGACACTGTCTTCAGA CTGAACTGGGCCACTTACCTTGCAAGCACAGAAAACATTATAGTAGCTAGCTTTGATGGC AGAGGAAGTGGTTACCAAGGAGATAAGATCATGCATGCAATCAACAGAAGACTGGGAACA TTTGAAGTTGAAGATCAAATTGAAGCAGCCAGACAATTTTCAAAAATGGGATTTGTGGAC AACAAACGAATTGCAATTTGGGGCTGGTCATATGGAGGGTACGTAACCTCAATGGTCCTG GGATCGGGAAGTGGCGTGTTCAAGTGTGGAATAGCCGTGGCGCCTGTATCCCGGTGGGAG TACTATGACTCAGTGTACACAGAACGTTACATGGGTCTCCCAACTCCAGAAGACAACCTT GACCATTACAGAAATTCAACAGTCATGAGCAGAGCTGAAAATTTTAAACAAGTTGAGTAC CTCCTTATTCATGGAACAGCAGATGATAACGTTCACTTTCAGCAGTCAGCTCAGATCTCC AAAGCCCTGGTCGATGTTGGAGTGGATTTCCAGGCAATGTGGTATACTGATGAAGACCAT GGAATAGCTAGCAGCACAGCACACCAACATATATATACCCACATGAGCCACTTCATAAAA CAATGTTTCTCTTTACCTTAG PF00930 DPPIV_N PF00326 Peptidase_S9 component cell component membrane function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function serine-type peptidase activity function hydrolase activity function dipeptidyl-peptidase IV activity function prolyl oligopeptidase activity process protein metabolism process cellular protein metabolism process physiological process process proteolysis process metabolism process macromolecule metabolism "
drug:(2R,3R)-7-(methylsulfonyl)-3-(2,4,5-trifluorophenyl)-1,2,3,4-tetrahydropyrido[1,2-a]benzimidazol-2-aminerdfs:label"(2R,3R)-7-(methylsulfonyl)-3-(2,4,5-trifluorophenyl)-1,2,3,4-tetrahydropyrido[1,2-a]benzimidazol-2-amine"
drug:(2R,3R)-7-(methylsulfonyl)-3-(2,4,5-trifluorophenyl)-1,2,3,4-tetrahydropyrido[1,2-a]benzimidazol-2-aminerdf:typedrugbank:drugs
drug:(2R,3R)-N^1^-[(1S)-2,2-DIMETHYL-1-(METHYLCARBAMOYL)PROPYL]-N^4^-HYDROXY-2-(2-METHYLPROPYL)-3-{[(1,3-THIAZOL-2-YLCARBONYL)AMINO]METHYL}BUTANEDIAMIDEdrugbank:description" experimental This compound belongs to the n-acyl-alpha amino acids and derivatives. These are compounds containing an alpha amino acid (or a derivative thereof) which bears an acyl group at his terminal nitrogen atom. N-acyl-alpha Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Alpha Amino Acid Amides N-acyl Amines Beta Amino Acids and Derivatives Thiazolecarboxamides Hydroxamic Acids Secondary Carboxylic Acid Amides Carboxylic Acids Enolates Polyamines beta amino acid or derivative thiazolecarboxylic acid or derivative thiazolecarboxamide azole thiazole carboxamide group secondary carboxylic acid amide hydroxamic acid carboxylic acid polyamine enolate amine organonitrogen compound logP 0.88 ALOGPS logS -4.4 ALOGPS Water Solubility 2.01e-02 g/l ALOGPS logP 0.52 ChemAxon IUPAC Name (2R,3R)-N-[(1S)-2,2-dimethyl-1-(methylcarbamoyl)propyl]-N'-hydroxy-2-(2-methylpropyl)-3-[(1,3-thiazol-2-ylformamido)methyl]butanediamide ChemAxon Traditional IUPAC Name (2R,3R)-N-[(1S)-2,2-dimethyl-1-(methylcarbamoyl)propyl]-N'-hydroxy-2-(2-methylpropyl)-3-[(1,3-thiazol-2-ylformamido)methyl]butanediamide ChemAxon Molecular Weight 455.572 ChemAxon Monoisotopic Weight 455.220239881 ChemAxon SMILES [H][C@@](CNC(=O)C1=NC=CS1)(C(=O)NO)[C@@]([H])(CC(C)C)C(=O)N[C@]([H])(C(=O)NC)C(C)(C)C ChemAxon Molecular Formula C20H33N5O5S ChemAxon InChI InChI=1S/C20H33N5O5S/c1-11(2)9-12(15(26)24-14(17(28)21-6)20(3,4)5)13(16(27)25-30)10-23-18(29)19-22-7-8-31-19/h7-8,11-14,30H,9-10H2,1-6H3,(H,21,28)(H,23,29)(H,24,26)(H,25,27)/t12-,13+,14-/m1/s1 ChemAxon InChIKey InChIKey=GAHIXYNNFMCKFQ-HZSPNIEDSA-N ChemAxon Polar Surface Area (PSA) 149.52 ChemAxon Refractivity 115.67 ChemAxon Polarizability 47.95 ChemAxon Rotatable Bond Count 11 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 8.85 ChemAxon pKa (strongest basic) 0.38 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PDB WR2 BE0003872 Disintegrin and metalloproteinase domain-containing protein 28 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Disintegrin and metalloproteinase domain-containing protein 28 Involved in metalloendopeptidase activity May play a role in the adhesive and proteolytic events that occur during lymphocyte emigration or may function in ectodomain shedding of lymphocyte surface target proteins, such as FASL and CD40L. May be involved in sperm maturation ADAM28 8p21.2 Isoform 2:Secreted 666-686 6.8 87180.0 Human HUGO Gene Nomenclature Committee (HGNC) GNC:206 GeneCards ADAM28 GenBank Gene Database AF137334 GenBank Protein Database 4583505 UniProtKB Q9UKQ2 UniProt Accession ADA28_HUMAN ADAM 28 eMDC II Epididymial metalloproteinase-like, disintegrin-like, and cysteine-rich protein II MDC-L Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L >Disintegrin and metalloproteinase domain-containing protein 28 MLQGLLPVSLLLSVAVSAIKELPGVKKYEVVYPIRLHPLHKREAKEPEQQEQFETELKYK MTINGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYYQGHILNEKVSDAS ISTCRGLRGYFSQGDQRYFIEPLSPIHRDGQEHALFKYNPDEKNYDSTCGMDGVLWAHDL QQNIALPATKLVKLKDRKVQEHEKYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNM LYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATE LAGTTVGLAFMSTMCSPYSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYSCKCPSTI CVMDKALSFYIPTDFSSCSRLSYDKFFEDKLSNCLFNAPLPTDIISTPICGNQLVEMGED CDCGTSEECTNICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNG KSGNCPDDRFQVNGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNRNEGGSK YGYCRRVDDTLIPCKANDTMCGKLFCQGGSDNLPWKGRIVTFLTCKTFDPEDTSQEIGMV ANGTKCGDNKVCINAECVDIEKAYKSTNCSSKCKGHAVCDHELQCQCEEGWIPPDCDDSS VVFHFSIVVGVLFPMAVIFVVVAMVIRHQSSREKQKKDQRPLSTTGTRPHKQKRKPQMVK AVQPQEMSQMKPHVYDLPVEGNEPPASFHKDTNALPPTVFKDNPMSTPKDSNPEA >2328 bp ATGTTGCAAGGTCTCCTGCCAGTCAGTCTCCTCCTCTCTGTTGCAGTAAGTGCTATAAAA GAACTCCCTGGGGTGAAGAAGTATGAAGTGGTTTATCCTATAAGACTTCATCCACTGCAT AAAAGAGAGGCCAAAGAGCCAGAGCAACAGGAACAATTTGAAACTGAATTAAAGTATAAA ATGACAATTAATGGAAAAATTGCAGTGCTTTATTTGAAAAAAAACAAGAACCTCCTTGCA CCAGGCTACACGGAAACATATTATAATTCCACTGGAAAGGAGATCACCACAAGCCCACAA ATTATGGATGATTGTTATTATCAAGGACATATTCTTAATGAAAAGGTTTCTGACGCTAGC ATCAGCACATGTAGGGGTCTAAGGGGCTACTTCAGTCAGGGGGATCAAAGATACTTTATT GAACCTTTAAGCCCCATACATCGGGATGGACAGGAGCATGCACTCTTCAAGTATAACCCT GATGAAAAGAATTATGACAGCACCTGTGGGATGGATGGTGTGTTGTGGGCCCACGATTTG CAGCAGAACATTGCCCTACCTGCCACCAAACTAGTAAAATTGAAAGACAGGAAGGTTCAG GAACATGAGAAATACATAGAATATTATCTGGTCCTGGATAATGGTGAGTTTAAAAGGTAC AATGAGAATCAAGATGAGATCAGAAAGAGGGTATTTGAGATGGCTAATTATGTCAACATG CTTTATAAAAAGCTCAATACTCATGTGGCCTTAGTTGGTATGGAAATCTGGACTGACAAG GATAAGATAAAGATAACCCCAAATGCAAGCTTCACCTTGGAGAATTTTTCTAAATGGAGG GGGAGTGTTCTCTCAAGAAGAAAGCGTCATGATATTGCTCAGTTAATCACAGCAACAGAA CTTGCTGGAACGACTGTGGGTCTTGCATTTATGTCTACAATGTGTTCTCCTTATTCTGTT GGCGTTGTTCAGGACCACAGCGATAATCTTCTTAGAGTTGCAGGGACAATGGCACATGAA ATGGGCCACAACTTTGGAATGTTTCATGACGACTATTCTTGCAAGTGTCCTTCTACAATA TGTGTGATGGACAAAGCACTGAGCTTCTATATACCCACAGACTTCAGTTCCTGCAGCCGT CTCAGCTATGACAAGTTTTTTGAAGATAAATTATCAAATTGCCTCTTTAATGCTCCATTG CCTACAGATATCATATCCACTCCAATTTGTGGGAACCAGTTGGTGGAAATGGGAGAGGAC TGTGATTGTGGGACATCTGAGGAATGTACCAATATTTGCTGTGATGCTAAGACATGTAAA ATCAAAGCAACTTTTCAATGTGCATTAGGAGAATGTTGTGAAAAATGCCAATTTAAAAAG GCTGGGATGGTGTGCAGACCAGCAAAAGATGAGTGCGACCTGCCTGAAATGTGTAATGGT AAATCTGGTAATTGTCCTGATGATAGATTCCAAGTCAATGGCTTCCCTTGCCATCACGGG AAGGGCCACTGCTTGATGGGCACATGCCCCACACTGCGGGAGCAGTGCACAGAGCTGTGG GGACCAGGAACTGAGGTTGCAGATAAGTCATGTTACAACAGGAATGAAGGTGGGTCAAAG TACGGGTACTGTCGCAGAGTGGATGACACACTCATTCCCTGCAAAGCAAATGATACCATG TGTGGGAAGTTGTTCTGTCAAGGTGGGTCGGATAATTTGCCCTGGAAAGGACGGATAGTG ACTTTCCTGACATGTAAAACATTTGATCCTGAAGACACAAGTCAAGAAATAGGCATGGTG GCCAATGGAACTAAGTGTGGCGATAACAAGGTTTGCATTAATGCAGAATGTGTGGATATT GAGAAAGCCTACAAATCAACCAATTGCTCATCCAAGTGCAAAGGACATGCTGTGTGTGAC CATGAGCTCCAGTGTCAATGTGAGGAAGGATGGATCCCTCCCGACTGCGATGACTCCTCA GTGGTCTTCCACTTCTCCATTGTGGTTGGGGTGCTGTTCCCAATGGCGGTCATTTTTGTG GTGGTTGCTATGGTAATCCGGCACCAGAGCTCCAGAGAAAAGCAGAAGAAAGATCAGAGG CCACTATCTACCACTGGCACCAGGCCACACAAACAGAAGAGGAAACCCCAGATGGTAAAG GCTGTTCAACCCCAAGAGATGAGTCAGATGAAGCCCCATGTGTATGATCTGCCAGTAGAA GGCAATGAGCCCCCAGCCTCTTTTCATAAAGACACAAACGCACTTCCCCCTACTGTTTTC AAGGATAATCCAATGTCTACACCTAAGGACTCAAATCCAGAAGCATGA PF01562 Pep_M12B_propep PF01421 Reprolysin PF00200 Disintegrin PF08516 ADAM_CR component extracellular matrix component extracellular matrix (sensu Metazoa) function ion binding function metallopeptidase activity function cation binding function metalloendopeptidase activity function transition metal ion binding function zinc ion binding function binding function catalytic activity function peptidase activity function hydrolase activity function endopeptidase activity process macromolecule metabolism process proteolysis process physiological process process protein metabolism process cellular protein metabolism process metabolism "
drug:(2R,3R)-N^1^-[(1S)-2,2-DIMETHYL-1-(METHYLCARBAMOYL)PROPYL]-N^4^-HYDROXY-2-(2-METHYLPROPYL)-3-{[(1,3-THIAZOL-2-YLCARBONYL)AMINO]METHYL}BUTANEDIAMIDErdfs:label"(2R,3R)-N^1^-[(1S)-2,2-DIMETHYL-1-(METHYLCARBAMOYL)PROPYL]-N^4^-HYDROXY-2-(2-METHYLPROPYL)-3-{[(1,3-THIAZOL-2-YLCARBONYL)AMINO]METHYL}BUTANEDIAMIDE"
drug:(2R,3R)-N^1^-[(1S)-2,2-DIMETHYL-1-(METHYLCARBAMOYL)PROPYL]-N^4^-HYDROXY-2-(2-METHYLPROPYL)-3-{[(1,3-THIAZOL-2-YLCARBONYL)AMINO]METHYL}BUTANEDIAMIDErdf:typedrugbank:drugs
drug:(2R,3R,4R,5S)-2-(HYDROXYMETHYL)-1-NONYLPIPERIDINE-3,4,5-TRIOLdrugbank:description" experimental This compound belongs to the piperidines. These are compounds containing a piperidine ring, which is a saturated aliphatic six-member ring with one nitrogen atom and five carbon atoms. Piperidines Organic Compounds Heterocyclic Compounds Piperidines Tertiary Amines Secondary Alcohols 1,2-Diols Polyamines Primary Alcohols polyol 1,2-diol secondary alcohol tertiary amine primary alcohol polyamine amine alcohol organonitrogen compound logP 1.3 ALOGPS logS -1.5 ALOGPS Water Solubility 9.58e+00 g/l ALOGPS logP 1.04 ChemAxon IUPAC Name (2R,3R,4R,5S)-2-(hydroxymethyl)-1-nonylpiperidine-3,4,5-triol ChemAxon Traditional IUPAC Name (2R,3R,4R,5S)-2-(hydroxymethyl)-1-nonylpiperidine-3,4,5-triol ChemAxon Molecular Weight 289.4109 ChemAxon Monoisotopic Weight 289.225308485 ChemAxon SMILES [H][C@]1(O)CN(CCCCCCCCC)[C@]([H])(CO)[C@@]([H])(O)[C@]1([H])O ChemAxon Molecular Formula C15H31NO4 ChemAxon InChI InChI=1S/C15H31NO4/c1-2-3-4-5-6-7-8-9-16-10-13(18)15(20)14(19)12(16)11-17/h12-15,17-20H,2-11H2,1H3/t12-,13+,14-,15-/m1/s1 ChemAxon InChIKey InChIKey=FTSCEGKYKXESFF-LXTVHRRPSA-N ChemAxon Polar Surface Area (PSA) 84.16 ChemAxon Refractivity 78.75 ChemAxon Polarizability 34.57 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 12.9 ChemAxon pKa (strongest basic) 8.37 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 501640 PubChem Substance 99444754 ChemSpider 438794 PDB NND BE0000978 Glucosylceramidase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Glucosylceramidase Involved in glucosylceramidase activity D-glucosyl-N-acylsphingosine + H(2)O = D- glucose + N-acylsphingosine GBA 1q21 Lysosome; lysosomal membrane; peripheral membrane protein; lumenal side. Note=Interaction with sapon None 7.66 59717.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:4177 GenAtlas GBA GeneCards GBA GenBank Gene Database M16328 GenBank Protein Database 183008 UniProtKB P04062 UniProt Accession GLCM_HUMAN Acid beta-glucosidase Alglucerase Beta-glucocerebrosidase D-glucosyl-N-acylsphingosine glucohydrolase EC 3.2.1.45 Glucosylceramidase precursor Imiglucerase >Glucosylceramidase precursor MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNAT YCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGF GGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDD FQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQP GDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIA RDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAK ATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDW NLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQK NDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ >1551 bp ATGGCTGGCAGCCTCACAGGTTTGCTTCTACTTCAGGCAGTGTCGTGGGCATCAGGTGCC CGCCCCTGCATCCCTAAAAGCTTCGGCTACAGCTCGGTGGTGTGTGTCTGCAATGCCACA TACTGTGACTCCTTTGACCCCCCGACCTTTCCTGCCCTTGGTACCTTCAGCCGCTATGAG AGTACACGCAGTGGGCGACGGATGGAGCTGAGTATGGGGCCCATCCAGGCTAATCACACG GGCACAGGCCTGCTACTGACCCTGCAGCCAGAACAGAAGTTCCAGAAAGTGAAGGGATTT GGAGGGGCCATGACAGATGCTGCTGCTCTCAACATCCTTGCCCTGTCACCCCCTGCCCAA AATTTGCTACTTAAATCGTACTTCTCTGAAGAAGGAATCGGATATAACATCATCCGGGTA CCCATGGCCAGCTGTGACTTCTCCATCCGCACCTACACCTATGCAGACACCCCTGATGAT TTCCAGTTGCACAACTTCAGCCTCCCAGAGGAAGATACCAAGCTCAAGATACCCCTGATT CACCGAGCCCTGCAGTTGGCCCAGCGTCCCGTTTCACTCCTTGCCAGCCCCTGGACATCA CCCACTTGGCTCAAGACCAATGGAGCGGTGAATGGGAAGGGGTCACTCAAGGGACAGCCC GGAGACATCTACCACCAGACCTGGGCCAGATACTTTGTGAAGTTCCTGGATGCCTATGCT GAGCACAAGTTACAGTTCTGGGCAGTGACAGCTGAAAATGAGCCTTCTGCTGGGCTGTTG AGTGGATACCCCTTCCAGTGCCTGGGCTTCACCCCTGAACATCAGCGAGACTTCATTGCC CGTGACCTAGGTCCTACCCTCGCCAACAGTACTCACCACAATGTCCGCCTACTCATGCTG GATGACCAACGCTTGCTGCTGCCCCACTGGGCAAAGGTGGTACTGACAGACCCAGAAGCA GCTAAATATGTTCATGGCATTGCTGTACATTGGTACCTGGACTTTCTGGCTCCAGCCAAA GCCACCCTAGGGGAGACACACCGCCTGTTCCCCAACACCATGCTCTTTGCCTCAGAGGCC TGTGTGGGCTCCAAGTTCTGGGAGCAGAGTGTGCGGCTAGGCTCCTGGGATCGAGGGATG CAGTACAGCCACAGCATCATCACGAACCTCCTGTACCATGTGGTCGGCTGGACCGACTGG AACCTTGCCCTGAACCCCGAAGGAGGACCCAATTGGGTGCGTAACTTTGTCGACAGTCCC ATCATTGTAGACATCACCAAGGACACGTTTTACAAACAGCCCATGTTCTACCACCTTGGC CACTTCAGCAAGTTCATTCCTGAGGGCTCCCAGAGAGTGGGGCTGGTTGCCAGTCAGAAG AACGACCTGGACGCAGTGGCACTGATGCATCCCGATGGCTCTGCTGTTGTGGTCGTGCTA AACCGCTCCTCTAAGGATGTGCCTCTTACCATCAAGGATCCTGCTGTGGGCTTCCTGGAG ACAATCTCACCTGGCTACTCCATTCACACCTACCTGTGGCATCGCCAGTGA PF02055 Glyco_hydro_30 component organelle component membrane-bound organelle component intracellular membrane-bound organelle component vacuole component lytic vacuole component lysosome function hydrolase activity, acting on glycosyl bonds function catalytic activity function hydrolase activity, hydrolyzing O-glycosyl compounds function hydrolase activity function glucosylceramidase activity process vacuole organization and biogenesis process lysosome organization and biogenesis process sphingolipid metabolism process organelle organization and biogenesis process primary metabolism process physiological process process lipid metabolism process cellular physiological process process cellular lipid metabolism process cell organization and biogenesis process metabolism process membrane lipid metabolism "
drug:(2R,3R,4R,5S)-2-(HYDROXYMETHYL)-1-NONYLPIPERIDINE-3,4,5-TRIOLrdfs:label"(2R,3R,4R,5S)-2-(HYDROXYMETHYL)-1-NONYLPIPERIDINE-3,4,5-TRIOL"
drug:(2R,3R,4R,5S)-2-(HYDROXYMETHYL)-1-NONYLPIPERIDINE-3,4,5-TRIOLrdf:typedrugbank:drugs
drug:(2R,3R,4S)-3-(4-HYDROXYPHENYL)-4-METHYL-2-[4-(2-PYRROLIDIN-1-YLETHOXY)PHENYL]CHROMAN-6-OLdrugbank:description" experimental This compound belongs to the isoflavanols. These are polycyclic compounds containing an hydroxylated isoflavan skeleton. Isoflavanols Organic Compounds Phenylpropanoids and Polyketides Isoflavonoids Isoflavans Stilbenes Benzopyrans Phenol Ethers Alkyl Aryl Ethers Phenols and Derivatives Pyrrolidines Tertiary Amines Polyols Enols Polyamines stilbene benzopyran chromane phenol ether phenol derivative alkyl aryl ether benzene pyrrolidine tertiary amine polyol ether polyamine enol amine organonitrogen compound logP 5.26 ALOGPS logS -5 ALOGPS Water Solubility 4.44e-03 g/l ALOGPS logP 5.17 ChemAxon IUPAC Name (2R,3R,4S)-3-(4-hydroxyphenyl)-4-methyl-2-{4-[2-(pyrrolidin-1-yl)ethoxy]phenyl}-3,4-dihydro-2H-1-benzopyran-6-ol ChemAxon Traditional IUPAC Name (2R,3R,4S)-3-(4-hydroxyphenyl)-4-methyl-2-{4-[2-(pyrrolidin-1-yl)ethoxy]phenyl}-3,4-dihydro-2H-1-benzopyran-6-ol ChemAxon Molecular Weight 445.55 ChemAxon Monoisotopic Weight 445.225308485 ChemAxon SMILES [H][C@@]1(C)C2=CC(O)=CC=C2O[C@@]([H])(C2=CC=C(OCCN3CCCC3)C=C2)[C@@]1([H])C1=CC=C(O)C=C1 ChemAxon Molecular Formula C28H31NO4 ChemAxon InChI InChI=1S/C28H31NO4/c1-19-25-18-23(31)10-13-26(25)33-28(27(19)20-4-8-22(30)9-5-20)21-6-11-24(12-7-21)32-17-16-29-14-2-3-15-29/h4-13,18-19,27-28,30-31H,2-3,14-17H2,1H3/t19-,27-,28+/m1/s1 ChemAxon InChIKey InChIKey=XPVKGTWRXBSJKO-LHXLBICKSA-N ChemAxon Polar Surface Area (PSA) 62.16 ChemAxon Refractivity 129.81 ChemAxon Polarizability 50.08 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 9.78 ChemAxon pKa (strongest basic) 8.9 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 5 ChemAxon Bioavailability 1 ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon ChEBI 41593 PubChem Compound 4369568 PubChem Substance 99444038 ChemSpider 3572095 PDB CM4 BE0000123 Estrogen receptor Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Estrogen receptor Involved in transcription factor activity Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues ESR1 6q25.1 Nucleus None 8.14 66217.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3467 GenAtlas ESR1 GeneCards ESR1 GenBank Gene Database X03635 GenBank Protein Database 31234 IUPHAR 620 Guide to Pharmacology 107 UniProtKB P03372 UniProt Accession ESR1_HUMAN ER ER-alpha Estradiol receptor >Estrogen receptor MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAY EFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPF LQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAK ETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQAC RLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKR SKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINW AKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEG MVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLD KITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLL LEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV >1788 bp ATGACCATGACCCTCCACACCAAAGCATCTGGGATGGCCCTACTGCATCAGATCCAAGGG AACGAGCTGGAGCCCCTGAACCGTCCGCAGCTCAAGATCCCCCTGGAGCGGCCCCTGGGC GAGGTGTACCTGGACAGCAGCAAGCCCGCCGTGTACAACTACCCCGAGGGCGCCGCCTAC GAGTTCAACGCCGCGGCCGCCGCCAACGCGCAGGTCTACGGTCAGACCGGCCTCCCCTAC GGCCCCGGGTCTGAGGCTGCGGCGTTCGGCTCCAACGGCCTGGGGGGTTTCCCCCCACTC AACAGCGTGTCTCCGAGCCCGCTGATGCTACTGCACCCGCCGCCGCAGCTGTCGCCTTTC CTGCAGCCCCACGGCCAGCAGGTGCCCTACTACCTGGAGAACGAGCCCAGCGGCTACACG GTGCGCGAGGCCGGCCCGCCGGCATTCTACAGGCCAAATTCAGATAATCGACGCCAGGGT GGCAGAGAAAGATTGGCCAGTACCAATGACAAGGGAAGTATGGCTATGGAATCTGCCAAG GAGACTCGCTACTGTGCAGTGTGCAATGACTATGCTTCAGGCTACCATTATGGAGTCTGG TCCTGTGAGGGCTGCAAGGCCTTCTTCAAGAGAAGTATTCAAGGACATAACGACTATATG TGTCCAGCCACCAACCAGTGCACCATTGATAAAAACAGGAGGAAGAGCTGCCAGGCCTGC CGGCTCCGCAAATGCTACGAAGTGGGAATGATGAAAGGTGGGATACGAAAAGACCGAAGA GGAGGGAGAATGTTGAAACACAAGCGCCAGAGAGATGATGGGGAGGGCAGGGGTGAAGTG GGGTCTGCTGGAGACATGAGAGCTGCCAACCTTTGGCCAAGCCCGCTCATGATCAAACGC TCTAAGAAGAACAGCCTGGCCTTGTCCCTGACGGCCGACCAGATGGTCAGTGCCTTGTTG GATGCTGAGCCCCCCATACTCTATTCCGAGTATGATCCTACCAGACCCTTCAGTGAAGCT TCGATGATGGGCTTACTGACCAACCTGGCAGACAGGGAGCTGGTTCACATGATCAACTGG GCGAAGAGGGTGCCAGGCTTTGTGGATTTGACCCTCCATGATCAGGTCCACCTTCTAGAA TGTGCCTGGCTAGAGATCCTGATGATTGGTCTCGTCTGGCGCTCCATGGAGCACCCAGTG AAGCTACTGTTTGCTCCTAACTTGCTCTTGGACAGGAACCAGGGAAAATGTGTAGAGGGC ATGGTGGAGATCTTCGACATGCTGCTGGCTACATCATCTCGGTTCCGCATGATGAATCTG CAGGGAGAGGAGTTTGTGTGCCTCAAATCTATTATTTTGCTTAATTCTGGAGTGTACACA TTTCTGTCCAGCACCCTGAAGTCTCTGGAAGAGAAGGACCATATCCACCGAGTCCTGGAC AAGATCACAGACACTTTGATCCACCTGATGGCCAAGGCAGGCCTGACCCTGCAGCAGCAG CACCAGCGGCTGGCCCAGCTCCTCCTCATCCTCTCCCACATCAGGCACATGAGTAACAAA GGCATGGAGCATCTGTACAGCATGAAGTGCAAGAACGTGGTGCCCCTCTATGACCTGCTG CTGGAGATGCTGGACGCCCACCGCCTACATGCGCCCACTAGCCGTGGAGGGGCATCCGTG GAGGAGACGGACCAAAGCCACTTGGCCACTGCGGGCTCTACTTCATCGCATTCCTTGCAA AAGTATTACATCACGGGGGAGGCAGAGGGTTTCCCTGCCACAGTCTGA PF00104 Hormone_recep PF00105 zf-C4 PF02159 Oest_recep component intracellular membrane-bound organelle component nucleus component organelle component membrane-bound organelle function signal transducer activity function receptor activity function nucleic acid binding function binding function steroid hormone receptor activity function ion binding function transcription factor activity function steroid binding function cation binding function ligand-dependent nuclear receptor activity function transition metal ion binding function DNA binding function zinc ion binding process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent process regulation of biological process process regulation of physiological process process regulation of metabolism "
drug:(2R,3R,4S)-3-(4-HYDROXYPHENYL)-4-METHYL-2-[4-(2-PYRROLIDIN-1-YLETHOXY)PHENYL]CHROMAN-6-OLrdfs:label"(2R,3R,4S)-3-(4-HYDROXYPHENYL)-4-METHYL-2-[4-(2-PYRROLIDIN-1-YLETHOXY)PHENYL]CHROMAN-6-OL"
drug:(2R,3R,4S)-3-(4-HYDROXYPHENYL)-4-METHYL-2-[4-(2-PYRROLIDIN-1-YLETHOXY)PHENYL]CHROMAN-6-OLrdf:typedrugbank:drugs
drug:(2R,3R,4S,5R)-2-[6-amino-8-[(3,4-dichlorophenyl)methylamino]purin-9-yl]-5-(hydroxymethyl)oxolane-3,4-dioldrugbank:description" experimental This compound belongs to the purine nucleosides and analogues. These are compounds comprising a purine base attached to a sugar. Purine Nucleosides and Analogues Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Glycosyl Compounds Pentoses Purines and Purine Derivatives Dichlorobenzenes Aminopyrimidines and Derivatives Aminoimidazoles Aryl Chlorides N-substituted Imidazoles Primary Aromatic Amines Tetrahydrofurans Oxolanes 1,2-Diols Secondary Alcohols Primary Alcohols Polyamines Ethers Secondary Amines Organochlorides pentose monosaccharide imidazopyrimidine purine 1,2-dichlorobenzene aminopyrimidine chlorobenzene aminoimidazole primary aromatic amine aryl halide aryl chloride n-substituted imidazole benzene monosaccharide pyrimidine tetrahydrofuran azole imidazole oxolane secondary alcohol 1,2-diol polyamine secondary amine primary alcohol ether primary amine amine alcohol organochloride organonitrogen compound organohalogen logP 1.39 ALOGPS logS -2.9 ALOGPS Water Solubility 5.11e-01 g/l ALOGPS logP 1 ChemAxon IUPAC Name (2R,3R,4S,5R)-2-(6-amino-8-{[(3,4-dichlorophenyl)methyl]amino}-9H-purin-9-yl)-5-(hydroxymethyl)oxolane-3,4-diol ChemAxon Traditional IUPAC Name (2R,3R,4S,5R)-2-(6-amino-8-{[(3,4-dichlorophenyl)methyl]amino}purin-9-yl)-5-(hydroxymethyl)oxolane-3,4-diol ChemAxon Molecular Weight 441.269 ChemAxon Monoisotopic Weight 440.076658508 ChemAxon SMILES [H][C@]1(CO)O[C@@]([H])(N2C(NCC3=CC=C(Cl)C(Cl)=C3)=NC3=C(N)N=CN=C23)[C@]([H])(O)[C@]1([H])O ChemAxon Molecular Formula C17H18Cl2N6O4 ChemAxon InChI InChI=1S/C17H18Cl2N6O4/c18-8-2-1-7(3-9(8)19)4-21-17-24-11-14(20)22-6-23-15(11)25(17)16-13(28)12(27)10(5-26)29-16/h1-3,6,10,12-13,16,26-28H,4-5H2,(H,21,24)(H2,20,22,23)/t10-,12-,13-,16-/m1/s1 ChemAxon InChIKey InChIKey=VBJKVZXRYLCYGQ-XNIJJKJLSA-N ChemAxon Polar Surface Area (PSA) 151.57 ChemAxon Refractivity 107.08 ChemAxon Polarizability 42.57 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 9 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 12.45 ChemAxon pKa (strongest basic) 4.7 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 25195347 PubChem Substance 99443516 ChemSpider 23337032 PDB 3BK BE0003774 BAG family molecular chaperone regulator 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown BAG family molecular chaperone regulator 1 Involved in protein binding Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli BAG1 9p12 Isoform 2:Cytoplasm. Nucleus None 8.34 38877.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:937 GeneCards BAG1 GenBank Gene Database Z35491 GenBank Protein Database 1143476 UniProtKB Q99933 UniProt Accession BAG1_HUMAN BAG-1 Bcl-2-associated athanogene 1 Glucocorticoid receptor-associated protein RAP46 >BAG family molecular chaperone regulator 1 MAQRGGARRPRGDRERLGSRLRALRPGREPRQSEPPAQRGPPPSRRPPARSTASGHDRPT RGAAAGARRPRMKKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQ EVTRDEESTRSEEVTREEMAAAGLTVTVTHSNEKHDLHVTSQQGSSEPVVQDLAQVVEEV IGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLIGKKNSPQEEVELKKLKHLEKSV EKIADQLEELNKELTGIQQGFLPKDLQAEALCKLDRRVKATIEQFMKILEEIDTLILPEN FKDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFALAE >825 bp ATGAAGAAGAAAACCCGGCGCCGCTCGACCCGGAGCGAGGAGTTGACCCGGAGCGAGGAG TTGACCCTGAGTGAGGAAGCGACCTGGAGTGAAGAGGCGACCCAGAGTGAGGAGGCGACC CAGGGCGAAGAGATGAATCGGAGCCAGGAGGTGACCCGGGACGAGGAGTCGACCCGGAGC GAGGAGGTGACCAGGGAGGAAATGGCGGCAGCTGGGCTCACCGTGACTGTCACCCACAGC AATGAGAAGCACGACCTTCATGTTACCTCCCAGCAGGGCAGCAGTGAACCAGTTGTCCAA GACCTGGCCCAGGTTGTTGAAGAGGTCATAGGGGTTCCACAGTCTTTTCAGAAACTCATA TTTAAGGGAAAATCTCTGAAGGAAATGGAAACACCGTTGTCAGCACTTGGAATACAAGAT GGTTGCCGGGTCATGTTAATTGGGAAAAAGAACAGTCCACAGGAAGAGGTTGAACTAAAG AAGTTGAAACATTTGGAGAAGTCTGTGGAGAAGATAGCTGACCAGCTGGAAGAGTTGAAT AAAGAGCTTACTGGAATCCAGCAGGGTTTTCTGCCCAAGGATTTGCAAGCTGAAGCTCTC TGCAAACTTGATAGGAGAGTAAAAGCCACAATAGAGCAGTTTATGAAGATCTTGGAGGAG ATTGACACACTGATCCTGCCAGAAAATTTCAAAGACAGTAGATTGAAAAGGAAAGGCTTG GTAAAAAAGGTTCAGGCATTCCTAGCCGAGTGTGACACAGTGGAGCAGAACATCTGCCAG GAGACTGAGCGGCTGCAGTCTACAAACTTTGCCCTGGCCGAGTGA PF00240 ubiquitin PF02179 BAG function protein binding function binding process biopolymer modification process protein modification process death process cell death process programmed cell death process apoptosis process physiological process process metabolism process macromolecule metabolism process biopolymer metabolism BE0003775 Heat shock cognate 71 kDa protein Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Heat shock cognate 71 kDa protein Posttranslational modification, protein turnover, chaperones Chaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co-chaperones HSPA8 11q24.1 Cytoplasm. Melanosome None 5.16 70897.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:5241 GeneCards HSPA8 GenBank Gene Database AB034951 GenBank Protein Database 11526573 UniProtKB P11142 UniProt Accession HSP7C_HUMAN Heat shock 70 kDa protein 8 >Heat shock cognate 71 kDa protein MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA MNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVS SMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAA IAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRA RFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELN KSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTI PTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDI DANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKN SLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELE KVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD >1482 bp ATGTCCAAGGGACCTGCAGTTGGTATTGATCTTGGCACCACCTACTCTTGTGTGGGTGTT TTCCAGCACGGAAAAGTCGAGATAATTGCCAATGATCAGGGAAACCGAACCACTCCAAGC TATGTCGCCTTTACGGACACTGAACGGTTGATCGGTGATGCCGCAAAGAATCAAGTTGCA ATGAACCCCACCAACACAGTTTTTGATGCCAAACGTCTGATTGGACGCAGATTTGATGAT GCTGTTGTCCAGTCTGATATGAAACATTGGCCCTTTATGGTGGTGAATGATGCTGGCAGG CCCAAGGTCCAAGTAGAATACAAGGGAGAGACCAAAAGCTTCTATCCAGAGGAGGTGTCT TCTATGGTTCTGACAAAGATGAAGGAAATTGCAGAAGCCTACCTTGGGAAGACTGTTACC AATGCTGTGGTCACAGTGCCAGCTTACTTTAATGACTCTCAGCGTCAGGCTACCAAAGAT GCTGGAACTATTGCTGGTCTCAATGTACTTAGAATTATTAATGAGCCAACTGCTGCTGCT ATTGCTTACGGCTTAGACAAAAAGGTTGGAGCAGAAAGAAACGTGCTCATCTTTGACCTG GGAGGTGGCACTTTTGATGTGTCAATCCTCACTATTGAGGATGGAATCTTTGAGGTCAAG TCTACAGCTGGAGACACCCACTTGGGTGGAGAAGATTTTGACAACCGAATGGTCAACCAT TTTATTGCTGAGTTTAAGCGCAAGCATAAGAAGGACATCAGTGAGAACAAGAGAGCTGTA AGACGCCTCCGTACTGCTTGTGAACGTGCTAAGCGTACCCTCTCTTCCAGCACCCAGGCC AGTATTGAGATCGATTCTCTCTATGAAGGAATCGACTTCTATACCTCCATTACCCGTGCC CGATTTGAAGAACTGAATGCTGACCTGTTCCGTGGCACCCTGGACCCAGTAGAGAAAGCC CTTCGAGATGCCAAACTAGACAAGTCACAGATTCATGATATTGTCCTGGTTGGTGGTTCT ACTCGTATCCCCAAGATTCAGAAGCTTCTCCAAGACTTCTTCAATGGAAAAGAACTGAAT AAGAGCATCAACCCTGATGAAGCTGTTGCTTATGGTGCAGCTGTCCAGGCAGCCATCTTG TCTGGAGACAAGTCTGAGAATGTTCAAGATTTGCTGCTCTTGGATGTCACTCCTCTTTCC CTTGGTATTGAAACTGCTGGTGGAGTCATGACTGTCCTCATCAAGCGTAATACCACCATT CCTACCAAGCAGACACAGACCTTCACTACCTATTCTGACAACCAGCCTGGTGTGCTTATT CAGGTTTATGAAGGCGAGCGTGCCATGACAAAGGATAACAACCTGCTTGGCAAGTTTGAA CTCACAGGCATGCCAGGAGGAATGCCTGGGGGATTTCCTGGTGGTGGAGCTCCTCCCTCT GGTGGTGCTTCCTCAGGGCCCACCATTGAAGAGGTTGATTAA PF00012 HSP70 function purine nucleotide binding function adenyl nucleotide binding function ATP binding function binding function nucleotide binding "
drug:(2R,3R,4S,5R)-2-[6-amino-8-[(3,4-dichlorophenyl)methylamino]purin-9-yl]-5-(hydroxymethyl)oxolane-3,4-diolrdfs:label"(2R,3R,4S,5R)-2-[6-amino-8-[(3,4-dichlorophenyl)methylamino]purin-9-yl]-5-(hydroxymethyl)oxolane-3,4-diol"
Skipped 86,826 rows
drug:ado-trastuzumab emtansinedrugbank:interactsWithdrug:Clozapine
drug:ado-trastuzumab emtansinedrugbank:interactsWithdrug:Natalizumab
drug:ado-trastuzumab emtansinedrugbank:interactsWithdrug:Phenytoin
drug:ado-trastuzumab emtansinedrugbank:interactsWithdrug:Pimecrolimus
drug:ado-trastuzumab emtansinedrugbank:interactsWithdrug:Tacrolimus
drug:ado-trastuzumab emtansinedrugbank:interactsWithdrug:Tofacitinib
drug:ado-trastuzumab emtansinerdfs:label"ado-trastuzumab emtansine"
drug:ado-trastuzumab emtansineowl:sameAsdrug:Belimumab
drug:ado-trastuzumab emtansineowl:sameAsdrug:Clozapine
drug:ado-trastuzumab emtansineowl:sameAsdrug:Natalizumab
drug:ado-trastuzumab emtansineowl:sameAsdrug:Phenytoin
drug:ado-trastuzumab emtansineowl:sameAsdrug:Pimecrolimus
drug:ado-trastuzumab emtansineowl:sameAsdrug:Tacrolimus
drug:ado-trastuzumab emtansineowl:sameAsdrug:Tofacitinib
drug:ado-trastuzumab emtansinerdf:typedrugbank:drugs
drug:albumin-interferon alphadrugbank:description"Albumin-interferon alpha (Albuferon) is a novel, long-acting form of interferon alpha. Recombinant interferon alpha is approved for the treatment of hepatitis C, hepatitis B, and a broad range of cancers. Human Genome Sciences modified interferon alpha to improve its pharmacological properties by using the company's proprietary albumin fusion technology. Human Genome Sciences is developing Albuferon as a potential treatment for chronic hepatitis C. "
drug:albumin-interferon alphardfs:label"albumin-interferon alpha"
drug:albumin-interferon alphardf:typedrugbank:drugs
drug:alpha-D-Xylopyranosedrugbank:description" experimental This compound belongs to the hexoses. These are monosaccharides in which the sugar unit is a hexose. Hexoses Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Monosaccharides Oxanes Secondary Alcohols 1,2-Diols Hemiacetals Polyamines oxane hemiacetal polyol 1,2-diol secondary alcohol polyamine ether alcohol logP -2.6 ALOGPS logS 0.91 ALOGPS Water Solubility 1.22e+03 g/l ALOGPS logP -2.3 ChemAxon IUPAC Name (2S,3R,4S,5R)-oxane-2,3,4,5-tetrol ChemAxon Traditional IUPAC Name α-D-xylose ChemAxon Molecular Weight 150.1299 ChemAxon Monoisotopic Weight 150.05282343 ChemAxon SMILES O[C@@H]1CO[C@H](O)[C@H](O)[C@H]1O ChemAxon Molecular Formula C5H10O5 ChemAxon InChI InChI=1S/C5H10O5/c6-2-1-10-5(9)4(8)3(2)7/h2-9H,1H2/t2-,3+,4-,5+/m1/s1 ChemAxon InChIKey InChIKey=SRBFZHDQGSBBOR-LECHCGJUSA-N ChemAxon Polar Surface Area (PSA) 90.15 ChemAxon Refractivity 29.96 ChemAxon Polarizability 13.18 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 11.31 ChemAxon pKa (strongest basic) -3.5 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon ChEBI 28518 KEGG Compound C02205 PDB XYS BE0001329 Chondroitinase-B Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Chondroitinase-B Cleaves the glycosaminoglycan, dermatan sulfate cslB None 8.94 56323.0 Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) GenBank Gene Database U27584 GenBank Protein Database 1002527 UniProtKB Q46079 UniProt Accession CSLB_PEDHD Chondroitin B eliminase Chondroitin B lyase Chondroitin sulfate B lyase Chondroitinase B precursor EC 4.2.2.19 >Chondroitinase B precursor MKMLNKLAGYLLPIMVLLNVAPCLGQVVASNETLYQVVKEVKPGGLVQIADGTYKDVQLI VSNSGKSGLPITIKALNPGKVFFTGDAKVELRGEHLILEGIWFKDGNRAIQAWKSHGPGL VAIYGSYNRITACVFDCFDEANSAYITTSLTEDGKVPQHCRIDHCSFTDKITFDQVINLN NTARAIKDGSVGGPGMYHRVDHCFFSNPQKPGNAGGGIRIGYYRNDIGRCLVDSNLFMRQ DSEAEIITSKSQENVYYGNTYLNCQGTMNFRHGDHQVAINNFYIGNDQRFGYGGMFVWGS RHVIACNYFELSETIKSRGNAALYLNPGAMASEHALAFDMLIANNAFINVNGYAIHFNPL DERRKEYCAANRLKFETPHQLMLKGNLFFKDKPYVYPFFKDDYFIAGKNSWTGNVALGVE KGIPVNISANRSAYKPVKIKDIQPIEGIALDLNALISKGITGKPLSWDEVRPYWLKEMPG TYALTARLSADRAAKFKAVIKRNKEH >1521 bp ATGAAGATGCTGAATAAACTAGCCGGATACTTATTGCCGATCATGGTGCTGCTGAATGTG GCACCATGCTTAGGTCAGGTTGTTGCTTCAAATGAAACTTTATACCAGGTTGTAAAGGAG GTAAAACCCGGTGGTCTGGTACAGATTGCCGATGGGACTTATAAAGATGTTCAGCTGATT GTCAGCAATTCAGGAAAATCTGGTTTGCCCATCACTATTAAAGCCCTGAACCCGGGTAAG GTTTTTTTTACCGGAGATGCTAAAGTAGAGCTGAGGGGCGAGCACCTGATACTGGAAGGC ATCTGGTTTAAAGACGGGAACAGAGCTATTCAGGCATGGAAATCACATGGACCCGGATTG GTGGCTATATATGGTAGCTATAACCGCATTACCGCATGTGTATTTGATTGTTTTGATGAA GCCAATTCTGCTTACATTACTACTTCGCTTACCGAAGACGGAAAGGTACCTCAACATTGC CGCATAGACCATTGCAGTTTTACCGATAAGATCACTTTTGACCAGGTAATTAACCTGAAC AATACAGCCAGAGCTATTAAAGACGGTTCGGTGGGAGGACCGGGGATGTACCATCGTGTT GATCACTGTTTTTTTTCCAATCCGCAAAAACCGGGTAATGCCGGAGGGGGAATCAGGATT GGCTATTACCGTAATGATATAGGCCGTTGTCTGGTAGACTCTAACCTGTTTATGCGTCAG GATTCGGAAGCAGAGATCATCACCAGCAAATCGCAGGAAAATGTTTATTATGGTAATACT TACCTGAATTGCCAGGGCACCATGAACTTTCGTCACGGTGATCATCAGGTGGCCATTAAC AATTTTTATATAGGCAATGACCAGCGATTTGGATACGGGGGAATGTTTGTTTGGGGAAGC AGGCATGTCATAGCCTGTAATTATTTTGAGCTGTCCGAAACCATAAAGTCGAGGGGGAAC GCCGCATTGTATTTAAACCCCGGTGCTATGGCTTCGGAGCATGCTCTTGCTTTCGATATG TTGATAGCCAACAACGCTTTCATCAATGTAAATGGGTATGCCATCCATTTTAATCCATTG GATGAGCGCAGAAAAGAATATTGTGCAGCCAATAGGCTTAAGTTCGAAACCCCGCACCAG CTAATGTTAAAAGGCAATCTTTTCTTTAAGGATAAACCTTATGTTTACCCATTTTTTAAA GATGATTATTTTATAGCAGGGAAAAATAGCTGGACTGGTAATGTAGCCTTAGGTGTGGAA AAGGGAATCCCTGTTAACATTTCGGCCAATAGGTCTGCCTATAAGCCGGTAAAAATTAAA GATATCCAGCCCATAGAAGGAATCGCTCTTGATCTCAATGCGCTGATCAGCAAAGGCATT ACAGGAAAGCCCCTTAGCTGGGATGAAGTAAGGCCCTACTGGTTAAAAGAAATGCCCGGG ACGTATGCTTTAACGGCCAGGCTTTCTGCAGATAGGGCTGCAAAGTTTAAAGCCGTAATT AAAAGAAATAAAGAGCACTGA BE0001416 Chondroitinase-AC Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Chondroitinase-AC Involved in catalytic activity Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4- enuronosyl groups cslA None 9.19 79695.0 Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) GenBank Gene Database U27583 GenBank Protein Database 1002525 UniProtKB Q59288 UniProt Accession CSLA_PEDHD Chondroitin AC eliminase Chondroitin AC lyase Chondroitin sulfate AC lyase Chondroitinase AC precursor EC 4.2.2.5 >Chondroitinase AC precursor MKKLFVTCIVFFSILSPALLIAQQTGTAELIMKRVMLDLKKPLRNMDKVAEKNLNTLQPD GSWKDVPYKDDAMTNWLPNNHLLQLETIIQAYIEKDSHYYGDDKVFDQISKAFKYWYDSD PKSRNWWHNEIATPQALGEMLILMRYGKKPLDEALVHKLTERMKRGEPEKKTGANKTDIA LHYFYRALLTSDEALLSFAVKELFYPVQFVHYEEGLQYDYSYLQHGPQLQISSYGAVFIT GVLKLANYVRDTPYALSTEKLAIFSKYYRDSYLKAIRGSYMDFNVEGRGVSRPDILNKKA EKKRLLVAKMIDLKHTEEWADAIARTDSTVAAGYKIEPYHHQFWNGDYVQHLRPAYSFNV RMVSKRTRRSESGNKENLLGRYLSDGATNIQLRGPEYYNIMPVWEWDKIPGITSRDYLTD RPLTKLWGEQGSNDFAGGVSDGVYGASAYALDYDSLQAKKAWFFFDKEIVCLGAGINSNA PENITTTLNQSWLNGPVISTAGKTGRGKITTFKAQGQFWLLHDAIGYYFPEGANLSLSTQ SQKGNWFHINNSHSKDEVSGDVFKLWINHGARPENAQYAYIVLPGINKPEEIKKYNGTAP KVLANTNQLQAVYHQQLDMVQAIFYTAGKLSVAGIEIETDKPCAVLIKHINGKQVIWAAD PLQKEKTAVLSIRDLKTGKTNRVKIDFPQQEFAGATVELK >2103 bp ATGAAGAAATTATTTGTAACCTGTATAGTCTTTTTCTCTATTTTAAGTCCTGCTCTGCTT ATTGCACAGCAGACCGGTACTGCAGAACTGATTATGAAGCGGGTGATGCTGGACCTTAAA AAGCCTTTGCGCAATATGGATAAGGTGGCGGAAAAGAACCTGAATACGCTGCAGCCTGAC GGTAGCTGGAAGGATGTGCCTTATAAAGATGATGCCATGACCAATTGGTTGCCAAACAAC CACCTGCTACAATTGGAAACTATTATACAGGCTTATATTGAAAAAGATAGTCACTATTAT GGCGACGATAAAGTGTTTGACCAGATTTCCAAAGCTTTTAAGTATTGGTATGACAGCGAC CCGAAAAGCCGCAACTGGTGGCACAATGAAATTGCCACTCCGCAGGCCCTTGGTGAAATG CTGATCCTGATGCGTTACGGTAAAAAGCCGCTTGATGAAGCATTGGTGCATAAATTGACC GAAAGAATGAAGCGGGGCGAACCGGAGAAGAAAACGGGGGCCAACAAAACAGATATCGCC CTGCATTACTTTTATCGTGCTTTGTTAACGTCTGATGAGGCTTTGCTTTCCTTCGCCGTA AAAGAATTGTTTTATCCCGTACAGTTTGTACACTATGAGGAAGGCCTGCAATACGATTAT TCCTACCTGCAGCACGGTCCGCAATTACAGATATCGAGCTACGGTGCCGTATTTATTACC GGGGTACTGAAACTTGCCAATTACGTTAGGGATACCCCTTATGCTTTAAGTACCGAGAAA CTGGCTATATTTTCAAAGTATTACCGCGACAGTTATCTGAAAGCTATCCGTGGAAGTTAT ATGGATTTTAACGTAGAAGGCCGCGGAGTAAGCCGGCCAGACATTCTAAATAAAAAGGCA GAAAAAAAGAGGTTGCTGGTGGCGAAGATGATCGATCTTAAGCATACTGAAGAATGGGCT GATGCGATAGCCAGGACAGATAGCACAGTTGCGGCCGGCTATAAGATTGAGCCCTATCAC CATCAGTTCTGGAATGGTGATTATGTGCAACATTTAAGACCTGCCTATTCTTTTAATGTT CGTATGGTGAGTAAGCGGACCCGACGCAGTGAATCCGGCAATAAAGAAAACCTGCTGGGC AGGTATTTATCTGATGGGGCTACTAACATACAATTGCGCGGACCAGAATACTATAACATT ATGCCGGTATGGGAATGGGACAAGATTCCTGGCATAACCAGCCGTGATTATTTAACCGAC AGACCTTTGACGAAGCTTTGGGGAGAGCAGGGGAGCAATGACTTTGCAGGAGGGGTGTCT GATGGTGTATACGGGGCCAGTGCCTACGCATTGGATTACGATAGCTTACAGGCAAAGAAA GCCTGGTTCTTTTTTGACAAAGAGATTGTATGTCTTGGTGCCGGTATCAACAGCAATGCC CCTGAAAACATTACCACTACCCTTAACCAGAGCTGGTTAAATGGCCCGGTTATAAGTACT GCAGGTAAAACCGGCCGGGGTAAAATAACAACGTTTAAAGCACAGGGACAGTTCTGGTTG TTGCACGATGCGATTGGTTATTACTTTCCTGAAGGGGCCAACCTTAGTCTGAGTACCCAG TCGCAAAAAGGCAATTGGTTCCACATCAACAATTCACATTCAAAAGATGAAGTTTCTGGT GATGTATTTAAGCTTTGGATCAACCATGGTGCCAGGCCAGAAAATGCGCAGTATGCTTAT ATCGTTTTGCCGGGAATAAACAAGCCGGAAGAAATTAAAAAATATAATGGAACGGCACCG AAAGTCCTTGCCAATACCAACCAGCTGCAGGCAGTTTATCATCAGCAGTTAGATATGGTA CAGGCTATCTTCTATACAGCTGGAAAATTAAGCGTAGCGGGCATAGAAATTGAAACAGAT AAGCCATGTGCAGTGCTGATCAAGCACATCAATGGCAAGCAGGTAATTTGGGCTGCCGAT CCATTGCAAAAAGAAAAGACTGCAGTGTTGAGCATCAGGGATTTAAAAACAGGAAAAACA AATCGGGTAAAAATTGATTTTCCGCAACAGGAATTTGCAGGTGCAACGGTTGAACTGAAA TAG PF02278 Lyase_8 PF02884 Lyase_8_C PF08124 Lyase_8_N component extracellular region function carbon-oxygen lyase activity function carbon-oxygen lyase activity, acting on polysaccharides function catalytic activity function lyase activity BE0001339 Exoglucanase/xylanase Cellulomonas fimi # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Exoglucanase/xylanase Carbohydrate transport and metabolism The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes:(1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the nonreducing end of the cellulose polymer chain; (3) Beta-1,4- glucosidases which hydrolyze the cellobiose and other short cello- oligosaccharides to glucose cex Cytoplasmic None 6.62 51291.0 Cellulomonas fimi GenBank Gene Database M15824 GenBank Protein Database 144425 UniProtKB P07986 UniProt Accession GUX_CELFI 1,4-beta-cellobiohydrolase Beta-1,4- glycanase CEX EC 3.2.1.8 EC 3.2.1.91 Endo-1,4-beta-xylanase B Exocellobiohydrolase Exoglucanase/xylanase >Exoglucanase/xylanase precursor [Includes: Exoglucanase MPRTTPAPGHPARGARTALRTTRRRAATLVVGATVVLPAQAATTLKEAADGAGRDFGFAL DPNRLSEAQYKAIADSEFNLVVAENAMKWDATEPSQNSFSFGAGDRVASYAADTGKELYG HTLVWHSQLPDWAKNLNGSAFESAMVNHVTKVADHFEGKVASWDVVNEAFADGDGPPQDS AFQQKLGNGYIETAFRAARAADPTAKLCINDYNVEGINAKSNSLYDLVKDFKARGVPLDC VGFQSHLIVGQVPGDFRQNLQRFADLGVDVRITELDIRMRTPSDATKLATQAADYKKVVQ ACMQVTRCQGVTVWGITDKYSWVPDVFPGEGAALVWDASYAKKPAYAAVMEAFGASPTPT PTTPTPTPTTPTPTPTSGPAGCQVLWGVNQWNTGFTANVTVKNTSSAPVDGWTLTFSFPS GQQVTQAWSSTVTQSGSAVTVRNAPWNGSIPAGGTAQFGFNGSHTGTNAAPTAFSLNGTP CTVG >1455 bp ATGCCTAGGACCACGCCCGCACCCGGCCACCCGGCCCGCGGCGCCCGCACCGCTCTGCGC ACGACGCGCCGCCGCGCGGCGACGCTCGTCGTCGGCGCCACGGTCGTGCTGCCCGCCCAG GCCGCGACCACGCTCAAGGAGGCCGCCGACGGCGCCGGCCGGGACTTCGGCTTCGCGCTC GACCCCAACCGGCTCTCGGAGGCGCAGTACAAGGCGATCGCCGACAGCGAGTTCAACCTC GTCGTCGCCGAGAACGCGATGAAGTGGGACGCCACCGAGCCCTCGCAGAACAGCTTCTCC TTCGGCGCGGGCGACCGCGTCGCGAGCTACGCCGCCGACACCGGCAAGGAGCTGTACGGC CACACGCTCGTCTGGCACTCGCAGCTGCCCGACTGGGCGAAGAACCTCAACGGCTCCGCG TTCGAGAGCGCGATGGTCAACCACGTGACGAAGGTCGCCGACCACTTCGAGGGCAAGGTC GCGTCGTGGGACGTCGTCAACGAGGCGTTCGCCGACGGCGACGGCCCGCCGCAGGACTCG GCGTTCCAGCAGAAGCTCGGCAACGGCTACATCGAGACCGCGTTCCGGGCGGCACGTGCG GCGGACCCGACCGCCAAGCTGTGCATCAACGACTACAACGTCGAGGGCATCAACGCGAAG AGCAACTCGCTCTACGACCTCGTCAAGGACTTCAAGGCGCGCGGCGTCCCGCTCGACTGC GTCGGGTTCCAGTCGCACCTCATCGTCGGCCAGGTGCCGGGCGACTTCCGGCAGAACCTG CAGCGGTTCGCGGACCTGGGCGTGGACGTGCGCATCACCGAGCTCGACATCCGCATGCGG ACGCCCTCCGACGCGACCAAGCTCGCGACCCAGGCGGCCGACTACAAGAAGGTCGTGCAG GCCTGCATGCAGGTGACCCGCTGCCAGGGCGTGACCGTCTGGGGCATCACCGACAAGTAC TCGTGGGTGCCGGACGTCTTCCCGGGCGAGGGGGCCGCGCTGGTGTGGGACGCGAGCTAC GCCAAGAAGCCGGCCTACGCCGCCGTGATGGAGGCCTTCGGCGCGAGCCCGACGCCGACG CCCACCACGCCGACCCCGACGCCCACGACGCCGACGCCGACCCCGACGTCCGGTCCGGCC GGGTGCCAGGTGCTGTGGGGCGTCAACCAGTGGAACACCGGCTTCACCGCGAACGTCACC GTGAAGAACACGTCCTCCGCTCCGGTCGACGGCTGGACGCTCACGTTCAGCTTCCCGTCC GGCCAGCAGGTCACCCAGGCGTGGAGCTCGACGGTCACGCAGTCCGGCTCGGCCGTGACG GTCCGCAACGCCCCGTGGAACGGCTCGATCCCGGCGGGCGGCACCGCGCAGTTCGGCTTC AACGGCTCGCACACGGGCACCAACGCCGCGCCGACGGCGTTCTCGCTCAACGGCACGCCC TGCACGGTCGGCTGA PF00553 CBM_2 PF00331 Glyco_hydro_10 function catalytic activity function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function pattern binding function polysaccharide binding function binding process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process BE0002844 Aldose 1-epimerase Lactococcus lactis unknown Aldose 1-epimerase Involved in isomerase activity galM None 5.01 37611.0 Lactococcus lactis GenBank Gene Database U60828 UniProtKB Q9ZB17 UniProt Accession Q9ZB17_9LACT >Aldose 1-epimerase MEIKIRDFGLGSDLISLTNKAGVTISFTNLGARIVDWQKDGKHLILGFDSAKEYLEKDAY PGATVGPTAGRIKDGLVKISGKDYILNQNEGPQTLHGGEESIHTKLWTYEVTDLGAEVQV KFSLVTNDGTNGYPGKIEMSVTHSFDDYNKWKIHYEAISDKDTVFNPTGHVYFNLNGDAS ESVENHGLRLAASRFVPLKDQTEIVRGDIVDIKNTDLDFRQEKQLSNAFNSNMEQVQLVK GIDHPFLLDQLGLDKEQARLTLDDTSISVFTDQPSIVIFTANFGDLGTLYHEKKQVHHGG ITFECQVSPGSEQIPELGDISLKAGEKYQATTIYSLHTK >1020 bp ATGGAAATTAAAATAAGAGATTTTGGCTTAGGAAGTGACTTAATTAGTCTAACCAATAAA GCAGGTGTCACAATTTCTTTTACAAATCTGGGCGCTCGGATTGTTGACTGGCAAAAAGAT GGAAAGCATCTGATTCTAGGCTTTGATTCAGCTAAAGAATATTTAGAAAAAGATGCCTAT CCTGGTGCAACAGTTGGACCTACAGCAGGAAGAATTAAGGATGGTTTGGTCAAAATTTCT GGAAAAGATTATATCTTAAATCAAAATGAAGGCCCTCAAACCTTACATGGTGGGGAAGAA AGTATTCATACTAAACTTTGGACATATGAAGTTACCGATTTAGGAGCTGAAGTTCAAGTC AAATTTTCCTTAGTTACTAATGACGGAACAAATGGTTATCCTGGTAAAATAGAAATGTCA GTAACTCATTCTTTTGATGATTACAATAAGTGGAAAATTCATTATGAGGCCATTTCTGAT AAAGACACTGTGTTTAATCCAACTGGGCATGTCTATTTTAATTTGAATGGTGATGCTAGT GAATCTGTTGAAAATCATGGACTTCGACTGGCCGCTTCAAGATTTGTTCCTTTAAAAGAC CAAACAGAAATTGTTCGTGGTGATATCGTTGATATAAAAAATACAGACTTGGATTTCCGT CAGGAAAAACAATTATCAAATGCCTTCAATTCTAATATGGAACAAGTTCAATTAGTTAAA GGAATTGACCATCCTTTCTTGTTAGACCAGTTAGGACTTGATAAAGAACAAGCTCGTTTA ACGCTTGATGATACTTCAATTTCAGTCTTTACCGACCAACCAAGTATTGTGATATTTACA GCAAATTTTGGTGATTTAGGAACTCTTTATCATGAGAAAAAGCAAGTGCACCATGGTGGA ATTACTTTTGAATGTCAAGTATCACCTGGGTCTGAGCAAATTCCAGAGCTTGGAGATATC AGCCTAAAAGCGGGAGAAAAATATCAAGCAACCACAATTTACAGCTTGCATACAAAATAA PF01263 Aldose_epim function racemase and epimerase activity function racemase and epimerase activity, acting on carbohydrates and derivatives function aldose 1-epimerase activity function catalytic activity function isomerase activity process monosaccharide metabolism process hexose metabolism process galactose metabolism process physiological process process metabolism process cellular metabolism process alcohol metabolism BE0003068 Endo-beta-1,4-xylanase Cellvibrio japonicus unknown Endo-beta-1,4-xylanase Involved in hydrolase activity, hydrolyzing O-glycosyl compounds Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans Cytoplasmic None 4.48 64884.0 Cellvibrio japonicus GenBank Gene Database Z48928 UniProtKB Q59675 UniProt Accession Q59675_9GAMM EC 3.2.1.8 Endo-beta-1,4-xylanase precursor >Endo-beta-1,4-xylanase MKKIQQLLMLSLISSTLIACGGGGGGGSTPTTSSSPQSSSPASTPSSASSSSIISSSSLS SSLSSSSLSSSSLSSSSASSVSSSSVAASEGNVVIEVDMANGWRGNASGSTSHSGITYSA DGVTFAALGDGVGAVFDIARPTTLEDAVIAMVVNVSAEFKASEANLQIFAQLKEDWSKGE WDCLAASSELTADTDLTLTCTIDEDDDKFNQTARDVQVGIQAKGTPAGTITIKSVTITLA QEAYSANVDHLRDLAPSDFPIGVAVSNTDSATYNLLTNSREQAVVKKHFNHLTAGNIMKM SYMQPTEGNFNFTNADAFVDWATENNMTVHGHALVWHSDYQVPNFMKNWAGSAEDFLAAL DTHITTIVDHYEAKGNLVSWDVVNEAIDDNSPANFRTTDSAFYVKSGNSSVYIERAFQTA RAADPAVILYYNDYNIEQNNAKTTKMVDMVKDFQARSIPIDGVGFQMHVCMNYPSIANIS AAMKKVVDLGLLVKITELDVAVNQPHCDAYPANKINPLTEAAQLAQKKRYCDVVKAYLDT VPVNQRGGISVWGTTDANTWLDGLYREQFEDEKISWPLLFDNNYNDKPALRGFADALIGT QCTNTH >1821 bp ATGAAAAAGATCCAGCAACTCCTCATGCTCTCCCTGATTAGCTCAACACTAATTGCCTGT GGCGGCGGTGGAGGGGGCGGTTCAACACCAACCACCAGCAGCTCACCCCAATCCTCTAGT CCAGCATCGACGCCATCCAGTGCTTCATCCTCATCGATCATATCCTCCTCATCGCTATCA TCATCGCTGTCTTCCTCATCACTATCCTCGTCATCGCTGTCTTCTTCATCGGCGAGCAGT GTTAGCAGCTCCAGTGTCGCTGCCAGCGAGGGCAATGTTGTTATAGAGGTGGACATGGCA AATGGCTGGAGAGGCAACGCATCAGGCAGTACCAGCCATTCCGGTATTACCTACAGTGCC GATGGCGTTACCTTTGCCGCACTGGGTGATGGCGTGGGCGCTGTTTTTGATATTGCCCGA CCAACCACACTGGAAGATGCTGTGATAGCAATGGTTGTTAATGTCAGCGCTGAATTTAAG GCCAGTGAAGCCAACTTGCAGATATTTGCCCAGTTAAAAGAAGACTGGTCAAAGGGCGAA TGGGATTGTCTGGCGGCCAGCAGCGAACTCACTGCGGATACTGACCTAACCCTGACCTGC ACCATTGATGAAGACGACGATAAATTCAACCAAACGGCGCGCGATGTACAAGTCGGTATC CAGGCCAAGGGAACACCCGCCGGAACTATCACCATTAAAAGCGTCACCATTACACTCGCA CAGGAAGCCTATTCAGCCAATGTCGATCACCTGCGCGACCTGGCCCCCAGCGATTTCCCC ATTGGCGTCGCCGTGTCCAATACCGACTCCGCCACTTACAACCTGCTCACCAACAGCAGA GAGCAGGCTGTGGTTAAAAAGCACTTCAATCATTTAACTGCCGGTAACATCATGAAGATG AGTTACATGCAACCTACCGAGGGCAATTTTAACTTCACCAACGCCGACGCCTTTGTGGAT TGGGCCACTGAAAATAATATGACGGTGCACGGCCACGCCCTGGTATGGCATTCCGATTAC CAGGTTCCCAACTTTATGAAAAACTGGGCAGGCAGTGCAGAAGACTTTTTAGCGGCCTTG GACACACATATCACCACCATTGTCGATCACTACGAAGCCAAGGGTAACCTCGTCAGTTGG GACGTCGTTAACGAAGCCATCGACGACAACAGTCCGGCAAACTTCCGCACGACGGATTCT GCGTTTTATGTGAAGAGCGGAAACAGCTCTGTCTATATTGAGCGCGCCTTCCAGACCGCG CGCGCGGCAGATCCCGCTGTGATCCTCTACTACAACGACTACAACATTGAGCAGAACAAT GCCAAGACCACCAAAATGGTCGATATGGTCAAGGACTTCCAGGCGCGCAGTATCCCGATT GACGGTGTGGGCTTCCAGATGCATGTCTGTATGAACTATCCATCCATCGCCAACATTTCT GCCGCGATGAAGAAAGTGGTCGACCTTGGCTTGCTGGTAAAAATTACCGAACTGGATGTT GCCGTCAACCAGCCCCATTGCGATGCGTATCCGGCCAACAAAATCAATCCGCTGACCGAA GCGGCGCAATTGGCCCAGAAAAAACGCTACTGCGACGTAGTGAAGGCCTATCTGGATACA GTCCCGGTGAATCAGCGCGGCGGTATCAGCGTCTGGGGAACTACCGATGCCAACACCTGG CTTGATGGCCTGTACAGAGAACAGTTTGAGGATGAAAAAATTTCCTGGCCCTTGCTGTTC GACAACAACTACAACGACAAACCTGCACTGCGCGGTTTTGCCGATGCGTTAATCGGTACG CAATGTACTAATACACATTGA PF00331 Glyco_hydro_10 PF03426 CBM_15 function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity function hydrolase activity process physiological process process metabolism process macromolecule metabolism process carbohydrate metabolism BE0003069 Reducing end xylose-releasing exo-oligoxylanase Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) unknown Reducing end xylose-releasing exo-oligoxylanase Involved in catalytic activity BH2105 Cytoplasmic None 4.45 45010.0 Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) GenBank Gene Database BA000004 UniProtKB Q9KB30 UniProt Accession REOX_BACHD >Xylanase Y MKKTTEGAFYTREYRNLFKEFGYSEAEIQERVKDTWEQLFGDNPETKIYYEVGDDLGYLL DTGNLDVRTEGMSYGMMMAVQMDRKDIFDRIWNWTMKNMYMTEGVHAGYFAWSCQPDGTK NSWGPAPDGEEYFALALFFASHRWGDGDEQPFNYSEQARKLLHTCVHNGEGGPGHPMWNR DNKLIKFIPEVEFSDPSYHLPHFYELFSLWANEEDRVFWKEAAEASREYLKIACHPETGL APEYAYYDGTPNDEKGYGHFFSDSYRVAANIGLDAEWFGGSEWSAEEINKIQAFFADKEP EDYRRYKIDGEPFEEKSLHPVGLIATNAMGSLASVDGPYAKANVDLFWNTPVRTGNRRYY DNCLYLFAMLALSGNFKIWFPEGQEEEH >1167 bp CTAGTGTTCCTCTTCTTGGCCCTCAGGAAACCAAATTTTAAAATTGCCGCTTAGTGCGAG CATCGCAAACAAATATAAACAATTATCGTAATAACGGCGGTTGCCGGTGCGAACCGGTGT GTTCCAGAACAAATCCACATTAGCTTTAGCGTATGGTCCATCAACAGAGGCTAAAGAACC CATCGCGTTAGTAGCAATCAGTCCGACAGGGTGCAATGATTTCTCTTCGAACGGTTCCCC GTCTATTTTATAGCGGCGGTAGTCTTCAGGCTCCTTATCTGCAAAAAACGCCTGGATCTT ATTTATCTCTTCTGCCGACCACTCGCTTCCTCCGAACCATTCAGCGTCAAGTCCAATATT AGCAGCCACACGATAAGAATCGCTAAAAAAGTGGCCGTATCCCTTTTCATCATTTGGCGT TCCATCATAGTAAGCATACTCAGGCGCAAGTCCTGTTTCAGGATGGCAAGCTATTTTCAA ATACTCCCGGCTCGCTTCAGCAGCCTCTTTCCAGAAGACGCGGTCCTCTTCGTTTGCCCA TAAACTGAACAGTTCATAAAAATGGGGGAGATGATAAGAGGGATCACTGAACTCCACTTC AGGTATGAATTTAATGAGCTTATTATCCCGGTTCCACATTGGATGGCCAGGACCACCTTC ACCATTGTGCACGCAAGTATGAAGTAGCTTACGAGCTTGTTCGCTGTAATTAAACGGCTG TTCATCACCATCGCCCCAGCGGTGCGAAGCAAAAAATAATGCAAGGGCAAAATATTCCTC TCCGTCCGGAGCTGGGCCCCAGGAGTTTTTAGTGCCATCAGGCTGGCATGACCAAGCGAA GTAGCCCGCGTGCACGCCTTCCGTCATATACATATTCTTCATCGTCCAATTCCAGATCCG GTCGAAAATATCCTTTCTGTCCATTTGAACAGCCATCATCATTCCGTAGGACATTCCTTC AGTCCGCACATCGAGGTTTCCCGTATCGAGGAGATAACCTAGATCATCGCCCACTTCATA ATAAATTTTCGTTTCTGGGTTATCGCCAAAAAGCTGTTCCCATGTGTCCTTAACTCGTTC TTGGATTTCCGCTTCCGAATACCCGAATTCCTTGAAAAGATTTCGGTACTCCCTCGTATA AAATGCACCTTCTGTCGTTTTCTTCAT PF01270 Glyco_hydro_8 function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process BE0003070 Endo-1,4-beta-xylanase Geobacillus stearothermophilus unknown Endo-1,4-beta-xylanase Involved in hydrolase activity, hydrolyzing O-glycosyl compounds Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans Secreted protein None 8.81 46764.0 Geobacillus stearothermophilus GenBank Gene Database Z29080 UniProtKB P40943 UniProt Accession XYN1_GEOSE 1,4-beta-D- xylan xylanohydrolase EC 3.2.1.8 Endo-1,4-beta-xylanase precursor Xylanase >Endo-1,4-beta-xylanase MRNVVRKPLTIGLALTLLLPMGMTATSAKNADSYAKKPHISALNAPQLDQRYKNEFTIGA AVEPYQLQNEKDVQMLKRHFNSIVAENVMKPISIQPEEGKFNFEQADRIVKFAKANGMDI RFHTLVWHSQVPQWFFLDKEGKPMVNETDPVKREQNKQLLLKRLETHIKTIVERYKDDIK YWDVVNEVVGDDGKLRNSPWYQIAGIDYIKVAFQAARKYGGDNIKLYMNDYNTEVEPKRT ALYNLVKQLKEEGVPIDGIGHQSHIQIGWPSEAEIEKTINMFAALGLDNQITELDVSMYG WPPRAYPTYDAIPKQKFLDQAARYDRLFKLYEKLSDKISNVTFWGIADNHTWLDSRADVY YDANGNVVVDPNAPYAKVEKGKGKDAPFVFGPDYKVKPAYWAIIDHK >1224 bp ATGCGGAACGTCGTGCGTAAACCATTGACAATCGGACTCGCTTTAACACTATTATTGCCC ATGGGAATGACGGCAACATCAGCGAAGAATGCAGATTCCTATGCGAAAAAACCTCACATC AGCGCATTGAATGCCCCACAATTGGATCAACGCTACAAAAACGAGTTCACGATTGGTGCG GCAGTAGAACCTTATCAACTACAAAATGAAAAAGACGTACAAATGCTAAAGCGCCACTTC AACAGCATTGTTGCCGAGAACGTAATGAAACCGATCAGCATTCAACCTGAGGAAGGAAAA TTCAATTTTGAACAAGCGGATCGAATTGTGAAGTTCGCTAAGGCAAATGGCATGGATATT CGCTTCCATACACTCGTTTGGCACAGCCAAGTACCTCAATGGTTCTTTCTTGACAAGGAA GGTAAGCCAATGGTTAATGAAACAGATCCAGTGAAACGTGAACAAAATAAACAACTGCTG TTAAAACGACTTGAAACTCATATTAAAACGATCGTCGAGCGGTACAAAGATGACATTAAG TACTGGGACGTTGTAAATGAGGTTGTGGGGGACGACGGAAAACTGCGCAACTCTCCATGG TATCAAATCGCCGGCATCGATTATATTAAAGTGGCATTCCAAGCAGCTAGAAAATATGGC GGAGACAACATTAAGCTTTACATGAATGATTACAATACAGAAGTCGAACCGAAGCGAACC GCTCTTTACAATTTAGTCAAACAACTGAAAGAAGAGGGTGTTCCGATCGACGGCATCGGC CATCAATCCCACATCCAAATCGGCTGGCCTTCTGAAGCAGAAATCGAGAAAACGATTAAC ATGTTCGCCGCTCTCGGTTTAGACAACCAAATCACTGAGCTTGATGTGAGCATGTACGGT TGGCCGCCGCGCGCTTACCCGACGTATGACGCCATTCCAAAACAAAAGTTTTTGGATCAG GCAGCGCGCTATGATCGTTTGTTCAAACTGTATGAAAAGTTGAGCGATAAAATTAGCAAC GTCACCTTCTGGGGCATCGCCGACAATCATACGTGGCTCGACAGCCGTGCGGATGTGTAC TATGACGCCAACGGGAATGTTGTGGTTGACCCGAACGCTCCGTACGCAAAAGTGGAAAAA GGGAAAGGAAAAGATGCGCCGTTCGTTTTTGGACCGGATTACAAAGTCAAACCCGCATAT TGGGCTATTATCGACCACAAATAG PF00331 Glyco_hydro_10 function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity function hydrolase activity process carbohydrate metabolism process physiological process process metabolism process macromolecule metabolism BE0002940 Endo-1,4-beta-xylanase Bacillus agaradhaerens unknown Endo-1,4-beta-xylanase Involved in hydrolase activity, hydrolyzing O-glycosyl compounds Cytoplasmic None 9.12 23308.0 Bacillus agaradhaerens UniProtKB Q7SIE2 UniProt Accession Q7SIE2_BACAG >Glycoside hydrolase QIVTDNSIGNHDGYDYEFWKDSGGSGTMILNHGGTFSAQWNNVNNILFRKGKKFNETQTH QQVGNMSINYGANFQPNGNAYLCVYGWTVDPLVAYYIVDSWGNWRPPGATPKGTITVDGG TYDIYETLRVNQPSIKGIATFKQYWSVRRSKRTSGTISVSNHFRAWENLGMNMGKMYEVA LTVEGYQSSGSANVYSNTLRINGNPLSTI PF00457 Glyco_hydro_11 function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process BE0002739 Endo-1,4-beta-xylanase A Clostridium stercorarium unknown Endo-1,4-beta-xylanase A Involved in carbohydrate binding Endoxylanase that degrades arabinoxylan and glucuronoxylan to xylobiose and xylotriose (in vitro) xynA Secreted protein None 4.88 70151.0 Clostridium stercorarium GenBank Gene Database AJ508403 UniProtKB Q8GJ44 UniProt Accession XYNA1_CLOSR 1,4-beta-D-xylan xylanohydrolase A EC 3.2.1.8 Endo-1,4-beta-xylanase A precursor Xylanase 11A Xyn11A >Endo-1,4-beta-xylanase A MKRKVKKMAAMATSIIMAIMIILHSIPVLAGRIIYDNETGTHGGYDYELWKDYGNTIMEL NDGGTFSCQWSNIGNALFRKGRKFNSDKTYQELGDIVVEYGCDYNPNGNSYLCVYGWTRN PLVEYYIVESWGSWRPPGATPKGTITVDGGTYEIYETTRVNQPSIDGTATFQQYWSVRTS KRTSGTISVTEHFKQWERMGMRMGKMYEVALTVEGYQSSGYANVYKNEIRIGANPTPAPS QSPIRRDAFSIIEAEEYNSTNSSTLQVIGTPNNGRGIGYIENGNTVTYSNIDFGSGATGF SATVATEVNTSIQIRSDSPTGTLLGTLYVSSTGSWNTYQTVSTNISKITGVHDIVLVFSG PVNVDNFIFSRSSPVPAPGDNTRDAYSIIQAEDYDSSYGPNLQIFSLPGGGSAIGYIENG YSTTYNNVNFANGLSSITARVATQISTSIQVRAGGATGTLLGTIYVPSTNSWDSYQNVTA NLSNITGVHDITLVFSGPVNVDYFVFTPANVNSGPTSPVGGTRSAFSNIQAEDYDSSYGP NLQIFSLPGGGSAIGYIENGYSTTYKNIDFGDGATSVTARVATQNATTIQVRLGSPSGTL LGTIYVGSTGSFDTYRDVSATISNTAGVKDIVLVFSGPVNVDWFVFSKSGT >1965 bp ATGAAGCGTAAGGTTAAGAAGATGGCAGCTATGGCAACGAGTATAATTATGGCTATCATG ATCATCCTACATAGTATACCAGTACTCGCCGGGCGAATAATTTACGACAATGAGACAGGC ACACATGGAGGCTACGACTATGAGCTCTGGAAAGACTACGGAAATACGATTATGGAACTT AACGACGGTGGTACTTTTAGTTGTCAATGGAGTAATATCGGTAATGCACTATTTAGAAAA GGGAGAAAATTTAATTCCGACAAAACCTATCAAGAATTAGGAGATATAGTAGTTGAATAT GGCTGTGATTACAATCCAAACGGAAATTCCTATTTGTGTGTTTACGGTTGGACAAGAAAT CCACTGGTTGAATATTACATTGTAGAAAGCTGGGGCAGCTGGCGTCCACCTGGAGCAACA CCCAAAGGAACCATCACAGTGGATGGCGGTACTTATGAAATATATGAAACTACCCGGGTA AATCAGCCTTCCATCGATGGAACTGCGACATTCCAACAATATTGGAGTGTTCGTACATCC AAGAGAACAAGCGGAACAATATCTGTCACTGAACATTTTAAACAGTGGGAAAGAATGGGC ATGCGAATGGGTAAGATGTATGAAGTTGCTCTTACCGTTGAAGGTTATCAGAGCAGTGGG TACGCTAATGTATACAAGAATGAAATCAGAATAGGTGCAAATCCAACTCCTGCCCCATCT CAAAGCCCAATTAGAAGAGATGCATTTTCAATAATCGAAGCGGAAGAATATAACAGCACA AATTCCTCCACTTTACAAGTGATTGGAACGCCAAATAATGGCAGAGGAATTGGTTATATT GAAAATGGTAATACCGTAACTTACAGCAATATAGATTTTGGTAGTGGTGCAACAGGGTTC TCTGCAACTGTTGCAACGGAGGTTAATACCTCAATTCAAATCCGTTCTGACAGTCCTACC GGAACTCTACTTGGTACCTTATATGTAAGTTCTACCGGCAGCTGGAATACATATCAAACC GTATCTACAAACATCAGCAAAATTACCGGCGTTCATGATATTGTATTGGTATTCTCAGGT CCAGTCAATGTGGACAACTTCATATTTAGCAGAAGTTCACCAGTGCCTGCACCTGGTGAT AACACAAGAGACGCATATTCTATCATTCAGGCCGAGGATTATGACAGCAGTTATGGCCCC AACCTTCAAATCTTTAGCTTACCAGGCGGTGGCAGCGCCATTGGCTATATTGAAAATGGT TATTCCACTACCTATAATAACGTTAATTTCGCCAACGGCTTAAGTTCTATAACAGCAAGA GTTGCCACTCAGATCTCAACTTCCATTCAGGTGAGAGCAGGAGGAGCAACCGGTACTTTA CTTGGTACAATATATGTTCCTTCGACAAATAGTTGGGATTCTTATCAGAATGTAACTGCC AACCTTAGCAATATTACAGGTGTGCATGATATTACCCTTGTCTTTTCAGGACCAGTGAAT GTGGACTACTTCGTATTTACACCAGCAAATGTAAATTCAGGGCCTACCTCCCCTGTCGGA GGTACAAGAAGTGCATTTTCCAATATTCAAGCCGAAGATTATGACAGCAGTTATGGTCCC AACCTTCAAATCTTTAGCTTACCAGGTGGTGGCAGCGCCATTGGCTATATTGAAAATGGT TATTCCACTACCTATAAAAATATTGATTTTGGTGACGGCGCAACGTCCGTAACAGCAAGA GTAGCTACCCAGAATGCTACTACCATTCAGGTAAGATTGGGAAGTCCATCGGGTACATTA CTTGGAACAATTTACGTGGGGTCCACAGGAAGCTTTGATACTTATAGGGATGTATCCGCT ACCATTAGTAATACTGCGGGTGTAAAAGATATTGTTCTTGTATTCTCAGGTCCTGTTAAT GTTGACTGGTTTGTATTCTCAAAATTCAGGAACTTAAGGGTATAG PF03422 CBM_6 PF00457 Glyco_hydro_11 function catalytic activity function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function carbohydrate binding function binding process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process BE0002766 Endo-1,4-beta-xylanase A Streptomyces lividans unknown Endo-1,4-beta-xylanase A Involved in hydrolase activity, hydrolyzing O-glycosyl compounds Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources xlnA Secreted protein None 6.61 51163.0 Streptomyces lividans GenBank Gene Database M64551 UniProtKB P26514 UniProt Accession XYNA_STRLI 1,4- beta-D-xylan xylanohydrolase A EC 3.2.1.8 Endo-1,4-beta-xylanase A precursor Xylanase A >Endo-1,4-beta-xylanase A MGSYALPRSGVRRSIRVLLLALVVGVLGTATALIAPPGAHAAESTLGAAAAQSGRYFGTA IASGRLSDSTYTSIAGREFNMVTAENEMKIDATEPQRGQFNFSSADRVYNWAVQNGKQVR GHTLAWHSQQPGWMQSLSGSALRQAMIDHINGVMAHYKGKIVQWDVVNEAFADGSSGARR DSNLQRSGNDWIEVAFRTARAADPSAKLCYNDYNVENWTWAKTQAMYNMVRDFKQRGVPI DCVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGAPASTYANVTNDCLAVSR CLGITVWGVRDSDSWRSEQTPLLFNNDGSKKAAYTAVLDALNGGDSSEPPADGGQIKGVG SGRCLDVPDASTSDGTQLQLWDCHSGTNQQWAATDAGELRVYGDKCLDAAGTSNGSKVQI YSCWGGDNQKWRLNSDGSVVGVQSGLCLDAVGNGTANGTLIQLYTCSNGSNQRWTRT >1434 bp ATGGGCTCCTACGCCCTTCCCAGATCAGGTGTCCGCAGGAGCATTCGCGTCCTGCTGCTG GCGCTGGTCGTCGGCGTACTCGGCACGGCCACCGCACTGATCGCGCCGCCGGGGGCACAC GCCGCCGAGAGCACGCTCGGCGCCGCGGCGGCGCAGAGCGGCCGCTACTTCGGCACCGCC ATCGCCTCGGGCAGGCTGAGCGACTCGACGTACACGTCGATCGCGGGCCGTGAGTTCAAC ATGGTGACGGCCGAGAACGAGATGAAGATCGACGCCACCGAACCGCAGCGGGGCCAGTTC AACTTCAGCTCCGCCGACCGCGTCTACAACTGGGCGGTGCAGAACGGCAAGCAGGTGCGC GGCCACACCCTGGCCTGGCACTCCCAGCAGCCCGGCTGGATGCAGAGCCTCAGCGGCAGC GCGCTGCGCCAGGCGATGATCGACCACATCAACGGCGTGATGGCCCACTACAAGGGCAAG ATCGTCCAGTGGGACGTCGTGAACGAGGCCTTCGCCGACGGCAGTTCGGGAGCGCGGCGG GACTCCAACCTGCAACGCAGCGGCAACGACTGGATCGAGGTCGCCTTCCGCACCGCGCGC GCCGCCGACCCGTCCGCCAAGCTCTGCTACAACGACTACAACGTCGAGAACTGGACCTGG GCCAAGACCCAGGCCATGTACAACATGGTGCGGGACTTCAAGCAGCGCGGCGTGCCGATC GACTGCGTCGGCTTCCAGTCGCACTTCAACAGCGGCAGCCCCTACAACAGCAACTTCCGC ACCACACTGCAGAACTTCGCCGCCCTCGGCGTCGACGTGGCCATCACCGAGCTGGACATC CAGGGCGCCCCGGCCTCGACCTACGCCAACGTGACCAACGACTGCCTGGCCGTCTCGCGC TGCCTCGGCATCACCGTCTGGGGTGTGCGCGACAGCGACTCCTGGCGGTCGGAGCAGACG CCGTTGCTGTTCAACAACGACGGCAGCAAGAAGGCCGCGTACACCGCCGTCCTCGACGCA CTCAACGGCGGCGACTCCTCGGAGCCCCCCGCGGACGGGGGACAGATCAAGGGCGTCGGT TCGGGCCGCTGCCTCGACGTGCCCGACGCCAGCACCTCCGACGGCACCCAGCTCCAGCTG TGGGACTGCCACAGCGGCACCAACCAGCAGTGGGCCGCCACTGACGCGGGCGAGCTCAGG GTCTACGGCGACAAGTGCCTGGACGCCGCAGGCACCAGCAACGGCTCCAAGGTCCAGATC TACAGCTGCTGGGGCGGCGACAACCAGAAGTGGCGCCTCAACTCCGACGGGTCCGTCGTC GGCGTCCAGTCCGGCCTCTGCCTCGACGCCGTCGGGAACGGCACGGCCAACGGCACCCTG ATCCAGCTGTACACCTGCTCCAACGGCAGCAACCAACGCTGGACCCGCACCTGA PF00331 Glyco_hydro_10 PF00652 Ricin_B_lectin function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity function hydrolase activity process carbohydrate metabolism process physiological process process metabolism process macromolecule metabolism BE0003071 Endo-1,4-beta-xylanase Bacillus circulans unknown Endo-1,4-beta-xylanase Involved in hydrolase activity, hydrolyzing O-glycosyl compounds Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans xlnA Cytoplasmic None 9.72 23359.0 Bacillus circulans GenBank Gene Database X07723 UniProtKB P09850 UniProt Accession XYNA_BACCI 1,4-beta-D- xylan xylanohydrolase EC 3.2.1.8 Endo-1,4-beta-xylanase precursor Xylanase >Endo-1,4-beta-xylanase MFKFKKNFLVGLSAALMSISLFSATASAASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSN TGNFVVGKGWTTGSPFRTINYNAGVWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTG TYKGTVKSDGGTYDIYTTTRYNAPSIDGDRTTFTQYWSVRQSKRPTGSNATITFTNHVNA WKSHGMNLGSNWAYQVMATEGYQSSGSSNVTVW >642 bp ATGTTTAAGTTTAAAAAGAATTTCTTAGTTGGATTATCGGCAGCTTTAATGAGTATTAGC TTGTTTTCGGCAACCGCCTCTGCAGCTAGCACAGACTACTGGCAAAATTGGACTGATGGG GGCGGTATAGTAAACGCTGTCAATGGGTCTGGCGGGAATTACAGTGTTAATTGGTCTAAT ACCGGAAATTTTGTTGTTGGTAAAGGTTGGACTACAGGTTCGCCATTTAGGACGATAAAC TATAATGCCGGAGTTTGGGCGCCGAATGGCAATGGATATTTAACTTTATATGGTTGGACG AGATCACCTCTCATAGAATATTATGTAGTGGATTCATGGGGTACTTATAGACCTACTGGA ACGTATAAAGGTACTGTAAAAAGTGATGGGGGTACATATGACATATATACAACTACACGT TATAACGCACCTTCCATTGATGGCGATCGCACTACTTTTACGCAGTACTGGAGTGTTCGC CAGTCGAAGAGACCAACTGGAAGCAACGCTACAATCACTTTCACGAATCATGTGAACGCA TGGAAGAGCCATGGAATGAATCTGGGCAGTAATTGGGCTTACCAAGTCATGGCGACAGAA GGATATCAAAGTAGTGGAAGTTCTAACGTAACAGTGTGGTAA PF00457 Glyco_hydro_11 function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process BE0003072 Hydrolase Streptomyces olivaceoviridis unknown Hydrolase Involved in hydrolase activity, hydrolyzing O-glycosyl compounds Cytoplasmic None 6.5 46750.0 Streptomyces olivaceoviridis UniProtKB Q7SI98 UniProt Accession Q7SI98_STROI >Hydrolase AESTLGAAAAQSGRYFGTAIASGKLGDSAYTTIASREFNMVTAENEMKIDATEPQRGQFN FSAGDRVYNWAVQNGKQVRGHTLAWHSQQPGWMQSLSGSTLRQAMIDHINGVMGHYKGKI AQWDVVNEAFSDDGSGGRRDSNLQRTGNDWIEVAFRTARAADPAAKLCYNDYNIENWTWA KTQGVYNMVRDFKQRGVPIDCVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQ GASSSTYAAVTNDCLAVSRCLGITVWGVRDTDSWRSGDTPLLFNGDGSKKAAYTAVLNAL NGGSSTPPPSGGGQIKGVGSGRCLDVPNASTTDGTQVQLYDCHSATNQQWTYTDAGELRV YGDKCLDAAGTGNGTKVQIYSCWGGDNQKWRLNSDGSIVGVQSGLCLDAVGGGTANGTLI QLYSCSNGSNQRWTRT PF00331 Glyco_hydro_10 PF00652 Ricin_B_lectin function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity function hydrolase activity process physiological process process metabolism process macromolecule metabolism process carbohydrate metabolism BE0003073 Endo-1,4-beta-xylanase Pseudoalteromonas haloplanktis unknown Endo-1,4-beta-xylanase Involved in catalytic activity xyl Cytoplasmic None 8.67 48407.0 Pseudoalteromonas haloplanktis GenBank Gene Database AJ427921 UniProtKB Q8RJN8 UniProt Accession Q8RJN8_PSEHA EC 3.2.1.8 Endo-1,4-beta-xylanase precursor >Endo-1,4-beta-xylanase MKVFFKITTLLLILISYQSLAAFNNNPSSVGAYSSGTYRNLAQEMGKTNIQQKVNSTFDN MFGYNNTQQLYYPYTENGVYKAHYIKAINPDEGDDIRTEGQSWGMTAAVMLNKQEEFDNL WRFAKAYQKNPDNHPDAKKQGVYAWKLKLNQNGFVYKVDEGPAPDGEEYFAFALLNASAR WGNSGEFNYYNDAITMLNTIKNKLMENQIIRFSPYIDNLTDPSYHIPAFYDYFANNVTNQ ADKNYWRQVATKSRTLLKNHFTKVSGSPHWNLPTFLSRLDGSPVIGYIFNGQANPGQWYE FDAWRVIMNVGLDAHLMGAQAWHKSAVNKALGFLSYAKTNNSKNCYEQVYSYGGAQNRGC AGEGQKAANAVALLASTNAGQANEFFNEFWSLSQPTGDYRYYNGSLYMLAMLHVSGNFKF YNNTFN >1281 bp ATGAAAGTATTTTTTAAAATAACAACTTTATTGTTAATACTAATAAGCTATCAATCACTT GCTGCATTTAATAATAACCCATCGAGTGTAGGCGCCTACAGTTCAGGGACATACCGTAAC CTCGCACAAGAAATGGGTAAAACAAATATACAGCAAAAGGTGAATAGTACTTTTGACAAT ATGTTTGGCTATAACAACACACAACAACTTTACTACCCGTACACCGAAAACGGTGTTTAT AAAGCACACTACATAAAAGCAATTAACCCAGACGAAGGCGACGATATAAGAACAGAAGGG CAATCGTGGGGAATGACCGCCGCTGTCATGCTTAATAAACAAGAAGAATTTGATAACCTA TGGCGCTTTGCAAAAGCGTATCAAAAAAATCCAGACAATCACCCTGATGCTAAAAAACAA GGCGTTTACGCGTGGAAACTAAAGCTTAATCAAAACGGCTTTGTTTATAAAGTGGATGAG GGCCCCGCTCCCGATGGCGAAGAGTACTTTGCGTTTGCACTACTTAATGCCTCTGCTCGT TGGGGGAATTCGGGTGAGTTTAACTACTACAACGATGCCATTACCATGTTAAACACAATT AAAAATAAGCTGATGGAAAACCAAATAATCCGCTTTTCACCTTACATTGATAACCTAACA GACCCTTCTTACCATATACCTGCGTTTTACGACTACTTTGCAAATAACGTAACTAACCAA GCAGACAAAAATTACTGGCGACAAGTAGCCACAAAAAGTAGAACCTTACTTAAAAACCAT TTTACAAAAGTAAGTGGTAGCCCGCATTGGAACTTACCTACATTTTTATCGCGCTTAGAT GGCAGCCCTGTTATTGGCTACATTTTTAACGGCCAAGCAAACCCAGGTCAATGGTATGAA TTTGATGCATGGCGCGTAATTATGAATGTGGGTTTAGACGCGCATTTAATGGGTGCTCAA GCGTGGCATAAAAGTGCAGTTAATAAAGCACTGGGCTTTTTAAGTTATGCAAAAACAAAC AACAGTAAAAACTGTTACGAGCAAGTGTATTCGTACGGTGGAGCGCAAAACAGAGGCTGT GCAGGCGAAGGTCAAAAAGCCGCGAATGCAGTAGCGTTACTTGCTTCAACAAATGCTGGG CAAGCAAATGAGTTTTTTAACGAATTTTGGTCTTTATCGCAACCAACGGGTGACTACCGT TACTATAATGGTTCGTTATATATGTTAGCTATGCTGCATGTATCGGGCAATTTTAAGTTT TATAACAACACGTTTAATTAA PF01270 Glyco_hydro_8 function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity function hydrolase activity process carbohydrate metabolism process physiological process process metabolism process macromolecule metabolism BE0004338 Lactase-phlorizin hydrolase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Lactase-phlorizin hydrolase Carbohydrate transport and metabolism LPH splits lactose in the small intestine LCT 2q21 Apical cell membrane 1883-1901 6.3 218570.8 Human HUGO Gene Nomenclature Committee (HGNC) GNC:6530 GeneCards LCT GenBank Gene Database X07994 GenBank Protein Database 34400 UniProtKB P09848 UniProt Accession LPH_HUMAN Lactase Lactase-glycosylceramidase Phlorizin hydrolase >Lactase-phlorizin hydrolase MELSWHVVFIALLSFSCWGSDWESDRNFISTAGPLTNDLLHNLSGLLGDQSSNFVAGDKD MYVCHQPLPTFLPEYFSSLHASQITHYKVFLSWAQLLPAGSTQNPDEKTVQCYRRLLKAL KTARLQPMVILHHQTLPASTLRRTEAFADLFADYATFAFHSFGDLVGIWFTFSDLEEVIK ELPHQESRASQLQTLSDAHRKAYEIYHESYAFQGGKLSVVLRAEDIPELLLEPPISALAQ DTVDFLSLDLSYECQNEASLRQKLSKLQTIEPKVKVFIFNLKLPDCPSTMKNPASLLFSL FEAINKDQVLTIGFDINEFLSCSSSSKKSMSCSLTGSLALQPDQQQDHETTDSSPASAYQ RVWEAFANQSRAERDAFLQDTFPEGFLWGASTGAFNVEGGWAEGGRGVSIWDPRRPLNTT EGQATLEVASDSYHKVASDVALLCGLRAQVYKFSISWSRIFPMGHGSSPSLPGVAYYNKL IDRLQDAGIEPMATLFHWDLPQALQDHGGWQNESVVDAFLDYAAFCFSTFGDRVKLWVTF HEPWVMSYAGYGTGQHPPGISDPGVASFKVAHLVLKAHARTWHHYNSHHRPQQQGHVGIV LNSDWAEPLSPERPEDLRASERFLHFMLGWFAHPVFVDGDYPATLRTQIQQMNRQCSHPV AQLPEFTEAEKQLLKGSADFLGLSHYTSRLISNAPQNTCIPSYDTIGGFSQHVNHVWPQT SSSWIRVVPWGIRRLLQFVSLEYTRGKVPIYLAGNGMPIGESENLFDDSLRVDYFNQYIN EVLKAIKEDSVDVRSYIARSLIDGFEGPSGYSQRFGLHHVNFSDSSKSRTPRKSAYFFTS IIEKNGFLTKGAKRLLPPNTVNLPSKVRAFTFPSEVPSKAKVVWEKFSSQPKFERDLFYH GTFRDDFLWGVSSSAYQIEGAWDADGKGPSIWDNFTHTPGSNVKDNATGDIACDSYHQLD ADLNMLRALKVKAYRFSISWSRIFPTGRNSSINSHGVDYYNRLINGLVASNIFPMVTLFH WDLPQALQDIGGWENPALIDLFDSYADFCFQTFGDRVKFWMTFNEPMYLAWLGYGSGEFP PGVKDPGWAPYRIAHAVIKAHARVYHTYDEKYRQEQKGVISLSLSTHWAEPKSPGVPRDV EAADRMLQFSLGWFAHPIFRNGDYPDTMKWKVGNRSELQHLATSRLPSFTEEEKRFIRAT ADVFCLNTYYSRIVQHKTPRLNPPSYEDDQEMAEEEDPSWPSTAMNRAAPWGTRRLLNWI KEEYGDIPIYITENGVGLTNPNTEDTDRIFYHKTYINEALKAYRLDGIDLRGYVAWSLMD NFEWLNGYTVKFGLYHVDFNNTNRPRTARASARYYTEVITNNGMPLAREDEFLYGRFPEG FIWSAASAAYQIEGAWRADGKGLSIWDTFSHTPLRVENDAIGDVACDSYHKIAEDLVTLQ NLGVSHYRFSISWSRILPDGTTRYINEAGLNYYVRLIDTLLAASIQPQVTIYHWDLPQTL QDVGGWENETIVQRFKEYADVLFQRLGDKVKFWITLNEPFVIAYQGYGYGTAAPGVSNRP GTAPYIVGHNLIKAHAEAWHLYNDVYRASQGGVISITISSDWAEPRDPSNQEDVEAARRY VQFMGGWFAHPIFKNGDYNEVMKTRIRDRSLAAGLNKSRLPEFTESEKRRINGTYDFFGF NHYTTVLAYNLNYATAISSFDADRGVASIADRSWPDSGSFWLKMTPFGFRRILNWLKEEY NDPPIYVTENGVSQREETDLNDTARIYYLRTYINEALKAVQDKVDLRGYTVWSAMDNFEW ATGFSERFGLHFVNYSDPSLPRIPKASAKFYASVVRCNGFPDPATGPHACLHQPDAGPTI SPVRQEEVQFLGLMLGTTEAQTALYVLFSLVLLGVCGLAFLSYKYCKRSKQGKTQRSQQE LSPVSSF >5784 bp ATGGAGCTGTCTTGGCATGTAGTCTTTATTGCCCTGCTAAGTTTTTCATGCTGGGGGTCA GACTGGGAGTCTGATAGAAATTTCATTTCCACCGCTGGTCCTCTAACCAATGACTTGCTG CACAACCTGAGTGGTCTCCTGGGAGACCAGAGTTCTAACTTTGTAGCAGGGGACAAAGAC ATGTATGTTTGTCACCAGCCACTGCCCACTTTCCTGCCAGAATACTTCAGCAGTCTCCAT GCCAGTCAGATCACCCATTATAAGGTATTTCTGTCATGGGCACAGCTCCTCCCAGCAGGA AGCACCCAGAATCCAGACGAGAAAACAGTGCAGTGCTACCGGCGACTCCTCAAGGCCCTC AAGACTGCACGGCTTCAGCCCATGGTCATCCTGCACCACCAGACCCTCCCTGCCAGCACC CTCCGGAGAACCGAAGCCTTTGCTGACCTCTTCGCCGACTATGCCACATTCGCCTTCCAC TCCTTCGGGGACCTAGTTGGGATCTGGTTCACCTTCAGTGACTTGGAGGAAGTGATCAAG GAGCTTCCCCACCAGGAATCAAGAGCGTCACAACTCCAGACCCTCAGTGATGCCCACAGA AAAGCCTATGAGATTTACCACGAAAGCTATGCTTTTCAGGGCGGAAAACTCTCTGTTGTC CTGCGAGCTGAAGATATCCCGGAGCTCCTGCTAGAACCACCCATATCTGCGCTTGCCCAG GACACGGTCGATTTCCTCTCTCTTGATTTGTCTTATGAATGCCAAAATGAGGCAAGTCTG CGGCAGAAGCTGAGTAAATTGCAGACCATTGAGCCAAAAGTGAAAGTTTTCATCTTCAAC CTAAAACTCCCAGACTGCCCCTCCACCATGAAGAACCCAGCCAGTCTGCTCTTCAGCCTT TTTGAAGCCATAAATAAAGACCAAGTGCTCACCATTGGGTTTGATATTAATGAGTTTCTG AGTTGTTCATCAAGTTCCAAGAAAAGCATGTCTTGTTCTCTGACTGGCAGCCTGGCCCTT CAGCCTGACCAGCAGCAGGACCACGAGACCACGGACTCCTCTCCTGCCTCTGCCTATCAG AGAGTCTGGGAAGCATTTGCCAATCAGTCCAGAGCGGAAAGGGATGCCTTCCTGCAGGAT ACTTTCCCTGAAGGCTTCCTCTGGGGTGCCTCCACAGGAGCCTTTAACGTGGAAGGAGGC TGGGCCGAGGGTGGGAGAGGGGTGAGCATCTGGGATCCACGCAGGCCCCTGAACACCACT GAGGGCCAAGCGACGCTGGAGGTGGCCAGCGACAGTTACCACAAGGTAGCCTCTGACGTC GCCCTGCTTTGCGGCCTCCGGGCTCAGGTGTACAAGTTCTCCATCTCCTGGTCCCGGATC TTCCCCATGGGGCACGGGAGCAGCCCCAGCCTCCCAGGCGTTGCCTACTACAACAAGCTG ATTGACAGGCTACAGGATGCGGGCATCGAGCCCATGGCCACGCTGTTCCACTGGGACCTG CCTCAGGCCCTGCAGGATCATGGTGGATGGCAGAATGAGAGCGTGGTGGATGCCTTCCTG GACTATGCGGCCTTCTGCTTCTCCACATTTGGGGACCGTGTGAAGCTGTGGGTGACCTTC CATGAGCCGTGGGTGATGAGCTACGCAGGCTATGGCACCGGCCAGCACCCTCCCGGCATC TCTGACCCAGGAGTGGCCTCTTTTAAGGTGGCTCACTTGGTCCTCAAGGCTCATGCCAGA ACTTGGCACCACTACAACAGCCATCATCGCCCACAGCAGCAGGGGCACGTGGGCATTGTG CTGAACTCAGACTGGGCAGAACCCCTGTCTCCAGAGAGGCCTGAGGACCTGAGAGCCTCT GAGCGCTTCTTGCACTTCATGCTGGGCTGGTTTGCACACCCCGTCTTTGTGGATGGAGAC TACCCAGCCACCCTGAGGACCCAGATCCAACAGATGAACAGACAGTGCTCCCATCCTGTG GCTCAACTCCCCGAGTTCACAGAGGCAGAGAAGCAGCTCCTGAAAGGCTCTGCTGATTTT CTGGGTCTGTCGCATTACACCTCCCGCCTCATCAGCAACGCCCCACAAAACACCTGCATC CCTAGCTATGATACCATTGGAGGCTTCTCCCAACACGTGAACCATGTGTGGCCCCAGACC TCATCCTCTTGGATTCGTGTGGTGCCCTGGGGGATAAGGAGGCTGTTGCAGTTTGTATCC CTGGAATACACAAGAGGAAAAGTTCCAATATACCTTGCCGGGAATGGCATGCCCATAGGG GAAAGTGAAAATCTCTTTGATGATTCCTTAAGAGTAGACTACTTCAATCAATATATCAAT GAGGTGCTCAAGGCTATCAAGGAAGACTCTGTGGATGTTCGTTCCTACATTGCTCGTTCC CTCATTGATGGCTTCGAAGGCCCTTCTGGTTACAGCCAGCGGTTTGGCCTGCACCACGTC AACTTCAGCGACAGCAGCAAGTCAAGGACTCCCAGGAAATCTGCCTACTTTTTCACTAGC ATCATAGAAAAGAACGGTTTCCTCACCAAGGGGGCAAAAAGACTGCTACCACCTAATACA GTAAACCTCCCCTCCAAAGTCAGAGCCTTCACTTTTCCATCTGAGGTGCCCTCCAAGGCT AAAGTCGTTTGGGAAAAGTTCTCCAGCCAACCCAAGTTCGAAAGAGATTTGTTCTACCAC GGGACGTTTCGGGATGACTTTCTGTGGGGCGTGTCCTCTTCCGCTTATCAGATTGAAGGC GCGTGGGATGCCGATGGCAAAGGCCCCAGCATCTGGGATAACTTTACCCACACACCAGGG AGCAATGTGAAAGACAATGCCACTGGAGACATCGCCTGTGACAGCTATCACCAGCTGGAT GCCGATCTGAATATGCTCCGAGCTTTGAAGGTGAAGGCCTACCGCTTCTCTATCTCCTGG TCTCGGATTTTCCCAACTGGGAGAAACAGCTCTATCAACAGTCATGGGGTTGATTATTAC AACAGGCTGATCAATGGCTTGGTGGCAAGCAACATCTTTCCCATGGTGACATTGTTCCAT TGGGACCTGCCCCAGGCCCTCCAGGATATCGGAGGCTGGGAGAATCCTGCCTTGATTGAC TTGTTTGACAGCTACGCAGACTTTTGTTTCCAGACCTTTGGTGATAGAGTCAAGTTTTGG ATGACTTTTAATGAGCCCATGTACCTGGCATGGCTAGGTTATGGCTCAGGGGAATTTCCC CCAGGGGTGAAGGACCCAGGCTGGGCACCATATAGGATAGCCCACACCGTCATCAAAGCC CATGCCAGAGTCTATCACACGTACGATGAGAAATACAGGCAGGAGCAGAAGGGGGTCATC TCGCTGAGCCTCAGTACACACTGGGCAGAGCCCAAGTCACCAGGGGTCCCCAGAGATGTG GAAGCCGCTGACCGAATGCTGCAGTTCTCCCTGGGCTGGTTTGCTCACCCCATTTTTAGA AACGGAGACTATCCTGACACCATGAAGTGGAAAGTGGGGAACAGGAGTGAACTGCAGCAC TTAGCCACCTCCCGCCTGCCAAGCTTCACTGAGGAAGAGAAGAGGTTCATCAGGGCGACG GCCGACGTCTTCTGCCTCAACACGTACTACTCCAGAATCGTGCAGCACAAAACACCCAGG CTAAACCCACCCTCCTACGAAGACGACCAGGAGATGGCTGAGGAGGAGGACCCTTCGTGG CCTTCCACGGCAATGAACAGAGCTGCGCCCTGGGGGACGCGAAGGCTGCTGAACTGGATC AAGGAAGAGTATGGTGACATCCCCATTTACATCACCGAAAACGGAGTGGGGCTGACCAAT CCGAACACGGAGGATACTGATAGGATATTTTACCACAAAACCTACATCAATGAGGCTTTG AAAGCCTACAGGCTCGATGGTATAGACCTTCGAGGGTATGTCGCCTGGTCTCTGATGGAC AACTTTGAGTGGCTAAATGGCTACACGGTCAAGTTTGGACTGTACCATGTTGATTTCAAC AACACGAACAGGCCTCGCACAGCAAGAGCCTCCGCCAGGTACTACACAGAGGTCATTACC AACAACGGCATGCCACTGGCCAGGGAGGATGAGTTTCTGTACGGACGGTTTCCTGAGGGC TTCATCTGGAGTGCAGCTTCTGCTGCATATCAGATTGAAGGTGCGTGGAGAGCAGATGGC AAAGGACTCAGCATTTGGGACACGTTTTCTCACACACCACTGAGGGTTGAGAACGATGCC ATTGGAGACGTGGCCTGTGACAGTTATCACAAGATTGCTGAGGATCTGGTCACCCTGCAG AACCTGGGTGTGTCCCACTACCGTTTTTCCATCTCCTGGTCTCGCATCCTCCCTGATGGA ACCACCAGGTACATCAATGAAGCGGGCCTGAACTACTACGTGAGGCTCATCGATACACTG CTGGCCGCCAGCATCCAGCCCCAGGTGACCATTTACCACTGGGACCTACCACAGACGCTC CAAGATGTAGGAGGCTGGGAGAATGAGACCATCGTGCAGCGGTTTAAGGAGTATGCAGAT GTGCTCTTCCAGAGGCTGGGAGACAAGGTGAAGTTTTGGATCACGTTGAATGAGCCCTTT GTCATTGCTTACCAGGGCTATGGCTACGGAACAGCAGCTCCAGGAGTCTCCAATAGGCCT GGCACTGCCCCCTACATTGTTGGCCACAATCTAATAAAGGCTCATGCTGAGGCCTGGCAT CTGTACAACGATGTGTACCGCGCCAGTCAAGGTGGCGTGATTTCCATCACCATCAGCAGT GACTGGGCTGAACCCAGAGATCCCTCTAACCAGGAGGATGTGGAGGCAGCCAGGAGATAT GTTCAGTTCATGGGAGGCTGGTTTGCACATCCTATTTTCAAGAATGGAGATTACAATGAG GTGATGAAGACGCGGATCCGTGACAGGAGCTTGGCTGCAGGCCTCAACAAGTCTCGGCTG CCAGAATTTACAGAGAGTGAGAAGAGGAGGATCAACGGCACCTATGACTTTTTTGGGTTC AATCACTACACCACTGTCCTCGCCTACAACCTCAACTATGCCACTGCCATCTCTTCTTTT GATGCAGACAGAGGAGTTGCTTCCATCGCAGATCGCTCGTGGCCAGACTCTGGCTCCTTC TGGCTGAAGATGACGCCTTTTGGCTTCAGGAGGATCCTGAACTGGTTAAAGGAGGAATAC AATGACCCTCCAATTTATGTCACAGAGAATGGAGTGTCCCAGCGGGAAGAAACAGACCTC AATGACACTGCAAGGATCTACTACCTTCGGACTTACATCAATGAGGCCCTCAAAGCTGTG CAGGACAAGGTGGACCTTCGAGGATACACAGTTTGGAGTGCGATGGACAATTTTGAGTGG GCCACAGGCTTTTCAGAGAGATTTGGTCTGCATTTTGTGAACTACAGTGACCCTTCTCTG CCAAGGATCCCCAAAGCATCAGCGAAGTTCTACGCCTCTGTGGTCCGATGCAATGGCTTC CCTGACCCCGCTACAGGGCCTCACGCTTGTCTCCACCAGCCAGATGCTGGACCCACCATC AGCCCCGTGAGACAGGAGGAGGTGCAGTTCCTGGGGCTAATGCTCGGCACCACAGAAGCA CAGACAGCTTTGTACGTTCTCTTTTCTCTTGTGCTTCTTGGAGTCTGTGGCTTGGCATTT CTGTCATACAAGTACTGCAAGCGCTCTAAGCAAGGGAAAACACAACGAAGCCAACAGGAA TTGAGCCCGGTGTCTTCATTCTGA PF00232 Glyco_hydro_1 function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process BE0002828 Endoxylanase Cellvibrio mixtus unknown Endoxylanase Involved in hydrolase activity, hydrolyzing O-glycosyl compounds xynC Cytoplasmic None 7.89 42914.0 Cellvibrio mixtus GenBank Gene Database AF049493 UniProtKB O68541 UniProt Accession O68541_9GAMM >Endoxylanase MNLSRRQLLALTSAGIAMGQASKLAAATKAAEQTGLKSAYKDNFLIGAALNATIASGADE RLNTLIAKEFNSITPENCMKWGVLRDAQGQWNWKDADAFVAFGTKHNLHMVGHTLVWHSQ IHDEVFKNADGSYISKAALQKKMEEHITTLAGRYKGKLAAWDVVNEAVGDDLKMRDSHWY KIMGDDFIYNAFTLANEVDPKAHLMYNDYNIERTGKREATVEMIERLQKRGMPIHGLGIQ GHLGIDTPPIAEIEKSIIAFAKLGLRVHFTELDVDVLPSVWELPVAEVSTRFEYKPERDP YTKGLPQEMQDKLAKRYEDLFKLFIKHSDKIDRATFWGVSDDASWLNGFPIPGRTNYPLL FDRKLQPKDAYFRLLDLKR >1140 bp ATGAATCTTTCACGTCGGCAACTTCTCGCACTAACCAGTGCGGGCATCGCGATGGGCCAA GCCAGCAAGCTTGCGGCAGCAACCAAAGCGGCGGAGCAAACCGGGCTTAAAAGTGCCTAC AAGGATAACTTTTTAATCGGCGCCGCACTCAATGCGACTATTGCGAGCGGTGCGGATGAA CGCCTTAATACCTTGATTGCCAAAGAGTTTAATTCAATTACGCCAGAAAACTGCATGAAA TGGGGTGTATTGCGCGATGCCCAAGGCCAGTGGAATTGGAAAGACGCCGATGCATTTGTT GCATTTGGCACCAAACACAATCTGCACATGGTCGGCCACACCTTGGTATGGCACAGCCAG ATCCACGATGAAGTATTTAAAAACGCCGATGGTAGTTACATCAGCAAAGCTGCGTTGCAG AAAAAAATGGAAGAGCACATCACCACCCTCGCGGGCCGCTATAAAGGCAAACTTGCCGCC TGGGATGTAGTGAATGAAGCGGTGGGCGATGATTTGAAAATGCGTGACAGCCATTGGTAC AAGATTATGGGCGATGATTTTATCTACAACGCCTTTACCCTTGCCAATGAAGTCGACCCC AAAGCGCACTTGATGTACAACGATTACAACATTGAACGCACCGGCAAACGCGAAGCAACA GTGGAAATGATCGAGCGCTTGCAAAAACGCGGCATGCCGATTCACGGTTTAGGAATTCAA GGACATTTGGGAATAGATACTCCGCCTATTGCCGAGATCGAAAAGAGTATTATCGCCTTC GCCAAATTGGGCCTGCGCGTGCACTTCACCGAGCTGGATGTAGACGTACTGCCTTCGGTA TGGGAACTGCCGGTAGCTGAAGTTTCTACCCGCTTTGAATACAAACCCGAGCGCGACCCC TATACCAAAGGTTTGCCGCAGGAAATGCAAGACAAATTGGCAAAACGCTACGAAGATTTA TTCAAATTATTTATCAAACACAGCGATAAAATCGACCGCGCCACCTTCTGGGGTGTAAGC GATGACGCAAGCTGGCTCAACGGCTTCCCGATTCCCGGTCGCACCAACTACCCACTGTTG TTTGATCGCAAACTACAACCGAAAGACGCTTACTTCCGTTTACTGGATTTAAAACGTTAA PF00331 Glyco_hydro_10 function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity function hydrolase activity process physiological process process metabolism process macromolecule metabolism process carbohydrate metabolism BE0001847 Beta-amylase Bacillus cereus # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Beta-amylase Involved in beta-amylase activity Hydrolysis of 1,4-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains spoII Cytoplasmic None 6.72 61629.0 Bacillus cereus GenBank Gene Database AB024519 GenBank Protein Database 4520330 UniProtKB P36924 UniProt Accession AMYB_BACCE 1,4-alpha-D-glucan maltohydrolase Beta-amylase precursor EC 3.2.1.2 >Beta-amylase precursor MKNQFQYCCIVILSVVMLFVSLLIPQASSAAVNGKGMNPDYKAYLMAPLKKIPEVTNWET FENDLRWAKQNGFYAITVDFWWGDMEKNGDQQFDFSYAQRFAQSVKNAGMKMIPIISTHQ CGGNVGDDCNVPIPSWVWNQKSDDSLYFKSETGTVNKETLNPLASDVIRKEYGELYTAFA AAMKPYKDVIAKIYLSGGPAGELRYPSYTTSDGTGYPSRGKFQAYTEFAKSKFRLWVLNK YGSLNEVNKAWGTKLISELAILPPSDGEQFLMNGYLSMYGKDYLEWYQGILENHTKLIGE LAHNAFDTTFQVPIGAKIAGVHWQYNNPTIPHGAEKPAGYNDYSHLLDAFKSAKLDVTFT CLEMTDKGSYPEYSMPKTLVQNIATLANEKGIVLNGENALSIGNEEEYKRVAEMAFNYNF AGFTLLRYQDVMYNNSLMGKFKDLLGVTPVMQTIVVKNVPTTIGDTVYITGNRAELGSWD TKQYPIQLYYDSHSNDWRGNVVLPAERNIEFKAFIKSKDGTVKSWQTIQQSWNPVPLKTT SHTSSW >1641 bp ATGAAAAATCAGTTTCAATATTGTTGTATTGTCATTTTGTCTGTAGTGATGTTATTTGTA TCATTATTAATTCCGCAAGCGAGTTCGGCAGCTGTAAATGGAAAAGGAATGAATCCAGAT TACAAAGCATATTTAATGGCGCCATTAAAAAAGATACCGGAAGTAACAAATTGGGAGACA TTTGAAAATGATTTACGATGGGCAAAACAAAATGGTTTTTATGCTATTACAGTTGATTTT TGGTGGGGGGATATGGAAAAGAACGGAGATCAGCAATTTGATTTTTCATACGCACAGCGC TTTGCTCAATCGGTAAAAAATGCAGGTATGAAAATGATTCCTATTATTTCCACACATCAG TGCGGTGGAAATGTTGGGGATGATTGCAATGTACCAATTCCTTCATGGGTTTGGAATCAA AAATCCGATGATAGCCTTTATTTTAAGTCTGAAACAGGAACTGTCAATAAAGAAACATTA AATCCACTTGCTTCAGATGTAATTCGAAAGGAATATGGTGAACTATATACAGCATTCGCA GCAGCTATGAAACCGTATAAAGATGTAATTGCAAAAATATATTTATCTGGAGGACCAGCT GGTGAACTAAGATATCCTTCATATACAACTTCCGATGGGACAGGATATCCCTCACGTGGA AAGTTTCAAGCGTATACAGAGTTTGCAAAATCTAAATTTCGTTTATGGGTATTAAATAAA TATGGTTCTCTAAATGAAGTGAATAAAGCATGGGGCACGAAACTGATTTCAGAGTTAGCA ATTTTACCACCAAGCGATGGGGAACAATTCTTAATGAATGGATATCTTTCTATGTATGGA AAAGACTATTTAGAATGGTATCAGGGCATCTTGGAAAATCATACAAAATTAATTGGTGAA TTAGCACATAACGCATTTGACACAACTTTCCAAGTACCAATTGGTGCAAAAATTGCAGGC GTACATTGGCAATATAATAACCCAACAATACCTCATGGAGCTGAAAAGCCTGCAGGGTAT AATGATTATAGCCATTTACTTGATGCTTTCAAAAGTGCAAAGCTAGATGTAACATTTACT TGCTTAGAAATGACAGATAAAGGTAGTTATCCGGAATATTCAATGCCAAAAACATTGGTA CAAAATATTGCAACATTAGCCAATGAAAAGGGAATTGTATTAAACGGTGAAAATGCTTTA AGTATCGGAAATGAAGAAGAGTATAAAAGAGTTGCAGAAATGGCTTTCAATTATAATTTT GCTGGATTTACGTTACTTCGTTATCAAGATGTAATGTATAACAATTCATTAATGGGGAAA TTTAAAGATTTATTAGGTGTAACCCCTGTTATGCAAACGATTGTAGTAAAAAATGTTCCT ACAACAATAGGAGATACTGTTTATATTACTGGGAATCGTGCGGAATTAGGAAGTTGGGAC ACAAAACAGTATCCAATTCAATTATATTATGATTCTCATAGTAATGATTGGAGAGGAAAT GTTGTGTTGCCAGCTGAAAGAAATATAGAATTTAAAGCATTTATTAAAAGTAAAGATGGA ACGGTTAAATCATGGCAAACAATACAACAAAGTTGGAATCCAGTGCCACTAAAGACTACC TCTCATACAAGTAGTTGGTAA PF00686 CBM_20 PF01373 Glyco_hydro_14 function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function amylase activity function beta-amylase activity function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process polysaccharide metabolism process polysaccharide catabolism process physiological process "
drug:alpha-D-Xylopyranoserdfs:label"alpha-D-Xylopyranose"
drug:alpha-D-Xylopyranoseowl:sameAsdrug:EXPT03270
drug:alpha-D-Xylopyranoserdf:typedrugbank:drugs
drug:alprazolam lingual spraydrugbank:description"Alprazolam lingual spray is developed by NovaDel Pharma Inc. which is engaged in the development of novel drug delivery systems for prescription and over-the-counter drugs. NovaDel's vision for an alprazolam lingual spray is one that could be used by patients prone to suffering from anxiety in the face of certain predictable stimuli (e.g., closed-in spaces, airplane flight, public speaking, etc.). Such patients could successfully navigate such settings by dosing just prior to the event or at the moment when they encounter such a situation."
drug:alprazolam lingual sprayrdfs:label"alprazolam lingual spray"
drug:alprazolam lingual sprayrdf:typedrugbank:drugs
drug:anecortave acetatedrugbank:description"Anecortave acetate (Retaane) is an analog of cortisol acetate; among the modifications to the steroid are the removal of the 11ß hydroxyl OH group and an addition of a 21-acetate group. As a result of these modifications, anecortave acetate lacks the typical antiinflammatory and immunosuppressive properties of glucocorticoids.Alcon Inc. is developing and marketing Retaane."
drug:anecortave acetaterdfs:label"anecortave acetate"
drug:anecortave acetaterdf:typedrugbank:drugs
drug:anti-alpha5Beta1-integrin antibodydrugbank:description"Integrins are important adhesion molecules that regulate tumor and endothelial cell survival, proliferation and migration. The integrin alpha5beta1 has been shown to play a critical role during angiogenesis. anti-alpha5beta1 integrin antibody inhibits angiogenesis, including vessel formation induced by vascular endothelial growth factor (VEGF), basic fibroblast growth factor (bFGF), as well as other pro-angiogenic growth factors."
drug:anti-alpha5Beta1-integrin antibodyrdfs:label"anti-alpha5Beta1-integrin antibody"
drug:anti-alpha5Beta1-integrin antibodyrdf:typedrugbank:drugs
drug:atamestane-plus-toremifenedrugbank:description"Atamestane plus toremifene slows disease progression as well as letrozole does in postmenopausal women with advanced receptor-positive breast cancer."
drug:atamestane-plus-toremifenerdfs:label"atamestane-plus-toremifene"
drug:atamestane-plus-toremifenerdf:typedrugbank:drugs
drug:autologous activated macrophage therapydrugbank:description"Autologous activated macrophage therapy is used to treat patients with acute complete spinal cord injury."
drug:autologous activated macrophage therapyrdfs:label"autologous activated macrophage therapy"
drug:autologous activated macrophage therapyrdf:typedrugbank:drugs
drug:autologous fibroblast transplantdrugbank:description"Autologous fibroblast transplant is an innovative cellular processing system which creates a natural, living cell therapy. By multiplying a patient’s own collagen-producing cells or fibroblasts into tens of millions of new cells, a personalized treatment is created which is then returned to the patient’s skin. This treatment, known as the Isolagen Therapy™, is designed to improve skin damage caused by the normal effects of aging, sun damage, acne and burns."
drug:autologous fibroblast transplantrdfs:label"autologous fibroblast transplant"
drug:autologous fibroblast transplantrdf:typedrugbank:drugs
drug:autologousadipose stem cell therapydrugbank:description"Cellerix has developed an autologous adipose stem cell therapy for the treatment of fistulas. This drug has shown safety and preliminary efficacy in phase I studies. However autologous adipose stem cell therapy autologous is also a promising therapeutic approach to overcome the current disadvantages of corneal transplantation."
drug:autologousadipose stem cell therapyrdfs:label"autologousadipose stem cell therapy"
drug:autologousadipose stem cell therapyrdf:typedrugbank:drugs
drug:benzyl (2-oxopropyl)carbamatedrugbank:description" experimental This compound belongs to the benzyloxycarbonyls. These are organic compounds containing a carbonyl group substituted with a benzyloxyl group. Benzyloxycarbonyls Organic Compounds Benzenoids Benzene and Substituted Derivatives Benzyloxycarbonyls Benzylethers Ketones Carbamic Acids and Derivatives Ethers Enolates Polyamines carbamic acid derivative ketone polyamine ether enolate amine carbonyl group organonitrogen compound logP 0.89 ALOGPS logS -2.7 ALOGPS Water Solubility 3.98e-01 g/l ALOGPS logP 1.34 ChemAxon IUPAC Name benzyl N-(2-oxopropyl)carbamate ChemAxon Traditional IUPAC Name benzyl N-(2-oxopropyl)carbamate ChemAxon Molecular Weight 207.2258 ChemAxon Monoisotopic Weight 207.089543287 ChemAxon SMILES CC(=O)CNC(=O)OCC1=CC=CC=C1 ChemAxon Molecular Formula C11H13NO3 ChemAxon InChI InChI=1S/C11H13NO3/c1-9(13)7-12-11(14)15-8-10-5-3-2-4-6-10/h2-6H,7-8H2,1H3,(H,12,14) ChemAxon InChIKey InChIKey=GVRXLHLFAABVLJ-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 55.4 ChemAxon Refractivity 55.23 ChemAxon Polarizability 21.7 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 13.78 ChemAxon pKa (strongest basic) -7.6 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 22747857 PubChem Substance 99443764 ChemSpider 11624889 PDB 959 BE0003801 Replicase polyprotein 1ab SARS-CoV # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Replicase polyprotein 1ab rep SARS-CoV UniProtKB P0C6X7 UniProt Accession R1AB_CVHSA "
drug:benzyl (2-oxopropyl)carbamaterdfs:label"benzyl (2-oxopropyl)carbamate"
drug:benzyl (2-oxopropyl)carbamaterdf:typedrugbank:drugs
drug:beta alethinedrugbank:description"Beta alethine is studied in the treatment of cancer. It belongs to a family of chemicals called disulfides. It is a low molecular weight disulfide that has been shown to exhibit in vivo antitumor activity in murine myeloma and melanoma models."
drug:beta alethinerdfs:label"beta alethine"
drug:beta alethinerdf:typedrugbank:drugs
drug:beta-D-Ribopyranosedrugbank:description" experimental This compound belongs to the hexoses. These are monosaccharides in which the sugar unit is a hexose. Hexoses Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Monosaccharides Oxanes Secondary Alcohols 1,2-Diols Hemiacetals Polyamines oxane hemiacetal polyol 1,2-diol secondary alcohol polyamine ether alcohol logP -2.6 ALOGPS logS 0.91 ALOGPS Water Solubility 1.22e+03 g/l ALOGPS logP -2.3 ChemAxon IUPAC Name (2R,3R,4R,5R)-oxane-2,3,4,5-tetrol ChemAxon Traditional IUPAC Name β-D-ribopyranose ChemAxon Molecular Weight 150.1299 ChemAxon Monoisotopic Weight 150.05282343 ChemAxon SMILES O[C@@H]1CO[C@@H](O)[C@H](O)[C@@H]1O ChemAxon Molecular Formula C5H10O5 ChemAxon InChI InChI=1S/C5H10O5/c6-2-1-10-5(9)4(8)3(2)7/h2-9H,1H2/t2-,3-,4-,5-/m1/s1 ChemAxon InChIKey InChIKey=SRBFZHDQGSBBOR-TXICZTDVSA-N ChemAxon Polar Surface Area (PSA) 90.15 ChemAxon Refractivity 29.96 ChemAxon Polarizability 13.23 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 11.31 ChemAxon pKa (strongest basic) -3.5 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon ChEBI 27476 PDB RIP BE0001940 D-ribose-binding periplasmic protein Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown D-ribose-binding periplasmic protein Carbohydrate transport and metabolism Involved in the high-affinity D-ribose membrane transport system and also serves as the primary chemoreceptor for chemotaxis rbsB Periplasm None 7.76 30951.0 Escherichia coli (strain K12) GenBank Gene Database K00511 GenBank Protein Database 147519 UniProtKB P02925 UniProt Accession RBSB_ECOLI D-ribose-binding periplasmic protein precursor >D-ribose-binding periplasmic protein precursor MNMKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLV VLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKG EVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFN VLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFD GTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVKQ >891 bp ATGAACATGAAAAAACTGGCTACCCTGGTTTCCGCTGTTGCGCTAAGCGCCACCGTCAGT GCGAATGCGATGGCAAAAGACACCATCGCGCTGGTGGTCTCCACGCTTAACAACCCGTTT TTTGTATCGCTGAAAGATGGCGCGCAGAAAGAGGCGGATAAACTTGGCTATAACTTGGTG GTGCTGGACTCCCAGAACAACCCGGCGAAAGAGCTGGCGAACGTGCAGGACTTAACCGTT CGCGGCACAAAAATCCTGCTGATTAACCCGACCGACTCCGACGCAGTGGGTAATGCTGTG AAGATGGCTAACCAAGCGAACATCCCGGTTATCACTCTTGACCGCCAAGCAACGAAAGGT GAAGTGGTGAGCCACATTGCTTCTGATAACGTACTGGGCGGCAAAATCGCTGGTGATTAC ATCGCGAAGAAAGCGGGTGAAGGTGCAAAAGTTATCGAGCTGCAAGGCATTGCTGGTACA TCCGCAGCCCGTGAACGTGGCGAAGGCTTCCAGCAGGCCGTTGCTGCTCACAAGTTTAAT GTTCTTGCCAGCCAGCCAGCAGATTTTGATCGCATTAAAGGTTTGAACGTAATGCAGAAC CTGTTGACCGCTCATCCGGATGTTCAGGCTGTATTCGCGCAGAATGATGAAATGGCGCTG GGGGCGCTGCGCGCACTGCAAACTGCCGGTAAATCGGATGTGATGGTCGTCGGATTTGAC GGTACACCGGATGGCGAAAAAGCGGTGAATGATGGCAAACTGGCAGCGACTATCGCTCAG CTACCCGATCAGATTGGCGCGAAAGGCGTCGAAACCGCAGATAAAGTGCTGAAAGGCGAG AAAGTTCAGGCTAAGTATCCGGTTGATCTGAAACTGGTTGTTAAGCAGTAG PF00532 Peripla_BP_1 BE0001942 D-ribose pyranase Bacillus subtilis (strain 168) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown D-ribose pyranase Carbohydrate transport and metabolism Involved in the high-affinity ribose membrane transport system rbsD Cell membrane; peripheral membrane protein (Potential) None 4.95 14228.0 Bacillus subtilis (strain 168) GenBank Gene Database Z25798 GenBank Protein Database 397496 UniProtKB P36946 UniProt Accession RBSD_BACSU >High affinity ribose transport protein rbsD MKKHGILNSHLAKILADLGHTDKIVIADAGLPVPDGVLKIDLSLKPGLPAFQDTAAVLAE EMAVEKVIAAAEIKASNQENAKFLENLFSEQEIEYLSHEEFKLLTKDAKAVIRTGEFTPY ANCILQAGVLF >396 bp ATGAAAAAACACGGTATACTGAACAGCCATCTTGCCAAGATTTTAGCCGACCTTGGCCAC ACTGATAAAATTGTCATCGCGGATGCCGGACTGCCGGTTCCTGACGGCGTTTTGAAAATT GATCTTTCACTGAAGCCGGGCCTTCCGGCTTTCCAAGATACAGCGGCAGTACTGGCTGAG GAAATGGCGGTCGAAAAAGTCATTGCTGCAGCTGAAATAAAAGCATCCAATCAGGAGAAT GCGAAATTTCTAGAAAATCTTTTCTCTGAACAAGAGATTGAATACCTTTCTCACGAGGAG TTTAAGCTGCTGACAAAAGATGCAAAGGCAGTCATAAGAACAGGAGAATTCACACCATAT GCCAACTGCATCCTGCAGGCAGGTGTACTTTTCTAG PF05025 RbsD_FucU process transport process carbohydrate transport process physiological process process cellular physiological process "
drug:beta-D-Ribopyranoserdfs:label"beta-D-Ribopyranose"
drug:beta-D-Ribopyranoseowl:sameAsdrug:EXPT02787
drug:beta-D-Ribopyranoserdf:typedrugbank:drugs
drug:beta-L-fucosedrugbank:description" 2438-80-4 experimental This compound belongs to the hexoses. These are monosaccharides in which the sugar unit is a hexose. Hexoses Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Monosaccharides Oxanes Secondary Alcohols 1,2-Diols Hemiacetals Polyamines oxane hemiacetal polyol 1,2-diol secondary alcohol polyamine ether alcohol 6-Deoxy-Beta-L-Galactose logP -2.4 ALOGPS logS 0.7 ALOGPS Water Solubility 8.27e+02 g/l ALOGPS logP -1.9 ChemAxon IUPAC Name (2S,3S,4R,5S,6S)-6-methyloxane-2,3,4,5-tetrol ChemAxon Traditional IUPAC Name β-L-fucose ChemAxon Molecular Weight 164.1565 ChemAxon Monoisotopic Weight 164.068473494 ChemAxon SMILES C[C@@H]1O[C@H](O)[C@@H](O)[C@H](O)[C@@H]1O ChemAxon Molecular Formula C6H12O5 ChemAxon InChI InChI=1S/C6H12O5/c1-2-3(7)4(8)5(9)6(10)11-2/h2-10H,1H3/t2-,3+,4+,5-,6-/m0/s1 ChemAxon InChIKey InChIKey=SHZGCJCMOBCMKK-KGJVWPDLSA-N ChemAxon Polar Surface Area (PSA) 90.15 ChemAxon Refractivity 34.38 ChemAxon Polarizability 15.28 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 11.3 ChemAxon pKa (strongest basic) -3.6 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Melting Point 140 °C PhysProp ChEBI 42589 PDB FUL Wikipedia Fucose SMP00064 Fructose and Mannose Degradation DB01593 Zinc DB02263 Glyceraldehyde-3-Phosphate DB03283 beta-L-fucose DB04326 1,3-Dihydroxyacetonephosphate P15121 Q00796 Q9NRX4 P19367 P34949 Q92871 P17858 P09467 Q9Y5P6 P04075 O60547 Q13630 O14772 Q8N0W3 P50053 P60174 P16118 P05062 SMP00725 Fructose intolerance, hereditary DB01593 Zinc DB02263 Glyceraldehyde-3-Phosphate DB03283 beta-L-fucose DB04326 1,3-Dihydroxyacetonephosphate P15121 Q00796 Q9NRX4 P19367 P34949 Q92871 P17858 P09467 Q9Y5P6 P04075 O60547 Q13630 O14772 Q8N0W3 P50053 P60174 P16118 P05062 SMP00561 Fructosuria DB01593 Zinc DB02263 Glyceraldehyde-3-Phosphate DB03283 beta-L-fucose DB04326 1,3-Dihydroxyacetonephosphate P15121 Q00796 Q9NRX4 P19367 P34949 Q92871 P17858 P09467 Q9Y5P6 P04075 O60547 Q13630 O14772 Q8N0W3 P50053 P60174 P16118 P05062 BE0002483 Alpha-L-fucosidase, putative Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) unknown Alpha-L-fucosidase, putative Involved in alpha-L-fucosidase activity TM_0306 Cytoplasmic None 6.05 52206.0 Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) GenBank Gene Database AE000512 UniProtKB Q9WYE2 UniProt Accession Q9WYE2_THEMA >Alpha-L-fucosidase, putative MISMKPRYKPDWESLREHTVPKWFDKAKFGIFIHWGIYSVPGWATPTGELGKVPMDAWFF QNPYAEWYENSLRIKESPTWEYHVKTYGENFEYEKFADLFTAEKWDPQEWADLFKKAGAK YVIPTTKHHDGFCLWGTKYTDFNSVKRGPKRDLVGDLAKAVREAGLRFGVYYSGGLDWRF TTEPIRYPEDLSYIRPNTYEYADYAYKQVMELVDLYLPDVLWNDMGWPEKGKEDLKYLFA YYYNKHPEGSVNDRWGVPHWDFKTAEYHVNYPGDLPGYKWEFTRGIGLSFGYNRNEGPEH MLSVEQLVYTLVDVVSKGGNLLLNVGPKGDGTIPDLQKERLLGLGEWLRKYGDAIYGTSV WERCCAKTEDGTEIRFTRKCNRIFVIFLGIPTGEKIVIEDLNLSAGTVRHFLTGERLSFK NVGKNLEITVPKKLLETDSITLVLEAVEE >1350 bp ATGATTTCTATGAAACCCCGTTACAAACCTGACTGGGAATCTCTGAGGGAACACACAGTA CCGAAATGGTTCGACAAGGCGAAATTCGGGATCTTCATTCACTGGGGGATTTACTCTGTT CCGGGATGGGCGACGCCCACCGGAGAACTCGGTAAAGTGCCGATGGATGCCTGGTTCTTC CAGAATCCGTACGCAGAGTGGTACGAAAATTCCCTCAGGATCAAGGAGAGTCCCACCTGG GAATACCACGTGAAGACCTACGGAGAAAATTTCGAGTACGAGAAGTTTGCGGATCTTTTC ACCGCAGAGAAGTGGGATCCACAAGAGTGGGCTGATCTCTTCAAAAAAGCAGGAGCGAAG TACGTGATACCGACAACGAAACACCACGATGGATTTTGTCTGTGGGGGACGAAATACACA GATTTCAACTCCGTGAAGAGAGGACCGAAGAGAGATCTCGTAGGAGATCTTGCAAAAGCC GTAAGAGAAGCAGGATTGAGATTTGGAGTGTACTACTCAGGAGGTCTGGACTGGCGCTTC ACGACCGAGCCGATAAGATACCCCGAGGATCTCTCCTACATCAGGCCGAACACTTACGAG TACGCAGATTATGCCTACAAACAGGTCATGGAACTTGTGGATCTGTACCTTCCCGACGTT CTCTGGAACGACATGGGCTGGCCGGAGAAAGGAAAGGAAGACCTGAAGTATCTCTTCGCT TACTACTACAACAAACATCCAGAAGGTTCTGTGAACGACAGGTGGGGAGTGCCGCACTGG GATTTCAAAACGGCCGAGTACCACGTGAACTATCCGGGGGATCTGCCGGGCTACAAATGG GAGTTTACGAGGGGAATAGGGCTCTCTTTTGGATACAACCGAAACGAGGGGCCGGAACAC ATGCTCTCTGTTGAACAGCTCGTCTACACACTCGTGGACGTTGTGAGCAAGGGAGGAAAT CTCCTTTTGAACGTTGGGCCAAAGGGTGACGGAACGATTCCGGATCTGCAAAAAGAAAGA CTCCTGGGCCTTGGTGAATGGCTGAGAAAGTACGGAGATGCCATCTACGGTACTTCTGTC TGGGAAAGGTGCTGTGCGAAGACTGAGGATGGAACAGAGATCAGGTTCACCAGAAAATGT AACAGAATCTTTGTCATCTTTCTCGGTATCCCGACCGGAGAAAAAATTGTAATTGAGGAT CTCAATCTATCAGCAGGGACAGTGAGACATTTCCTGACGGGGGAGAGATTGAGCTTCAAA AATGTGGGAAAGAACCTGGAAATCACAGTACCCAAAAAGCTCCTTGAAACAGACAGCATA ACACTCGTGTTGGAGGCGGTGGAAGAATGA PF01120 Alpha_L_fucos function hydrolase activity function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function fucosidase activity function alpha-L-fucosidase activity function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process BE0000426 Acetylcholinesterase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Acetylcholinesterase Lipid transport and metabolism Rapidly hydrolyzes choline released into the synapse ACHE 7q22 Cytoplasmic None 6.24 67797.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:108 GenAtlas ACHE GeneCards ACHE GenBank Gene Database M55040 GenBank Protein Database 177975 UniProtKB P22303 UniProt Accession ACES_HUMAN Acetylcholinesterase precursor AChE EC 3.1.1.7 >Acetylcholinesterase precursor MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN QFDHYSKQDRCSDL >1845 bp ATGAGGCCCCCGCAGTGTCTGCTGCACACGCCTTCCCTGGCTTCCCCACTCCTTCTCCTC CTCCTCTGGCTCCTGGGTGGAGGAGTGGGGGCTGAGGGCCGGGAGGATGCAGAGCTGCTG GTGACGGTGCGTGGGGGCCGGCTGCGGGGCATTCGCCTGAAGACCCCCGGGGGCCCTGTC TCTGCTTTCCTGGGCATCCCCTTTGCGGAGCCACCCATGGGACCCCGTCGCTTTCTGCCA CCGGAGCCCAAGCAGCCTTGGTCAGGGGTGGTAGACGCTACAACCTTCCAGAGTGTCTGC TACCAATATGTGGACACCCTATACCCAGGTTTTGAGGGCACCGAGATGTGGAACCCCAAC CGTGAGCTGAGCGAGGACTGCCTGTACCTCAACGTGTGGACACCATACCCCCGGCCTACA TCCCCCACCCCTGTCCTCGTCTGGATCTATGGGGGTGGCTTCTACAGTGGGGCCTCCTCC TTGGACGTGTACGATGGCCGCTTCTTGGTACAGGCCGAGAGGACTGTGCTGGTGTCCATG AACTACCGGGTGGGAGCCTTTGGCTTCCTGGCCCTGCCGGGGAGCCGAGAGGCCCCGGGC AATGTGGGTCTCCTGGATCAGAGGCTGGCCCTGCAGTGGGTGCAGGAGAACGTGGCAGCC TTCGGGGGTGACCCGACATCAGTGACGCTGTTTGGGGAGAGCGCGGGAGCCGCCTCGGTG GGCATGCACCTGCTGTCCCCGCCCAGCCGGGGCCTGTTCCACAGGGCCGTGCTGCAGAGC GGTGCCCCCAATGGACCCTGGGCCACGGTGGGCATGGGAGAGGCCCGTCGCAGGGCCACG CAGCTGGCCCACCTTGTGGGCTGTCCTCCAGGCGGCACTGGTGGGAATGACACAGAGCTG GTAGCCTGCCTTCGGACACGACCAGCGCAGGTCCTGGTGAACCACGAATGGCACGTGCTG CCTCAAGAAAGCGTCTTCCGGTTCTCCTTCGTGCCTGTGGTAGATGGAGACTTCCTCAGT GACACCCCAGAGGCCCTCATCAACGCGGGAGACTTCCACGGCCTGCAGGTGCTGGTGGGT GTGGTGAAGGATGAGGGCTCGTATTTTCTGGTTTACGGGGCCCCAGGCTTCAGCAAAGAC AACGAGTCTCTCATCAGCCGGGCCGAGTTCCTGGCCGGGGTGCGGGTCGGGGTTCCCCAG GTAAGTGACCTGGCAGCCGAGGCTGTGGTCCTGCATTACACAGACTGGCTGCATCCCGAG GACCCGGCACGCCTGAGGGAGGCCCTGAGCGATGTGGTGGGCGACCACAATGTCGTGTGC CCCGTGGCCCAGCTGGCTGGGCGACTGGCTGCCCAGGGTGCCCGGGTCTACGCCTACGTC TTTGAACACCGTGCTTCCACGCTCTCCTGGCCCCTGTGGATGGGGGTGCCCCACGGCTAC GAGATCGAGTTCATCTTTGGGATCCCCCTGGACCCCTCTCGAAACTACACGGCAGAGGAG AAAATCTTCGCCCAGCGACTGATGCGATACTGGGCCAACTTTGCCCGCACAGGGGATCCC AATGAGCCCCGAGACCCCAAGGCCCCACAATGGCCCCCGTACACGGCGGGGGCTCAGCAG TACGTTAGTCTGGACCTGCGGCCGCTGGAGGTGCGGCGGGGGCTGCGCGCCCAGGCCTGC GCCTTCTGGAACCGCTTCCTCCCCAAATTGCTCAGCGCCACCGACACGCTCGACGAGGCG GAGCGCCAGTGGAAGGCCGAGTTCCACCGCTGGAGCTCCTACATGGTGCACTGGAAGAAC CAGTTCGACCACTACAGCAAGCAGGATCGCTGCTCAGACCTGTGA PF00135 COesterase function hydrolase activity, acting on ester bonds function carboxylic ester hydrolase activity function cholinesterase activity function catalytic activity function hydrolase activity "
drug:beta-L-fucoserdfs:label"beta-L-fucose"
drug:beta-L-fucoseowl:sameAsdrug:1,3-Dihydroxyacetonephosphate
drug:beta-L-fucoseowl:sameAsdrug:EXPT01510
drug:beta-L-fucoseowl:sameAsdrug:Glyceraldehyde-3-Phosphate
drug:beta-L-fucoseowl:sameAsdrug:Zinc
drug:beta-L-fucoseowl:sameAsdrug:beta-L-fucose
drug:beta-L-fucoserdf:typedrugbank:drugs
drug:beta-Naphthoflavonedrugbank:description"beta-Naphthoflavone, also known as 5,6-benzoflavone, is a potent agonist of the aryl hydrocarbon receptor and as such is an inducer of such detoxification enzymes as cytochromes P450 (CYPs) and uridine 5'-diphospho-glucuronosyltransferases (UGTs). β-Naphthoflavone is a putative chemopreventive agent."
drug:beta-Naphthoflavonedrugbank:drugCategorydrugcategory:Enzyme Inhibitors
drug:beta-Naphthoflavonerdfs:label"beta-Naphthoflavone"
drug:beta-Naphthoflavonerdf:typedrugbank:drugs
drug:beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamidedrugbank:description" experimental This compound belongs to the peptides. These are compounds containing an amide derived from two or more amino carboxylic acid molecules (the same or different) by formation of a covalent bond from the carbonyl carbon of one to the nitrogen atom of another. Peptides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Diphenylmethanes Alpha Amino Acid Amides Phenylpropylamines Amphetamines and Derivatives Pyrrolidinecarboxamides Tertiary Carboxylic Acid Amides Tertiary Amines Secondary Carboxylic Acid Amides Enolates Carboxylic Acids Polyamines Monoalkylamines diphenylmethane alpha-amino acid amide amphetamine or derivative phenylpropylamine alpha-amino acid or derivative pyrrolidine carboxylic acid or derivative pyrrolidine-2-carboxamide benzene pyrrolidine tertiary carboxylic acid amide carboxamide group secondary carboxylic acid amide tertiary amine enolate polyamine carboxylic acid primary aliphatic amine amine primary amine organonitrogen compound logP 2.6 ALOGPS logS -4.5 ALOGPS Water Solubility 1.27e-02 g/l ALOGPS logP 2.61 ChemAxon IUPAC Name (2S)-1-[(2R)-2-amino-3,3-diphenylpropanoyl]-N-propylpyrrolidine-2-carboxamide ChemAxon Traditional IUPAC Name (2S)-1-[(2R)-2-amino-3,3-diphenylpropanoyl]-N-propylpyrrolidine-2-carboxamide ChemAxon Molecular Weight 379.4953 ChemAxon Monoisotopic Weight 379.225977187 ChemAxon SMILES [H][C@@](N)(C(C1=CC=CC=C1)C1=CC=CC=C1)C(=O)N1CCC[C@@]1([H])C(=O)NCCC ChemAxon Molecular Formula C23H29N3O2 ChemAxon InChI InChI=1S/C23H29N3O2/c1-2-15-25-22(27)19-14-9-16-26(19)23(28)21(24)20(17-10-5-3-6-11-17)18-12-7-4-8-13-18/h3-8,10-13,19-21H,2,9,14-16,24H2,1H3,(H,25,27)/t19-,21+/m0/s1 ChemAxon InChIKey InChIKey=HZKKJPDVZGOOPU-PZJWPPBQSA-N ChemAxon Polar Surface Area (PSA) 75.43 ChemAxon Refractivity 110.66 ChemAxon Polarizability 42.21 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 15.59 ChemAxon pKa (strongest basic) 7.66 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 25271577 PubChem Substance 99443554 ChemSpider 23338407 PDB 44U BE0000048 Prothrombin Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Prothrombin Involved in blood clotting cascade Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C F2 11p11-q12 Secreted protein; extracellular space None 5.7 70037.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3535 GenAtlas F2 GeneCards F2 GenBank Gene Database M17262 GenBank Protein Database 339641 UniProtKB P00734 UniProt Accession THRB_HUMAN Activated Factor II [IIa] Coagulation factor II EC 3.4.21.5 Prothrombin precursor Thrombin >Prothrombin precursor MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY GFYTHVFRLKKWIQKVIDQFGE >1869 bp ATGGCGCACGTCCGAGGCTTGCAGCTGCCTGGCTGCCTGGCCCTGGCTGCCCTGTGTAGC CTTGTGCACAGCCAGCATGTGTTCCTGGCTCCTCAGCAAGCACGGTCGCTGCTCCAGCGG GTCCGGCGAGCCAACACCTTCTTGGAGGAGGTGCGCAAGGGCAACCTAGAGCGAGAGTGC GTGGAGGAGACGTGCAGCTACGAGGAGGCCTTCGAGGCTCTGGAGTCCTCCACGGCTACG GATGTGTTCTGGGCCAAGTACACAGCTTGTGAGACAGCGAGGACGCCTCGAGATAAGCTT GCTGCATGTCTGGAAGGTAACTGTGCTGAGGGTCTGGGTACGAACTACCGAGGGCATGTG AACATCACCCGGTCAGGCATTGAGTGCCAGCTATGGAGGAGTCGCTACCCACATAAGCCT GAAATCAACTCCACTACCCATCCTGGGGCCGACCTACAGGAGAATTTCTGCCGCAACCCC GACAGCAGCACCACGGGACCCTGGTGCTACACTACAGACCCCACCGTGAGGAGGCAGGAA TGCAGCATCCCTGTCTGTGGCCAGGATCAAGTCACTGTAGCGATGACTCCACGCTCCGAA GGCTCCAGTGTGAATCTGTCACCTCCATTGGAGCAGTGTGTCCCTGATCGGGGGCAGCAG TACCAGGGGCGCCTGGCGGTGACCACACATGGGCTCCCCTGCCTGGCCTGGGCCAGCGCA CAGGCCAAGGCCCTGAGCAAGCACCAGGACTTCAACTCAGCTGTGCAGCTGGTGGAGAAC TTCTGCCGCAACCCAGACGGGGATGAGGAGGGCGTGTGGTGCTATGTGGCCGGGAAGCCT GGCGACTTTGGGTACTGCGACCTCAACTATTGTGAGGAGGCCGTGGAGGAGGAGACAGGA GATGGGCTGGATGAGGACTCAGACAGGGCCATCGAAGGGCGTACCGCCACCAGTGAGTAC CAGACTTTCTTCAATCCGAGGACCTTTGGCTCGGGAGAGGCAGACTGTGGGCTGCGACCT CTGTTCGAGAAGAAGTCGCTGGAGGACAAAACCGAAAGAGAGCTCCTGGAATCCTACATC GACGGGCGCATTGTGGAGGGCTCGGATGCAGAGATCGGCATGTCACCTTGGCAGGTGATG CTTTTCCGGAAGAGTCCCCAGGAGCTGCTGTGTGGGGCCAGCCTCATCAGTGACCGCTGG GTCCTCACCGCCGCCCACTGCCTCCTGTACCCGCCCTGGGACAAGAACTTCACCGAGAAT GACCTTCTGGTGCGCATTGGCAAGCACTCCCGCACAAGGTACGAGCGAAACATTGAAAAG ATATCCATGTTGGAAAAGATCTACATCCACCCCAGGTACAACTGGCGGGAGAACCTGGAC CGGGACATTGCCCTGATGAAGCTGAAGAAGCCTGTTGCCTTCAGTGACTACATTCACCCT GTGTGTCTGCCCGACAGGGAGACGGCAGCCAGCTTGCTCCAGGCTGGATACAAGGGGCGG GTGACAGGCTGGGGCAACCTGAAGGAGACGTGGACAGCCAACGTTGGTAAGGGGCAGCCC AGTGTCCTGCAGGTGGTGAACCTGCCCATTGTGGAGCGGCCGGTCTGCAAGGACTCCACC CGGATCCGCATCACTGACAACATGTTCTGTGCTGGTTACAAGCCTGATGAAGGGAAACGA GGGGATGCCTGTGAAGGTGACAGTGGGGGACCCTTTGTCATGAAGAGCCCCTTTAACAAC CGCTGGTATCAAATGGGCATCGTCTCATGGGGTGAAGGCTGTGACCGGGATGGGAAATAT GGCTTCTACACACATGTGTTCCGCCTGAAGAAGTGGATACAGAAGGTCATTGATCAGTTT GGAGAGTAG PF00594 Gla PF00051 Kringle PF00089 Trypsin component extracellular region function catalytic activity function thrombin activity function hydrolase activity function calcium ion binding function peptidase activity function ion binding function endopeptidase activity function cation binding function serine-type endopeptidase activity function binding process blood coagulation process metabolism process macromolecule metabolism process protein metabolism process proteolysis process cellular protein metabolism process organismal physiological process process regulation of body fluids process physiological process process hemostasis "
drug:beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamiderdfs:label"beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamide"
drug:beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamiderdf:typedrugbank:drugs
drug:bis(4-hydroxyphenyl)methanonedrugbank:description" experimental This compound belongs to the benzophenones. These are organic compounds containing a ketone attached to two phenyl groups. Benzophenones Organic Compounds Benzenoids Benzene and Substituted Derivatives Benzophenones Diphenylmethanes Acetophenones Benzoyl Derivatives Phenols and Derivatives Ketones Enols Enolates Polyamines acetophenone benzoyl phenol derivative ketone enol polyamine enolate carbonyl group logP 2.77 ALOGPS logS -3 ALOGPS Water Solubility 1.90e-01 g/l ALOGPS logP 2.83 ChemAxon IUPAC Name 4-[(4-hydroxyphenyl)carbonyl]phenol ChemAxon Traditional IUPAC Name 4-[(4-hydroxyphenyl)carbonyl]phenol ChemAxon Molecular Weight 214.2167 ChemAxon Monoisotopic Weight 214.062994186 ChemAxon SMILES OC1=CC=C(C=C1)C(=O)C1=CC=C(O)C=C1 ChemAxon Molecular Formula C13H10O3 ChemAxon InChI InChI=1S/C13H10O3/c14-11-5-1-9(2-6-11)13(16)10-3-7-12(15)8-4-10/h1-8,14-15H ChemAxon InChIKey InChIKey=RXNYJUSEXLAVNQ-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 57.53 ChemAxon Refractivity 60.6 ChemAxon Polarizability 22.24 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 7.55 ChemAxon pKa (strongest basic) -6.9 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 69150 PubChem Substance 99444106 ChemSpider 62365 PDB DBE BE0001730 Lanosterol 14-alpha demethylase Mycobacterium tuberculosis # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Lanosterol 14-alpha demethylase Secondary metabolites biosynthesis, transport and catabolism Its precise biological substrate is not known. Catalyzes C14-demethylation of lanosterol, 24,25-dihydrolanosterol and obtusifoliol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene- 3-beta-ol cyp51 Cytoplasm None 5.71 50878.0 Mycobacterium tuberculosis GenBank Gene Database BX842574 GenBank Protein Database 1550642 UniProtKB P0A512 UniProt Accession CP51_MYCTU CYPLI EC 1.14.13.70 Lanosterol 14-alpha demethylase P450-14DM P450-LIA1 Sterol 14- alpha demethylase >Cytochrome P450 51 MSAVALPRVSGGHDEHGHLEEFRTDPIGLMQRVRDECGDVGTFQLAGKQVVLLSGSHANE FFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEMLHNAALRGEQMKGHAATIEDQ VRRMIADWGEAGEIDLLDFFAELTIYTSSACLIGKKFRDQLDGRFAKLYHELERGTDPLA YVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPR FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHA LRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFP DPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA QPPESYRNDHSKMVVQLAQPACVRYRRRTGV >1356 bp TTAAACTCCCGTTCGCCGGCGGTAGCGCACGCAAGCGGGCTGGGCCAACTGCACCACCAT CTTCGAATGGTCGTTACGATAGCTTTCTGGCGGTTGCGCCATCTCAAACTCATACTCGCG CAACAACACCGAGAAGATCGCTTTGATCTGCATGATGGCGAACGCCGCCCCCACGCAACG ATGCCGGCCGGCGCCGAACGGAATCCACGTCCAGCGGTTGAGCAGATCTTCCTGGCGCGG CTGCTCGTATCGTGCTGGCACGAAGTCGTGGGGATCGGGGAAGTCTTCGGGGATCCGGTT GGAGATCGCCGGGGAGGCCGCCACCAGATCGCCCTCATGAATCCGGTGGCCTTGCACCTC GAACTCGCCCTTGGCCACTCGCATGAGGATGATCAGCGGAGGGTGCAGGCGCAGCGTCTC TTTCAGCACGTTTTCCAGCTGCGGAATCTGGCGCAGCGCATGGAAACTCACCGATCGGCC GTCGCCGTACAGCTCGTCGAGTTCGTCGATCACGGCCGCGTAGGCGTCGCGATGGCGCAT CAACTCGATCAGCGTCCACGAAGCCGTACCCGAGCTGGTGTGATGGCCGGCGAACATCAT CGAGATGAACATGCCGGTGATCTCGTCGGCCGAGAACCGGGGAGTGCCGGTCTCAGCCTT GACGGCGATGAGCACGTCGAGCATGTCACGGTCGCTCTTGTCGGTGGGTGGGTTGGCGAT CCGGCCGTTCATGATGTCCGCAACCAGTGCCACCAGACCATTGCGGGCTTCGTCGCGGCG ACGGAAGCTCTCGATCGGCAGATACGGGTCGACGTAGGCTAGTGGGTCGGTGCCGCGCTC CAACTCGTGATAGAGCTTGGCGAATCGCCCGTCGAGCTGGTCGCGGAACTTCTTGCCGAT CAGGCAGGCCGAGGAGGTGTAGATGGTCAGCTCGGCGAAGAAGTCCAGCAGATCGATCTC GCCGGCCTCACCCCAGTCGGCGATCATCCGTCGGACTTGATCTTCGATGGTGGCAGCGTG GCCCTTCATCTGCTCGCCGCGTAGCGCGGCATTGTGCAGCATCTCTTTACGCCGTTCCGG GCTGGCGTCGAACACCACGCCCTCGCCGAAGATCGGCGTCATGAACGGGTATGCCTTGGC CTGGTCCAGGTCGTCGTCGCCCGCCCGGAAGAAGAATTCGTTGGCGTGCGAGCCGGACAG CAGCACGACCTGCTTCCCGGCCAGCTGGAAGGTACCGACGTCTCCGCATTCGTCGCGGAC CCGTTGCATCAGCCCGATCGGATCGGTGCGGAACTCCTCGAGGTGGCCGTGTTCGTCGTG GCCACCCGAAACCCGGGGTAGTGCAACAGCGCTCAT PF00067 p450 function tetrapyrrole binding function catalytic activity function heme binding function monooxygenase activity function oxidoreductase activity function ion binding function cation binding function transition metal ion binding function iron ion binding function binding process physiological process process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport "
drug:bis(4-hydroxyphenyl)methanonerdfs:label"bis(4-hydroxyphenyl)methanone"
drug:bis(4-hydroxyphenyl)methanonerdf:typedrugbank:drugs
drug:bis(4-nitrophenyl) hydrogen phosphatedrugbank:description" experimental This compound belongs to the nitrophenols and derivatives. These are compounds containing a nitrophenol moiety, which consists of a benzene ring bearing both an hydroxyl group and a nitro group on two different ring carbon atoms. Nitrophenols and Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenols and Derivatives Nitrobenzenes Organophosphate Esters Organic Phosphoric Acids Nitro Compounds Nitronic Acids Organic Oxoazanium Compounds Polyamines phosphoric acid ester organic phosphate nitronic acid nitro compound polyamine organic oxoazanium organonitrogen compound amine logP 2.08 ALOGPS logS -4.5 ALOGPS Water Solubility 1.16e-02 g/l ALOGPS logP 2.93 ChemAxon IUPAC Name bis(4-nitrophenoxy)phosphinic acid ChemAxon Traditional IUPAC Name bis(4-nitrophenoxy)phosphinic acid ChemAxon Molecular Weight 340.1822 ChemAxon Monoisotopic Weight 340.009651786 ChemAxon SMILES OP(=O)(OC1=CC=C(C=C1)[N+]([O-])=O)OC1=CC=C(C=C1)[N+]([O-])=O ChemAxon Molecular Formula C12H9N2O8P ChemAxon InChI InChI=1S/C12H9N2O8P/c15-13(16)9-1-5-11(6-2-9)21-23(19,20)22-12-7-3-10(4-8-12)14(17)18/h1-8H,(H,19,20) ChemAxon InChIKey InChIKey=MHSVUSZEHNVFKW-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 147.4 ChemAxon Refractivity 77.82 ChemAxon Polarizability 27.79 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 0.85 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 255 PubChem Substance 99443889 ChemSpider 250 PDB B4N BE0003865 Uncharacterized protein PA1000 Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Uncharacterized protein PA1000 Involved in hydrolase activity PA1000 None 5.25 34305.9 Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) GenBank Gene Database M33810 GenBank Protein Database 1196759 UniProtKB P20581 UniProt Accession Y1000_PSEAE >Uncharacterized protein PA1000 MLRLSAPGQLDDDLCLLGDVQVPVFLLRLGEASWALVEGGISRDAELVWADLCRWVADPS QVHYWLITHKHYDHCGLLPYLCPRLPNVQVLASERTCQAWKSESAVRVVERLNRQLLRAE QRLPEACAWDALPVRAVADGEWLELGPRHRLQVIEAHGHSDDHVVFYDVRRRRLFCGDAL GEFDEAEGVWRPLVFDDMEAYLESLERLQRLPTLLQLIPGHGGLLRGRLAADGAESAYTE CLRLCRRLLWRQSMGESLDELSEELHRAWGGQSVDFLPGELHLGSMRRMLEILSRQALPL D >906 bp ATGTTGAGGCTTTCGGCTCCCGGTCAACTGGATGATGACCTGTGCCTGTTGGGGGACGTC CAGGTGCCGGTGTTCCTGCTGCGTCTCGGTGAGGCGAGCTGGGCGCTGGTTGAAGGAGGG ATCAGCCGGGATGCCGAATTGGTTTGGGCGGACCTGTGCCGCTGGGTCGCCGACCCGTCC CAGGTGCACTACTGGCTGATCACCCACAAGCACTACGACCACTGCGGCCTGCTGCCCTAC CTGTGTCCGCGGCTGCCGAACGTACAGGTCCTGGCGTCCGAGCGGACCTGCCAGGCCTGG AAGTCGGAAAGCGCGGTGCGGGTGGTCGAGCGCTTGAACCGGCAACTGTTGCGTGCGGAG CAGCGGTTGCCCGAGGCCTGTGCCTGGGACGCTCTGCCGGTTCGCGCGGTGGCCGACGGC GAGTGGCTGGAGCTGGGACCGCGGCATCGCCTGCAGGTCATAGAGGCCCACGGCCACAGC GACGATCACGTGGTTTTCTACGACGTGCGACGCCGACGCCTGTTCTGCGGCGATGCCCTG GGCGAGTTCGACGAGGCAGAGGGGGTGTGGCGGCCGCTGGTGTTCGACGACATGGAGGCT TACCTGGAGTCCCTGGAACGTCTGCAGCGTCTGCCGACCCTGCTGCAACTGATCCCGGGA CACGGCGGCCTGCTGCGGGGGCGGCTGGCCGCGGATGGGGCCGAGTCGGCCTATACCGAG TGTCTGCGCCTGTGCCGGCGGTTGCTCTGGCGCCAGTCCATGGGCGAATCCCTCGACGAA CTGAGCGAGGAGCTGCACCGCGCCTGGGGTGGGCAGAGCGTCGACTTCCTGCCCGGCGAA CTGCACCTGGGGAGCATGCGCCGGATGCTGGAGATTCTCTCCCGCCAGGCGCTGCCTCTG GACTGA PF00753 Lactamase_B "
drug:bis(4-nitrophenyl) hydrogen phosphaterdfs:label"bis(4-nitrophenyl) hydrogen phosphate"
drug:bis(4-nitrophenyl) hydrogen phosphaterdf:typedrugbank:drugs
drug:bis(molybdopterin)tungsten cofactordrugbank:description" experimental tungsten-molybdopterin W-molybdopterin cofactor logP -3.1 ChemAxon IUPAC Name magnesium(2+) ion bis([(5aS,8S,9aS)-2-amino-4-oxo-8-[(phosphonatooxy)methyl]-6-sulfanidyl-1H,4H,5H,5aH,8H,9aH,10H-pyrano[3,2-g]pteridin-7-yl]sulfanide) tungsten ChemAxon Traditional IUPAC Name magnesium bis([(5aS,8S,9aS)-2-amino-4-oxo-8-[(phosphonatooxy)methyl]-6-sulfanidyl-1H,5H,5aH,8H,9aH,10H-pyrano[3,2-g]pteridin-7-yl]sulfanide) tungsten ChemAxon Molecular Weight 990.79 ChemAxon Monoisotopic Weight 989.897996389 ChemAxon SMILES [Mg++].[W].NC1=NC(=O)C2=C(N[C@H]3O[C@@H](COP([O-])([O-])=O)C([S-])=C([S-])[C@H]3N2)N1.NC1=NC(=O)C2=C(N[C@H]3O[C@@H](COP([O-])([O-])=O)C([S-])=C([S-])[C@H]3N2)N1 ChemAxon Molecular Formula C20H20MgN10O12P2S4W ChemAxon InChI InChI=1S/2C10H14N5O6PS2.Mg.W/c2*11-10-14-7-4(8(16)15-10)12-3-6(24)5(23)2(21-9(3)13-7)1-20-22(17,18)19;;/h2*2-3,9,12,23-24H,1H2,(H2,17,18,19)(H4,11,13,14,15,16);;/q;;+2;/p-8/t2*2-,3+,9-;;/m00../s1 ChemAxon InChIKey InChIKey=DMQGNSGNJQBKMK-QPNRVYIWSA-F ChemAxon Polar Surface Area (PSA) 173.19 ChemAxon Refractivity 98.01 ChemAxon Polarizability 33.73 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 10 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 1.2 ChemAxon pKa (strongest basic) 3.13 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 6 ChemAxon Bioavailability 1 ChemAxon MDDR-Like Rule true ChemAxon ChEBI 30402 PubChem Compound 46936218 PubChem Substance 46506611 ChemSpider 4573846 PDB PTT "
drug:bis(molybdopterin)tungsten cofactorrdfs:label"bis(molybdopterin)tungsten cofactor"
drug:bis(molybdopterin)tungsten cofactorowl:sameAsdrug:EXPT02688
drug:bis(molybdopterin)tungsten cofactorrdf:typedrugbank:drugs
drug:cat hair allergenic extractsdrugbank:description"Cat hair allergenic extracts vaccine is developed by Greer Laboratories for the treatment of allergic reaction and allergic rhinitis. This vaccine has completed phase I of clinical trial."
drug:cat hair allergenic extractsrdfs:label"cat hair allergenic extracts"
drug:cat hair allergenic extractsrdf:typedrugbank:drugs
drug:corticotropin-releasing factordrugbank:description"Corticotropin-releasing factor is studied in the treatment of brain cancer. It is made naturally by the hypothalamus (a part of the brain) and can also be made in the laboratory. Human corticotropin-releasing factor may help reduce symptoms caused by edema (swelling) of the brain. It is a type of neurohormone, also called hCRF."
drug:corticotropin-releasing factordrugbank:interactsWithdrug:Heparin
drug:corticotropin-releasing factorrdfs:label"corticotropin-releasing factor"
drug:corticotropin-releasing factorowl:sameAsdrug:Heparin
drug:corticotropin-releasing factorrdf:typedrugbank:drugs
drug:cryopreserved human liver cellsdrugbank:description"Vesta Therapeutics is a privately held company developing cell therapeutics for liver repair and regeneration. The Company's technology is centered on the isolation, expansion, and cryopreservation of liver cells (human hepatocytes) obtained from organ donor livers that are not suitable for whole organ transplantation. "
drug:cryopreserved human liver cellsrdfs:label"cryopreserved human liver cells"
drug:cryopreserved human liver cellsrdf:typedrugbank:drugs
drug:cyclic 3',5'-thymidine monophosphatedrugbank:description" experimental This compound belongs to the pyrimidine nucleosides and analogues. These are compounds comprising a pyrimidine base attached to a sugar. Pyrimidine Nucleosides and Analogues Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Glycosyl Compounds Pyrimidones Organic Phosphoric Acids Organophosphate Esters Hydropyrimidines Dihydrofurans Ethers Polyamines pyrimidone hydropyrimidine organic phosphate pyrimidine phosphoric acid ester dihydrofuran polyamine ether amine organonitrogen compound 2',3'-dehydro-2',3'-deoxy-thymidine 5'-monophosphate 2',3'-dideoxy-2',3-didehydrothymidine 5'-monophosphate 3',5'-Cyclic dtmp cTMP Cyclic tmp D4T-MP d4TMP logP -0.98 ALOGPS logS -1.8 ALOGPS Water Solubility 4.64e+00 g/l ALOGPS logP -0.36 ChemAxon IUPAC Name {[(2S,5R)-5-(5-methyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-1-yl)-2,5-dihydrofuran-2-yl]methoxy}phosphonic acid ChemAxon Traditional IUPAC Name [(2S,5R)-5-(5-methyl-2,4-dioxo-3H-pyrimidin-1-yl)-2,5-dihydrofuran-2-yl]methoxyphosphonic acid ChemAxon Molecular Weight 304.1932 ChemAxon Monoisotopic Weight 304.046037292 ChemAxon SMILES [H][C@]1(COP(O)(O)=O)O[C@]([H])(C=C1)N1C=C(C)C(=O)NC1=O ChemAxon Molecular Formula C10H13N2O7P ChemAxon InChI InChI=1S/C10H13N2O7P/c1-6-4-12(10(14)11-9(6)13)8-3-2-7(19-8)5-18-20(15,16)17/h2-4,7-8H,5H2,1H3,(H,11,13,14)(H2,15,16,17)/t7-,8+/m0/s1 ChemAxon InChIKey InChIKey=XLPGURCDSRIXFL-JGVFFNPUSA-N ChemAxon Polar Surface Area (PSA) 125.4 ChemAxon Refractivity 66.19 ChemAxon Polarizability 25.93 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 1.24 ChemAxon pKa (strongest basic) -4.2 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 461278 PubChem Substance 46508608 ChemSpider 405848 PDB D4M BE0001515 5'(3')-deoxyribonucleotidase, mitochondrial Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown 5'(3')-deoxyribonucleotidase, mitochondrial Involved in nucleotidase activity Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP NT5M 17p11.2 Mitochondrion None 8.12 25862.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:15769 GenAtlas NT5M GeneCards NT5M GenBank Gene Database AJ277557 GenBank Protein Database 9408106 UniProtKB Q9NPB1 UniProt Accession NT5M_HUMAN 5',3'-nucleotidase, mitochondrial 5'(3')-deoxyribonucleotidase, mitochondrial precursor Deoxy-5'-nucleotidase 2 dNT-2 EC 3.1.3.- >5'(3')-deoxyribonucleotidase, mitochondrial precursor MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC >687 bp ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC ATTCTGGACAGCAAGCGGCCCTGCTGA PF06941 NT5C "
drug:cyclic 3',5'-thymidine monophosphaterdfs:label"cyclic 3',5'-thymidine monophosphate"
drug:cyclic 3',5'-thymidine monophosphaterdf:typedrugbank:drugs
drug:dehydroepiandrosterone sulfatedrugbank:description"DHEA sulfate is the major steroid of the fetal adrenal. DHEA-S is the principal adrenal androgen and is secreted together with cortisol under the control of ACTH and prolactin. DHEA-S is elevated with hyperprolactinemia."
drug:dehydroepiandrosterone sulfaterdfs:label"dehydroepiandrosterone sulfate"
drug:dehydroepiandrosterone sulfaterdf:typedrugbank:drugs
drug:deoxycytidylyl-3',5'-guanosinedrugbank:description" 52474-59-6 experimental This compound belongs to the purine ribonucleoside monophosphates. These are nucleotides consisting of a purine base linked to a ribose to which one monophosphate group is attached. Purine Ribonucleoside Monophosphates Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Glycosyl Compounds Pyrimidine Nucleosides and Analogues Other Disaccharides Hypoxanthines Pyrimidones Aminopyrimidines and Derivatives Primary Aromatic Amines N-substituted Imidazoles Organic Phosphoric Acids Hydropyrimidines Organophosphate Esters Oxolanes Tetrahydrofurans Secondary Alcohols Primary Alcohols Ethers Polyamines pentose disaccharide disaccharide hypoxanthine imidazopyrimidine purine aminopyrimidine pyrimidone primary aromatic amine hydropyrimidine phosphoric acid ester n-substituted imidazole organic phosphate pyrimidine imidazole tetrahydrofuran azole oxolane secondary alcohol polyamine primary alcohol ether alcohol organonitrogen compound amine primary amine Humans and other mammals logP -2.2 ALOGPS logS -2.3 ALOGPS Water Solubility 2.91e+00 g/l ALOGPS logP -3.2 ChemAxon IUPAC Name {[(2S,3R,5R)-5-(4-amino-2-oxo-1,2-dihydropyrimidin-1-yl)-2-(hydroxymethyl)oxolan-3-yl]oxy}({[(2S,3R,5R)-5-(2-amino-6-oxo-6,9-dihydro-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy})phosphinic acid ChemAxon Traditional IUPAC Name [(2S,3R,5R)-5-(4-amino-2-oxopyrimidin-1-yl)-2-(hydroxymethyl)oxolan-3-yl]oxy[(2S,3R,5R)-5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxyphosphinic acid ChemAxon Molecular Weight 556.4232 ChemAxon Monoisotopic Weight 556.143125572 ChemAxon SMILES NC1=NC2=C(N=CN2[C@H]2C[C@@H](O)[C@H](CO[P@@](O)(=O)O[C@@H]3C[C@@H](O[C@H]3CO)N3C=CC(N)=NC3=O)O2)C(=O)N1 ChemAxon Molecular Formula C19H25N8O10P ChemAxon InChI InChI=1S/C19H25N8O10P/c20-12-1-2-26(19(31)23-12)14-4-9(10(5-28)35-14)37-38(32,33)34-6-11-8(29)3-13(36-11)27-7-22-15-16(27)24-18(21)25-17(15)30/h1-2,7-11,13-14,28-29H,3-6H2,(H,32,33)(H2,20,23,31)(H3,21,24,25,30)/t8-,9-,10+,11+,13-,14-/m1/s1 ChemAxon InChIKey InChIKey=OBCJQWSXSLYWHI-BSTSDWCZSA-N ChemAxon Polar Surface Area (PSA) 258.67 ChemAxon Refractivity 123.24 ChemAxon Polarizability 50.02 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 13 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) 2.04 ChemAxon pKa (strongest basic) 1.4 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 5 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 46936643 PubChem Substance 46504759 PDB CGP BE0003317 Ribonuclease pancreatic Human # Listgarten JN, Maes D, Wyns L, Aguilar CF, Palmer RA: Structure of the crystalline complex of deoxycytidylyl-3',5'-guanosine (3',5'-dCpdG) cocrystallized with ribonuclease at 1.9 A resolution. Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):767-71. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15299807 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Ribonuclease pancreatic Involved in nucleic acid binding Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA RNASE1 14q11.2 Secreted protein None 8.94 17644.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:10044 GenAtlas RNASE1 GenBank Gene Database D26129 UniProtKB P07998 UniProt Accession RNAS1_HUMAN EC 3.1.27.5 HP-RNase RIB-1 Ribonuclease pancreatic precursor RNase 1 RNase A RNase UpI-1 >Ribonuclease pancreatic MALEKSLVRLLLLVLILLVLGWVQPSLGKESRAKKFQRQHMDSDSSPSSSSTYCNQMMRR RNMTQGRCKPVNTFVHEPLVDVQNVCFQEKVTCKNGQGNCYKSNSSMHITDCRLTNGSRY PNCAYRTSPKERHIIVACEGSPYVPVHFDASVEDST >471 bp ATGGCTCTGGAGAAGTCTCTTGTCCGGCTCCTTCTGCTTGTCCTGATACTGCTGGTGCTG GGCTGGGTCCAGCCTTCCCTGGGCAAGGAATCCCGGGCCAAGAAATTCCAGCGGCAGCAT ATGGACTCAGACAGTTCCCCCAGCAGCAGCTCCACCTACTGTAACCAAATGATGAGGCGC CGGAATATGACACAGGGGCGGTGCAAACCAGTGAACACCTTTGTGCACGAGCCCCTGGTA GATGTCCAGAATGTCTGTTTCCAGGAAAAGGTCACCTGCAAGAACGGGCAGGGCAACTGC TACAAGAGCAACTCCAGCATGCACATCACAGACTGCCGCCTGACAAACGGCTCCAGGTAC CCCAACTGTGCATACCGGACCAGCCCGAAGGAGAGACACATCATTGTGGCCTGTGAAGGG AGCCCATATGTGCCAGTCCACTTTGATGCTTCTGTGGAGGACTCTACCTAA PF00074 RnaseA function hydrolase activity function nucleic acid binding function hydrolase activity, acting on ester bonds function nuclease activity function endonuclease activity function endoribonuclease activity function endoribonuclease activity, producing 3'-phosphomonoesters function pancreatic ribonuclease activity function binding function catalytic activity "
drug:deoxycytidylyl-3',5'-guanosinerdfs:label"deoxycytidylyl-3',5'-guanosine"
drug:deoxycytidylyl-3',5'-guanosineowl:sameAsdrug:EXPT00901
drug:deoxycytidylyl-3',5'-guanosinerdf:typedrugbank:drugs
drug:desmethylprodinedrugbank:description"Desmethylprodine, a derivative of meperidine, is an opioid analgesic with the potency of morphine. It has been listed as a Schedule I controlled drug in the United States, and thus is not used clinically. It is known to be a designer drug, synthesized in 1977, for the purpose of recreational use. Illicit manufacturing has occurred. "
drug:desmethylprodinerdfs:label"desmethylprodine"
drug:desmethylprodinerdf:typedrugbank:drugs
drug:diethyl [(1R)-1,5-diaminopentyl]boronatedrugbank:description" experimental This compound belongs to the boronic acid esters. These are compounds comprising the boronic acid ester functional group RN(X)OR' (R,R'=alkyl,aryl; X= any O,N,Hal residue). Boronic Acid Esters Organic Compounds Organic Acids and Derivatives Boronic Acid Derivatives Boronic Acid Esters Polyamines Organoboron Compounds Monoalkylamines polyamine primary amine primary aliphatic amine organonitrogen compound amine organoboron compound organic metalloid moeity logP 0.85 ALOGPS logS -1.5 ALOGPS Water Solubility 6.26e+00 g/l ALOGPS logP 1.76 ChemAxon IUPAC Name diethyl [(1R)-1,5-diaminopentyl]boronate ChemAxon Traditional IUPAC Name diethyl (1R)-1,5-diaminopentylboronate ChemAxon Molecular Weight 202.102 ChemAxon Monoisotopic Weight 202.185258456 ChemAxon SMILES [H][C@](N)(CCCCN)B(OCC)OCC ChemAxon Molecular Formula C9H23BN2O2 ChemAxon InChI InChI=1S/C9H23BN2O2/c1-3-13-10(14-4-2)9(12)7-5-6-8-11/h9H,3-8,11-12H2,1-2H3/t9-/m0/s1 ChemAxon InChIKey InChIKey=FYUGRVWDCBMIQX-VIFPVBQESA-N ChemAxon Polar Surface Area (PSA) 70.5 ChemAxon Refractivity 54.13 ChemAxon Polarizability 25.13 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest basic) 10.26 ChemAxon Physiological Charge 2 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937028 PubChem Substance 99443311 PDB 0AY BE0001739 Trypsin-1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Trypsin-1 Involved in protease activity Preferential cleavage:Arg-|-Xaa, Lys-|-Xaa PRSS1 7q32-qter|7q34 Secreted protein; extracellular space None 6.48 26558.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9475 GenAtlas PRSS1 GeneCards PRSS1 GenBank Gene Database M22612 GenBank Protein Database 521216 UniProtKB P07477 UniProt Accession TRY1_HUMAN Cationic trypsinogen EC 3.4.21.4 Serine protease 1 Trypsin I Trypsin-1 precursor >Trypsin-1 precursor MNPLLILTFVAAALAAPFDDDDKIVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVS AGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVIN ARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKIT SNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIK NTIAANS >744 bp ATGAATCCACTCCTGATCCTTACCTTTGTGGCAGCTGCTCTTGCTGCCCCCTTTGATGAT GATGACAAGATCGTTGGGGGCTACAACTGTGAGGAGAATTCTGTCCCCTACCAGGTGTCC CTGAATTCTGGCTACCACTTCTGTGGTGGCTCCCTCATCAACGAACAGTGGGTGGTATCA GCAGGCCACTGCTACAAGTCCCGCATCCAGGTGAGACTGGGAGAGCACAACATCGAAGTC CTGGAGGGGAATGAGCAGTTCATCAATGCAGCCAAGATCATCCGCCACCCCCAATACGAC AGGAAGACTCTGAACAATGACATCATGTTAATCAAGCTCTCCTCACGTGCAGTAATCAAC GCCCGCGTGTCCACCATCTCTCTGCCCACCGCCCCTCCAGCCACTGGCACGAAGTGCCTC ATCTCTGGCTGGGGCAACACTGCGAGCTCTGGCGCCGACTACCCAGACGAGCTGCAGTGC CTGGATGCTCCTGTGCTGAGCCAGGCTAAGTGTGAAGCCTCCTACCCTGGAAAGATTACC AGCAACATGTTCTGTGTGGGCTTCCTTGAGGGAGGCAAGGATTCATGTCAGGGTGATTCT GGTGGCCCTGTGGTCTGCAATGGACAGCTCCAAGGAGTTGTCTCCTGGGGTGATGGCTGT GCCCAGAAGAACAAGCCTGGAGTCTACACCAAGGTCTACAACTACGTGAAATGGATTAAG AACACCATAGCTGCCAATAGCTAA PF00089 Trypsin function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function hydrolase activity process protein metabolism process cellular protein metabolism process proteolysis process physiological process process metabolism process macromolecule metabolism "
drug:diethyl [(1R)-1,5-diaminopentyl]boronaterdfs:label"diethyl [(1R)-1,5-diaminopentyl]boronate"
drug:diethyl [(1R)-1,5-diaminopentyl]boronaterdf:typedrugbank:drugs
drug:difluoro(5-{2-[(5-octyl-1H-pyrrol-2-yl-kappaN)methylidene]-2H-pyrrol-5-yl-kappaN}pentanoato)borondrugbank:description" experimental This compound belongs to the substituted pyrroles. These are heterocyclic compounds containing a pyrrole ring substituted at one or more positions. Substituted Pyrroles Organic Compounds Heterocyclic Compounds Pyrroles Substituted Pyrroles Unsaturated Fatty Acids Polyamines Enolates Carboxylic Acids carboxylic acid derivative enolate carboxylic acid polyamine organonitrogen compound logP 3.88 ALOGPS logS -5.8 ALOGPS Water Solubility 6.89e-04 g/l ALOGPS logP 0.56 ChemAxon IUPAC Name 12-(4-carboxybutyl)-2,2-difluoro-4-octyl-1$l^{5},3-diaza-2-boratricyclo[7.3.0.0^{3,7}]dodeca-1(12),4,6,8,10-pentaen-1-ylium-2-uide ChemAxon Traditional IUPAC Name 12-(4-carboxybutyl)-2,2-difluoro-4-octyl-1$l^{5},3-diaza-2-boratricyclo[7.3.0.0^{3,7}]dodeca-1(12),4,6,8,10-pentaen-1-ylium-2-uide ChemAxon Molecular Weight 404.302 ChemAxon Monoisotopic Weight 404.244665122 ChemAxon SMILES CCCCCCCCC1=CC=C2C=C3C=CC(CCCCC(O)=O)=[N+]3[B-](F)(F)N12 ChemAxon Molecular Formula C22H31BF2N2O2 ChemAxon InChI InChI=1S/C22H31BF2N2O2/c1-2-3-4-5-6-7-10-18-13-15-20-17-21-16-14-19(11-8-9-12-22(28)29)27(21)23(24,25)26(18)20/h13-17H,2-12H2,1H3,(H,28,29) ChemAxon InChIKey InChIKey=JNKJCLYKBRBEKW-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 45.24 ChemAxon Refractivity 115.15 ChemAxon Polarizability 45.8 ChemAxon Rotatable Bond Count 12 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 4.53 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 46937076 PubChem Substance 99443980 PDB C08 BE0000215 Peroxisome proliferator-activated receptor gamma Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Peroxisome proliferator-activated receptor gamma Involved in DNA binding Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis PPARG 3p25 Nucleus None 5.77 57621.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9236 GenAtlas PPARG GeneCards PPARG GenBank Gene Database U79012 GenBank Protein Database 1711117 IUPHAR 595 Guide to Pharmacology 86 UniProtKB P37231 UniProt Accession PPARG_HUMAN PPAR-gamma >Peroxisome proliferator-activated receptor gamma MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSF DIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKT QLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNC RIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLR ALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQE QSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLAS LMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVII LSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQL LQVIKKTETDMSLHPLLQEIYKDLY >1518 bp ATGGGTGAAACTCTGGGAGATTCTCCTATTGACCCAGAAAGCGATTCCTTCACTGATACA CTGTCTGCAAACATATCACAAGAAATGACCATGGTTGACACAGAGATGCCATTCTGGCCC ACCAACTTTGGGATCAGCTCCGTGGATCTCTCCGTAATGGAAGACCACTCCCACTCCTTT GATATCAAGCCCTTCACTACTGTTGACTTCTCCAGCATTTCTACTCCACATTACGAAGAC ATTCCATTCACAAGAACAGATCCAGTGGTTGCAGATTACAAGTATGACCTGAAACTTCAA GAGTACCAAAGTGCAATCAAAGTGGAGCCTGCATCTCCACCTTATTATTCTGAGAAGACT CAGCTCTACAATAAGCCTCATGAAGAGCCTTCCAACTCCCTCATGGCAATTGAATGTCGT GTCTGTGGAGATAAAGCTTCTGGATTTCACTATGGAGTTCATGCTTGTGAAGGATGCAAG GGTTTCTTCCGGAGAACAATCAGATTGAAGCTTATCTATGACAGATGTGATCTTAACTGT CGGATCCACAAAAAAAGTAGAAATAAATGTCAGTACTGTCGGTTTCAGAAATGCCTTGCA GTGGGGATGTCTCATAATGCCATCAGGTTTGGGCGGATGCCACAGGCCGAGAAGGAGAAG CTGTTGGCGGAGATCTCCAGTGATATCGACCAGCTGAATCCAGAGTCCGCTGACCTCCGG GCCCTGGCAAAACATTTGTATGACTCATACATAAAGTCCTTCCCGCTGACCAAAGCAAAG GCGAGGGCGATCTTGACAGGAAAGACAACAGACAAATCACCATTCGTTATCTATGACATG AATTCCTTAATGATGGGAGAAGATAAAATCAAGTTCAAACACATCACCCCCCTGCAGGAG CAGAGCAAAGAGGTGGCCATCCGCATCTTTCAGGGCTGCCAGTTTCGCTCCGTGGAGGCT GTGCAGGAGATCACAGAGTATGCCAAAAGCATTCCTGGTTTTGTAAATCTTGACTTGAAC GACCAAGTAACTCTCCTCAAATATGGAGTCCACGAGATCATTTACACAATGCTGGCCTCC TTGATGAATAAAGATGGGGTTCTCATATCCGAGGGCCAAGGCTTCATGACAAGGGAGTTT CTAAAGAGCCTGCGAAAGCCTTTTGGTGACTTTATGGAGCCCAAGTTTGAGTTTGCTGTG AAGTTCAATGCACTGGAATTAGATGACAGCGACTTGGCAATATTTATTGCTGTCATTATT CTCAGTGGAGACCGCCCAGGTTTGCTGAATGTGAAGCCCATTGAAGACATTCAAGACAAC CTGCTACAAGCCCTGGAGCTCCAGCTGAAGCTGAACCACCCTGAGTCCTCACAGCTGTTT GCCAAGCTGCTCCAGAAAATGACAGACCTCAGACAGATTGTCACGGAACACGTGCAGCTA CTGCAGGTGATCAAGAAGACGGAGACAGACATGAGTCTTCACCCGCTCCTGCAGGAGATC TACAAGGACTTGTACTAG PF00104 Hormone_recep PF00105 zf-C4 component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function steroid hormone receptor activity function transcription factor activity function ligand-dependent nuclear receptor activity function DNA binding function binding function signal transducer activity function receptor activity function nucleic acid binding process regulation of biological process process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent "
drug:difluoro(5-{2-[(5-octyl-1H-pyrrol-2-yl-kappaN)methylidene]-2H-pyrrol-5-yl-kappaN}pentanoato)boronrdfs:label"difluoro(5-{2-[(5-octyl-1H-pyrrol-2-yl-kappaN)methylidene]-2H-pyrrol-5-yl-kappaN}pentanoato)boron"
drug:difluoro(5-{2-[(5-octyl-1H-pyrrol-2-yl-kappaN)methylidene]-2H-pyrrol-5-yl-kappaN}pentanoato)boronrdf:typedrugbank:drugs
drug:dimethyl (1R,4S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylatedrugbank:description" experimental This compound belongs to the stilbenes. These are organic compounds containing a 1,2-diphenylethylene moiety. Stilbenes (C6-C2-C6 ) are derived from the common phenylpropene (C6-C3) skeleton building block. The introduction of one or more hydroxyl groups to a phenyl ring lead to stilbenoids. Stilbenes Organic Compounds Phenylpropanoids and Polyketides Stilbenes Phenols and Derivatives Dicarboxylic Acids and Derivatives Dihydrofurans Polyols Carboxylic Acid Esters Enolates Ethers Polyamines Enols phenol derivative benzene dicarboxylic acid derivative dihydrofuran polyol carboxylic acid ester ether enol polyamine enolate carboxylic acid derivative logP 2.64 ALOGPS logS -4.6 ALOGPS Water Solubility 9.42e-03 g/l ALOGPS logP 3.01 ChemAxon IUPAC Name 2,3-dimethyl (1S,4R)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylate ChemAxon Traditional IUPAC Name 2,3-dimethyl (1S,4R)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylate ChemAxon Molecular Weight 394.3741 ChemAxon Monoisotopic Weight 394.10525293 ChemAxon SMILES [H][C@]12O[C@]([H])(C(C(=O)OC)=C1C(=O)OC)C(=C2C1=CC=C(O)C=C1)C1=CC=C(O)C=C1 ChemAxon Molecular Formula C22H18O7 ChemAxon InChI InChI=1S/C22H18O7/c1-27-21(25)17-18(22(26)28-2)20-16(12-5-9-14(24)10-6-12)15(19(17)29-20)11-3-7-13(23)8-4-11/h3-10,19-20,23-24H,1-2H3/t19-,20+ ChemAxon InChIKey InChIKey=CRLQCBACIMUGDZ-BGYRXZFFSA-N ChemAxon Polar Surface Area (PSA) 102.29 ChemAxon Refractivity 103.3 ChemAxon Polarizability 40.03 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 8.91 ChemAxon pKa (strongest basic) -4.3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 11531308 PubChem Substance 99444403 ChemSpider 9706091 PDB HZ3 BE0000123 Estrogen receptor Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Estrogen receptor Involved in transcription factor activity Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues ESR1 6q25.1 Nucleus None 8.14 66217.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3467 GenAtlas ESR1 GeneCards ESR1 GenBank Gene Database X03635 GenBank Protein Database 31234 IUPHAR 620 Guide to Pharmacology 107 UniProtKB P03372 UniProt Accession ESR1_HUMAN ER ER-alpha Estradiol receptor >Estrogen receptor MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAY EFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPF LQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAK ETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQAC RLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKR SKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINW AKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEG MVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLD KITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLL LEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV >1788 bp ATGACCATGACCCTCCACACCAAAGCATCTGGGATGGCCCTACTGCATCAGATCCAAGGG AACGAGCTGGAGCCCCTGAACCGTCCGCAGCTCAAGATCCCCCTGGAGCGGCCCCTGGGC GAGGTGTACCTGGACAGCAGCAAGCCCGCCGTGTACAACTACCCCGAGGGCGCCGCCTAC GAGTTCAACGCCGCGGCCGCCGCCAACGCGCAGGTCTACGGTCAGACCGGCCTCCCCTAC GGCCCCGGGTCTGAGGCTGCGGCGTTCGGCTCCAACGGCCTGGGGGGTTTCCCCCCACTC AACAGCGTGTCTCCGAGCCCGCTGATGCTACTGCACCCGCCGCCGCAGCTGTCGCCTTTC CTGCAGCCCCACGGCCAGCAGGTGCCCTACTACCTGGAGAACGAGCCCAGCGGCTACACG GTGCGCGAGGCCGGCCCGCCGGCATTCTACAGGCCAAATTCAGATAATCGACGCCAGGGT GGCAGAGAAAGATTGGCCAGTACCAATGACAAGGGAAGTATGGCTATGGAATCTGCCAAG GAGACTCGCTACTGTGCAGTGTGCAATGACTATGCTTCAGGCTACCATTATGGAGTCTGG TCCTGTGAGGGCTGCAAGGCCTTCTTCAAGAGAAGTATTCAAGGACATAACGACTATATG TGTCCAGCCACCAACCAGTGCACCATTGATAAAAACAGGAGGAAGAGCTGCCAGGCCTGC CGGCTCCGCAAATGCTACGAAGTGGGAATGATGAAAGGTGGGATACGAAAAGACCGAAGA GGAGGGAGAATGTTGAAACACAAGCGCCAGAGAGATGATGGGGAGGGCAGGGGTGAAGTG GGGTCTGCTGGAGACATGAGAGCTGCCAACCTTTGGCCAAGCCCGCTCATGATCAAACGC TCTAAGAAGAACAGCCTGGCCTTGTCCCTGACGGCCGACCAGATGGTCAGTGCCTTGTTG GATGCTGAGCCCCCCATACTCTATTCCGAGTATGATCCTACCAGACCCTTCAGTGAAGCT TCGATGATGGGCTTACTGACCAACCTGGCAGACAGGGAGCTGGTTCACATGATCAACTGG GCGAAGAGGGTGCCAGGCTTTGTGGATTTGACCCTCCATGATCAGGTCCACCTTCTAGAA TGTGCCTGGCTAGAGATCCTGATGATTGGTCTCGTCTGGCGCTCCATGGAGCACCCAGTG AAGCTACTGTTTGCTCCTAACTTGCTCTTGGACAGGAACCAGGGAAAATGTGTAGAGGGC ATGGTGGAGATCTTCGACATGCTGCTGGCTACATCATCTCGGTTCCGCATGATGAATCTG CAGGGAGAGGAGTTTGTGTGCCTCAAATCTATTATTTTGCTTAATTCTGGAGTGTACACA TTTCTGTCCAGCACCCTGAAGTCTCTGGAAGAGAAGGACCATATCCACCGAGTCCTGGAC AAGATCACAGACACTTTGATCCACCTGATGGCCAAGGCAGGCCTGACCCTGCAGCAGCAG CACCAGCGGCTGGCCCAGCTCCTCCTCATCCTCTCCCACATCAGGCACATGAGTAACAAA GGCATGGAGCATCTGTACAGCATGAAGTGCAAGAACGTGGTGCCCCTCTATGACCTGCTG CTGGAGATGCTGGACGCCCACCGCCTACATGCGCCCACTAGCCGTGGAGGGGCATCCGTG GAGGAGACGGACCAAAGCCACTTGGCCACTGCGGGCTCTACTTCATCGCATTCCTTGCAA AAGTATTACATCACGGGGGAGGCAGAGGGTTTCCCTGCCACAGTCTGA PF00104 Hormone_recep PF00105 zf-C4 PF02159 Oest_recep component intracellular membrane-bound organelle component nucleus component organelle component membrane-bound organelle function signal transducer activity function receptor activity function nucleic acid binding function binding function steroid hormone receptor activity function ion binding function transcription factor activity function steroid binding function cation binding function ligand-dependent nuclear receptor activity function transition metal ion binding function DNA binding function zinc ion binding process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent process regulation of biological process process regulation of physiological process process regulation of metabolism BE0003740 Nuclear receptor coactivator 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Nuclear receptor coactivator 2 Involved in nuclear hormone receptor binding Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF- 2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues NCOA2 8q13.3 Nucleus None 6.62 159155.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:7669 GeneCards NCOA2 GenBank Gene Database X97674 GenBank Protein Database 1877215 UniProtKB Q15596 UniProt Accession NCOA2_HUMAN hTIF2 NCoA-2 Transcriptional intermediary factor 2 >Nuclear receptor coactivator 2 MSGMGENTSDPSRAETRKRKECPDQLGPSPKRNTEKRNREQENKYIEELAELIFANFNDI DNFNFKPDKCAILKETVKQIRQIKEQEKAAAANIDEVQKSDVSSTGQGVIDKDALGPMML EALDGFFFVVNLEGNVVFVSENVTQYLRYNQEELMNKSVYSILHVGDHTEFVKNLLPKSI VNGGSWSGEPPRRNSHTFNCRMLVKPLPDSEEEGHDNQEAHQKYETMQCFAVSQPKSIKE EGEDLQSCLICVARRVPMKERPVLPSSESFTTRQDLQGKITSLDTSTMRAAMKPGWEDLV RRCIQKFHAQHEGESVSYAKRHHHEVLRQGLAFSQIYRFSLSDGTLVAAQTKSKLIRSQT TNEPQLVISLHMLHREQNVCVMNPDLTGQTMGKPLNPISSNSPAHQALCSGNPGQDMTLS SNINFPINGPKEQMGMPMGRFGGSGGMNHVSGMQATTPQGSNYALKMNSPSQSSPGMNPG QPTSMLSPRHRMSPGVAGSPRIPPSQFSPAGSLHSPVGVCSSTGNSHSYTNSSLNALQAL SEGHGVSLGSSLASPDLKMGNLQNSPVNMNPPPLSKMGSLDSKDCFGLYGEPSEGTTGQA ESSCHPGEQKETNDPNLPPAVSSERADGQSRLHDSKGQTKLLQLLTTKSDQMEPSPLASS LSDTNKDSTGSLPGSGSTHGTSLKEKHKILHRLLQDSSSPVDLAKLTAEATGKDLSQESS STAPGSEVTIKQEPVSPKKKENALLRYLLDKDDTKDIGLPEITPKLERLDSKTDPASNTK LIAMKTEKEEMSFEPGDQPGSELDNLEEILDDLQNSQLPQLFPDTRPGAPAGSVDKQAII NDLMQLTAENSPVTPVGAQKTALRISQSTFNNPRPGQLGRLLPNQNLPLDITLQSPTGAG PFPPIRNSSPYSVIPQPGMMGNQGMIGNQGNLGNSSTGMIGNSASRPTMPSGEWAPQSSA VRVTCAATTSAMNRPVQGGMIRNPAASIPMRPSSQPGQRQTLQSQVMNIGPSELEMNMGG PQYSQQQAPPNQTAPWPESILPIDQASFASQNRQPFGSSPDDLLCPHPAAESPSDEGALL DQLYLALRNFDGLEEIDRALGIPELVSQSQAVDPEQFSSQDSNIMLEQKAPVFPQQYASQ AQMAQGSYSPMQDPNFHTMGQRPSYATLRMQPRPGLRPTGLVQNQPNQLRLQLQHRLQAQ QNRQPLMNQISNVSNVNLTLRPGVPTQAPINAQMLAQRQREILNQHLRQRQMHQQQQVQQ RTLMMRGQGLNMTPSMVAPSGMPATMSNPRIPQANAQQFPFPPNYGISQQPDPGFTGATT PQSPLMSPRMAHTQSPMMQQSQANPAYQAPSDINGWAQGNMGGNSMFSQQSPPHFGQQAN TSMYSNNMNINVSMATNTGGMSSMNQMTGQISMTSVTSVPTSGLSSMGPEQVNDPALRGG NLFPNQLPGMDMIKQEGDTTRKYC >4395 bp ATGAGTGGGATGGGAGAAAATACCTCTGACCCCTCCAGGGCAGAGACAAGAAAGCGCAAG GAATGTCCTGACCAACTTGGACCCAGCCCCAAAAGGAACACTGAAAAACGTAATCGTGAA CAGGAAAATAAATATATAGAAGAACTTGCAGAGTTGATTTTTGCAAATTTTAATGATATA GACAACTTTAACTTCAAACCTGACAAATGTGCAATCTTAAAAGAAACTGTGAAGCAAATT CGTCAGATCAAAGAACAAGAGAAAGCAGCAGCTGCCAACATAGATGAAGTGCAGAAGTCA GATGTATCCTCTACAGGGCAGGGTGTCATCGACAAGGATGCGCTGGGGCCTATGATGCTT GAGGCCCTTGATGGGTTCTTCTTTGTAGTGAACCTGGAAGGCAACGTTGTGTTTGTGTCA GAGAATGTGACACAGTATCTAAGGTATAACCAAGAAGAGCTGATGAACAAAAGTGTATAT AGCATCTTGCATGTTGGGGACCACACGGAATTTGTCAAAAACCTGCTGCCAAAGTCTATA GTAAATGGGGGATCTTGGTCTGGCGAACCTCCGAGGCGGAACAGCCATACCTTCAATTGT CGGATGCTGGTAAAACCTTTACCTGATTCAGAAGAGGAGGGTCATGATAACCAGGAAGCT CATCAGAAATATGAAACTATGCAGTGCTTCGCTGTCTCTCAACCAAAGTCCATCAAAGAA GAAGGAGAAGATTTGCAGTCCTGCTTGATTTGCGTGGCAAGAAGAGTTCCCATGAAGGAA AGACCAGTTCTTCCCTCATCAGAAAGTTTTACTACTCGCCAGGATCTCCAAGGCAAGATC ACGTCTCTGGATACCAGCACCATGAGAGCAGCCATGAAACCAGGCTGGGAGGACCTGGTA AGAAGGTGTATTCAGAAGTTCCATGCGCAGCATGAAGGAGAATCTGTGTCCTATGCTAAG AGGCATCATCATGAAGTACTGAGACAAGGATTGGCATTCAGTCAAATCTATCGTTTTTCC TTGTCTGATGGCACTCTTGTTGCTGCACAAACGAAGAGCAAACTCATCCGTTCTCAGACT ACTAATGAACCTCAACTTGTAATATCTTTACATATGCTTCACAGAGAGCAGAATGTGTGT GTGATGAATCCGGATCTGACTGGACAAACGATGGGGAAGCCACTGAATCCAATTAGCTCT AACAGCCCTGCCCATCAGGCCCTGTGCAGTGGGAACCCAGGTCAGGACATGACCCTCAGT AGCAATATAAATTTTCCCATAAATGGCCCAAAGGAACAAATGGGCATGCCCATGGGCAGG TTTGGTGGTTCTGGGGGAATGAACCATGTGTCAGGCATGCAAGCAACCACTCCTCAGGGT AGTAACTATGCACTCAAAATGAACAGCCCCTCACAAAGCAGCCCTGGCATGAATCCAGGA CAGCCCACCTCCATGCTTTCACCAAGGCATCGCATGAGCCCTGGAGTGGCTGGCAGCCCT CGAATCCCACCCAGTCAGTTTTCCCCTGCAGGAAGCTTGCATTCCCCTGTGGGAGTTTGC AGCAGCACAGGAAATAGCCATAGTTATACCAACAGCTCCCTCAATGCACTTCAGGCCCTC AGCGAGGGGCACGGGGTCTCATTAGGGTCATCGTTGGCTTCACCAGACCTAAAAATGGGC AATTTGCAAAACTCCCCAGTTAATATGAATCCTCCCCCACTCAGCAAGATGGGAAGCTTG GACTCAAAAGACTGTTTTGGACTATATGGGGAGCCCTCTGAAGGTACAACTGGACAAGCA GAGAGCAGCTGCCATCCTGGAGAGCAAAAGGAAACAAATGACCCCAACCTGCCCCCGGCC GTGAGCAGTGAGAGAGCTGACGGGCAGAGCAGACTGCATGACAGCAAAGGGCAGACCAAA CTCCTGCAGCTGCTGACCACCAAATCTGATCAGATGGAGCCCTCGCCCTTAGCCAGCTCT TTGTCGGATACAAACAAAGACTCCACAGGTAGCTTGCCTGGTTCTGGGTCTACACATGGA ACCTCGCTCAAGGAGAAGCATAAAATTTTGCACAGACTCTTGCAGGACAGCAGTTCCCCT GTGGACTTGGCCAAGTTAACAGCAGAAGCCACAGGCAAAGACCTGAGCCAGGAGTCCAGC AGCACAGCTCCTGGATCAGAAGTGACTATTAAACAAGAGCCGGTGAGCCCCAAGAAGAAA GAGAATGCACTACTTCGCTATTTGCTAGATAAAGATGATACTAAAGATATTGGTTTACCA GAAATAACCCCCAAACTTGAGAGACTGGACAGTAAGACAGATCCTGCCAGTAACACAAAA TTAATAGCAATGAAAACTGAGAAGGAGGAGATGAGCTTTGAGCCTGGTGACCAGCCTGGC AGTGAGCTGGACAACTTGGAGGAGATTTTGGATGATTTGCAGAATAGTCAATTACCACAG CTTTTCCCAGACACGAGGCCAGGCGCCCCTGCTGGATCAGTTGACAAGCAAGCCATCATC AATGACCTCATGCAACTCACAGCTGAAAACAGCCCTGTCACACCTGTTGGAGCCCAGAAA ACAGCACTGCGAATTTCACAGAGCACTTTTAATAACCCACGACCAGGGCAACTGGGCAGG TTATTGCCAAACCAGAATTTACCACTTGACATCACATTGCAAAGCCCAACTGGTGCTGGA CCTTTCCCACCAATCAGAAACAGTAGTCCCTACTCAGTGATACCTCAGCCAGGAATGATG GGTAATCAAGGGATGATAGGAAACCAAGGAAATTTAGGGAACAGTAGCACAGGAATGATT GGTAACAGTGCTTCTCGGCCTACTATGCCATCTGGAGAATGGGCACCGCAGAGTTCGGCT GTGAGAGTCACCTGTGCTGCTACCACCAGTGCCATGAACCGGCCAGTCCAAGGAGGTATG ATTCGGAACCCAGCAGCCAGCATCCCCATGAGGCCCAGCAGCCAGCCTGGCCAAAGACAG ACGCTTCAGTCTCAGGTCATGAATATAGGGCCATCTGAATTAGAGATGAACATGGGGGGA CCTCAGTATAGCCAACAACAAGCTCCTCCAAATCAGACTGCCCCATGGCCTGAAAGCATC CTGCCTATAGACCAGGCGTCTTTTGCCAGCCAAAACAGGCAGCCATTTGGCAGTTCTCCA GATGACTTGCTATGTCCACATCCTGCAGCTGAGTCTCCGAGTGATGAGGGAGCTCTCCTG GACCAGCTGTATCTGGCCTTGCGGAATTTTGATGGCCTGGAGGAGATTGATAGAGCCTTA GGAATACCCGAACTGGTCAGCCAGAGCCAAGCAGTAGATCCAGAACAGTTCTCAAGTCAG GATTCCAACATCATGCTGGAGCAGAAGGCGCCCGTTTTCCCACAGCAGTATGCATCTCAG GCACAAATGGCCCAGGGTAGCTATTCTCCCATGCAAGATCCAAACTTTCACACCATGGGA CAGCGGCCTAGTTATGCCACACTCCGTATGCAGCCCAGACCGGGCCTCAGGCCCACGGGC CTAGTGCAGAACCAGCCAAATCAACTAAGACTTCAACTTCAGCATCGCCTCCAAGCACAG CAGAATCGCCAGCCACTTATGAATCAAATCAGCAATGTTTCCAATGTGAACTTGACTCTG AGGCCTGGAGTACCAACACAGGCACCTATTAATGCACAGATGCTGGCCCAGAGACAGAGG GAAATCCTGAACCAGCATCTTCGACAGAGACAAATGCATCAGCAACAGCAAGTTCAGCAA CGAACTTTGATGATGAGAGGACAAGGGTTGAATATGACACCAAGCATGGTGGCTCCTAGT GGTATGCCAGCAACTATGAGCAACCCTCGGATTCCCCAGGCAAATGCACAGCAGTTTCCA TTTCCTCCAAACTACGGAATAAGTCAGCAACCTGATCCAGGCTTTACTGGGGCTACGACT CCCCAGAGCCCACTTATGTCACCCCGAATGGCACATACACAGAGTCCCATGATGCAACAG TCTCAGGCCAACCCAGCCTATCAGGCCCCCTCCGACATAAATGGATGGGCGCAGGGGAAC ATGGGCGGAAACAGCATGTTTTCCCAGCAGTCCCCACCACACTTTGGGCAGCAAGCAAAC ACCAGCATGTACAGTAACAACATGAACATCAATGTGTCCATGGCGACCAACACAGGTGGC ATGAGCAGCATGAACCAGATGACAGGACAGATCAGCATGACCTCAGTGACCTCCGTGCCT ACGTCAGGGCTGTCCTCCATGGGTCCCGAGCAGGTTAATGATCCTGCTCTGAGGGGAGGC AACCTGTTCCCAAACCAGCTGCCTGGAATGGATATGATTAAGCAGGAGGGAGACACAACA CGGAAATATTGCTGA PF00989 PAS PF07469 DUF1518 PF08815 Nuc_rec_co-act PF08832 SRC-1 component organelle component membrane-bound organelle component intracellular membrane-bound organelle component nucleus function protein binding function signal transducer activity function transcription factor binding function transcription regulator activity function transcription cofactor activity function transcription coactivator activity function binding process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent process cellular process process cell communication process signal transduction process regulation of biological process process regulation of physiological process process regulation of metabolism "
drug:dimethyl (1R,4S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylaterdfs:label"dimethyl (1R,4S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylate"
drug:dimethyl (1R,4S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylaterdf:typedrugbank:drugs
drug:dioxothiomolybdenum(VI) iondrugbank:description" experimental This compound belongs to the transition metal oxides. These are inorganic compounds containing an oxygen atom of an oxidation state of -2, in which the heaviest atom bonded to the oxygen is a transition metal. Transition Metal Oxides Inorganic Compounds Mixed Metal/Non-metal Compounds Transition Metal Organides Transition Metal Oxides logP -0.3 ChemAxon IUPAC Name molybdenumoylthiol ChemAxon Traditional IUPAC Name molybdenumoylthiol ChemAxon Molecular Weight 161.01 ChemAxon Monoisotopic Weight 162.875132812 ChemAxon SMILES S[Mo](=O)=O ChemAxon Molecular Formula HMoO2S ChemAxon InChI InChI=1S/Mo.2O.H2S/h;;;1H2/q+1;;;/p-1 ChemAxon InChIKey InChIKey=BDSRWPHSAKXXRG-UHFFFAOYSA-M ChemAxon Polar Surface Area (PSA) 34.14 ChemAxon Refractivity 9.44 ChemAxon Polarizability 7.48 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 8.65 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 5162682 PubChem Substance 46508283 ChemSpider 21542383 PDB MOS BE0002204 Xanthine dehydrogenase/oxidase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Xanthine dehydrogenase/oxidase Nucleotide transport and metabolism This enzyme can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups XDH 2p23.1 Peroxisome None 7.7 146426.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:12805 GenAtlas XDH GeneCards XDH GenBank Gene Database D11456 GenBank Protein Database 10336525 UniProtKB P47989 UniProt Accession XDH_HUMAN EC 1.17.1.4 EC 1.17.3.2 Xanthine oxidase XD XO >Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDR LQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGI VMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCC MNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQAS TLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFG AACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISD LNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSA FKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKE ELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLD PTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRY ENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDK VTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDL KKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKM LGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGR HPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGR LCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKL EGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGA LLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAA SVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLG YSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAF VQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAV GEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVT GVPENCKPWSVRV >4002 bp ATGACAGCAGACAAATTGGTTTTCTTTGTGAATGGCAGAAAGGTGGTGGAGAAAAATGCA GATCCAGAGACAACCCTTTTGGCCTACCTGAGAAGAAAGTTGGGGCTGAGTGGAACCAAG CTCGGCTGTGGAGAGGGGGGCTGCGGGGCTTGCACAGTGATGCTCTCCAAGTATGATCGT CTGCAGAACAAGATCGTCCACTTTTCTGCCAATGCCTGCCTGGCCCCCATCTGCTCCTTG CACCATGTTGCAGTGACAACTGTGGAAGGAATAGGAAGCACCAAGACGAGGCTGCATCCT GTGCAGGAGAGAATTGCCAAAAGCCACGGCTCCCAGTGCGGGTTCTGCACCCCTGGCATC GTCATGAGTATGTACACACTGCTCCGGAATCAGCCCGAGCCCACCATGGAGGAGATTGAG AATGCCTTCCAAGGAAATCTGTGCCGCTGCACAGGCTACAGACCCATCCTCCAGGGCTTC CGGACCTTTGCCAGGGATGGTGGATGCTGTGGAGGAGATGGGAATAATCCAAATTGCTGC ATGAACCAGAAGAAAGACCACTCAGTCAGCCTCTCGCCATCTTTATTCAAACCAGAGGAG TTCACGCCCCTGGATCCAACCCAGGAGCCCATTTTTCCCCCAGAGTTGCTGAGGCTGAAA GACACTCCTCGGAAGCAGCTGCGATTTGAAGGGGAGCGTGTGACGTGGATACAGGCCTCA ACCCTCAAGGAGCTGCTGGACCTCAAGGCTCAGCACCCTGACGCCAAGCTGGTCGTGGGG AACACGGAGATTGGCATTGAGATGAAGTTCAAGAATATGCTGTTTCCTATGATTGTCTGC CCAGCCTGGATCCCTGAGCTGAATTCGGTAGAACATGGACCCGACGGTATCTCCTTTGGA GCTGCTTGCCCCCTGAGCATTGTGGAAAAAACCCTGGTGGATGCTGTTGCTAAGCTTCCT GCCCAAAAGACAGAGGTGTTCAGAGGGGTCCTGGAGCAGCTGCGCTGGTTTGCTGGGAAG CAAGTCAAGTCTGTGGCGTCCGTTGGAGGGAACATCATCACTGCCAGCCCCATCTCCGAC CTCAACCCCGTGTTCATGGCCAGTGGGGCCAAGCTGACACTTGTGTCCAGAGGCACCAGG AGAACTGTCCAGATGGACCACACCTTCTTCCCTGGCTACAGAAAGACCCTGCTGAGCCCG GAGGAGATACTGCTCTCCATAGAGATCCCCTACAGCAGGGAGGGGGAGTATTTCTCAGCA TTCAAGCAGGCCTCCCGGAGAGAAGATGACATTGCCAAGGTAACCAGTGGCATGAGAGTT TTATTCAAGCCAGGAACCACAGAGGTACAGGAGCTGGCCCTTTGCTATGGTGGAATGGCC AACAGAACCATCTCAGCCCTCAAGACCACTCAGAGGCAGCTTTCCAAGCTCTGGAAGGAG GAGCTGCTGCAGGACGTGTGTGCAGGACTGGCAGAGGAGCTGCATCTGCCTCCCGATGCC CCTGGTGGCATGGTGGACTTCCGGTGCACCCTCACCCTCAGCTTCTTCTTCAAGTTCTAC CTGACAGTCCTTCAGAAGCTGGGCCAAGAGAACCTGGAAGACAAGTGTGGTAAACTGGAC CCCACTTTCGCCAGTGCAACTTTACTGTTTCAGAAAGACCCCCCAGCCGATGTCCAGCTC TTCCAAGAGGTGCCCAAGGGTCAGTCTGAGGAGGACATGGTGGGCCGGCCCCTGCCCCAC CTGGCAGCGGACATGCAGGCCTCTGGTGAGGCCGTGTACTGTGACGACATTCCTCGCTAC GAGAATGAGCTGTCTCTCCGGCTGGTCACCAGCACCCGGGCCCACGCCAAGATCAAGTCC ATAGATACATCAGAAGCTAAGAAGGTTCCAGGGTTTGTTTGTTTCATTTCCGCTGATGAT GTTCCTGGGAGTAACATAACTGGAATTTGTAATGATGAGACAGTCTTTGCGAAGGATAAG GTTACTTGTGTTGGGCATATCATTGGTGCTGTGGTTGCTGACACCCCGGAACACACACAG AGAGCTGCCCAAGGGGTGAAAATCACCTATGAAGAACTACCAGCCATTATCACAATTGAG GATGCTATAAAGAACAACTCCTTTTATGGACCTGAGCTGAAGATCGAGAAAGGGGACCTA AAGAAGGGGTTTTCCGAAGCAGATAATGTTGTGTCAGGGGAGATATACATCGGTGGCCAA GAGCACTTCTACCTGGAGACTCACTGCACCATTGCTGTTCCAAAAGGCGAGGCAGGGGAG ATGGAGCTCTTTGTGTCTACACAGAACACCATGAAGACCCAGAGCTTTGTTGCAAAAATG TTGGGGGTTCCAGCAAACCGGATTGTGGTTCGAGTGAAGAGAATGGGAGGAGGCTTTGGA GGCAAGGAGACCCGGAGCACTGTGGTGTCCACGGCAGTGGCCCTGGCTGCATATAAGACC GGCCGCCCTGTGCGATGCATGCTGGACCGTGATGAGGACATGCTGATAACTGGTGGCAGA CATCCCTTCCTGGCCAGATACAAGGTTGGCTTCATGAAGACTGGGACAGTTGTGGCTCTT GAGGTGGACCACTTCAGCAATGTGGGGAACACCCAGGATCTCTCTCAGAGTATTATGGAA CGAGCTTTATTCCACATGGACAACTGCTATAAAATCCCCAACATCCGGGGCACTGGGCGG CTGTGCAAAACCAACCTTCCCTCCAACACGGCCTTCCGGGGCTTTGGGGGGCCCCAGGGG ATGCTCATTGCCGAGTGCTGGATGAGTGAAGTTGCAGTGACCTGTGGGATGCCTGCAGAG GAGGTGCGGAGAAAAAACCTGTACAAAGAAGGGGACCTGACACACTTCAACCAGAAGCTT GAGGGTTTCACCTTGCCCAGATGCTGGGAAGAATGCCTAGCAAGCTCTCAGTATCATGCT CGGAAGAGTGAGGTTGACAAGTTCAACAAGGAGAATTGTTGGAAAAAGAGAGGATTGTGC ATAATTCCCACCAAGTTTGGAATAAGCTTCACAGTTCCTTTTCTGAATCAGGCAGGAGCC CTACTTCATGTGTACACAGATGGCTCTGTGCTGCTGACCCACGGGGGGACTGAGATGGGC CAAGGCCTTCATACCAAAATGGTCCAGGTGGCCAGTAGAGCTCTGAAAATCCCCACCTCT AAGATTTATATCAGCGAGACAAGCACTAACACTGTGCCCAACACCTCTCCCACGGCTGCC TCTGTCAGCGCTGACCTCAATGGACAGGCCGTCTATGCGGCTTGTCAGACCATCTTGAAA AGGCTGGAACCCTACAAGAAGAAGAATCCCAGTGGCTCCTGGGAAGACTGGGTCACAGCT GCCTACATGGACACAGTGAGCTTGTCTGCCACTGGGTTTTATAGAACACCCAATCTGGGC TACAGCTTTGAGACTAACTCAGGGAACCCCTTCCACTACTTCAGCTATGGGGTGGCTTGC TCTGAAGTAGAAATCGACTGCCTAACAGGAGATCATAAGAACCTCCGCACAGATATTGTC ATGGATGTTGGCTCCAGTCTAAACCCTGCCATTGATATTGGACAGGTGGAAGGGGCATTT GTCCAGGGCCTTGGCCTCTTCACCCTAGAGGAGCTACACTATTCCCCCGAGGGGAGCCTG CACACCCGTGGCCCTAGCACCTACAAGATCCCGGCATTTGGCAGCATCCCCATTGAGTTC AGGGTGTCCCTGCTCCGCGACTGCCCCAACAAGAAGGCCATCTATGCATCGAAGGCTGTT GGAGAGCCGCCCCTCTTCCTGGCTGCTTCTATCTTCTTTGCCATCAAAGATGCCATCCGT GCAGCTCGAGCTCAGCACACAGGTAATAACGTGAAGGAACTCTTCCGGCTAGACAGCCCT GCCACCCCGGAGAAGATCCGCAATGCCTGCGTGGACAAGTTCACCACCCTGTGTGTCACT GGTGTCCCAGAAAACTGCAAACCCTGGTCTGTGAGGGTCTAA PF00111 Fer2 PF01315 Ald_Xan_dh_C PF02738 Ald_Xan_dh_C2 PF01799 Fer2_2 PF03450 CO_deh_flav_C PF00941 FAD_binding_5 function oxidoreductase activity function ion binding function cation binding function transition metal ion binding function iron ion binding function transporter activity function binding function electron transporter activity function catalytic activity function metal ion binding process physiological process process generation of precursor metabolites and energy process electron transport process metabolism process cellular metabolism "
drug:dioxothiomolybdenum(VI) ionrdfs:label"dioxothiomolybdenum(VI) ion"
drug:dioxothiomolybdenum(VI) ionowl:sameAsdrug:EXPT02214
drug:dioxothiomolybdenum(VI) ionrdf:typedrugbank:drugs
drug:doxorubicin TransDrugdrugbank:description"Doxorubicin Transdrug(R) is an investigational drug to treat hepatocellular carcinoma (HCC), primary liver cancer."
drug:doxorubicin TransDrugdrugbank:interactsWithdrug:Telithromycin
drug:doxorubicin TransDrugdrugbank:interactsWithdrug:Terbinafine
drug:doxorubicin TransDrugrdfs:label"doxorubicin TransDrug"
drug:doxorubicin TransDrugowl:sameAsdrug:Telithromycin
drug:doxorubicin TransDrugowl:sameAsdrug:Terbinafine
drug:doxorubicin TransDrugrdf:typedrugbank:drugs
drug:dust mite allergen extractsdrugbank:description"Dust mite allergen extracts is new allergy vaccine which is currently under clinical evaluation for the prevention or relief of symptoms caused by specific dust mite. It consists of a 50:50 mixture of the mite Dermatophagoides pteronyssinus and D. farinae protein derived from aqueous extracts of the mites which is chemically modified by glutaraldehyde and adsorbed onto -tyrosine with addition of the immunostimulatory adjuvant, monophosphoryl lipid A “Polymite�. "
drug:dust mite allergen extractsrdfs:label"dust mite allergen extracts"
drug:dust mite allergen extractsrdf:typedrugbank:drugs
drug:eiRNAdrugbank:description"eiRNA (expressed interfering RNA) is an approach to RNAi therapeutics, whereby a plasmid DNA coding for desired dsRNA is delivered to diseased cells enabling the cells to carry out dsRNA production internally thereby invoking the RNAi response against a targeted disease causing gene."
drug:eiRNArdfs:label"eiRNA"
drug:eiRNArdf:typedrugbank:drugs
drug:ethyl 3-[(E)-2-amino-1-cyanoethenyl]-6,7-dichloro-1-methyl-1H-indole-2-carboxylatedrugbank:description" experimental This compound belongs to the indolecarboxylic acids and derivatives. These are compounds containing a carboxylic acid group (or a derivative thereof) linked to an indole. Indolecarboxylic Acids and Derivatives Organic Compounds Heterocyclic Compounds Indoles and Derivatives Indolecarboxylic Acids and Derivatives Alpha Amino Acids and Derivatives Indoles Pyrrole Carboxylic Acids and Derivatives Chlorobenzenes N-methylpyrroles Aryl Chlorides Carboxylic Acid Esters Enamines Dialkyl Ethers Enolates Nitriles Polyamines Organochlorides alpha-amino acid or derivative indole pyrrole-2-carboxylic acid or derivative chlorobenzene n-methylpyrrole benzene substituted pyrrole n-substituted pyrrole aryl halide aryl chloride pyrrole carboxylic acid ester enolate nitrile carbonitrile ether enamine dialkyl ether polyamine carboxylic acid derivative organonitrogen compound organochloride amine organohalogen logP 3.53 ALOGPS logS -4 ALOGPS Water Solubility 3.59e-02 g/l ALOGPS logP 3.01 ChemAxon IUPAC Name ethyl 3-[(1E)-2-amino-1-cyanoeth-1-en-1-yl]-6,7-dichloro-1-methyl-1H-indole-2-carboxylate ChemAxon Traditional IUPAC Name ethyl 3-[(1E)-2-amino-1-cyanoeth-1-en-1-yl]-6,7-dichloro-1-methylindole-2-carboxylate ChemAxon Molecular Weight 338.189 ChemAxon Monoisotopic Weight 337.038482089 ChemAxon SMILES CCOC(=O)C1=C(\C(=C/N)C#N)C2=C(N1C)C(Cl)=C(Cl)C=C2 ChemAxon Molecular Formula C15H13Cl2N3O2 ChemAxon InChI InChI=1S/C15H13Cl2N3O2/c1-3-22-15(21)14-11(8(6-18)7-19)9-4-5-10(16)12(17)13(9)20(14)2/h4-6H,3,18H2,1-2H3/b8-6- ChemAxon InChIKey InChIKey=CXJCGSPAPOTTSF-VURMDHGXSA-N ChemAxon Polar Surface Area (PSA) 81.04 ChemAxon Refractivity 86.6 ChemAxon Polarizability 32.76 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 2.04 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon ChemSpider 22378449 PDB V25 BE0001824 Dual specificity protein kinase CLK1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dual specificity protein kinase CLK1 Involved in protein kinase activity Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates serines, threonines and tyrosines CLK1 2q33 Nucleus None 9.02 57206.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:2068 GenAtlas CLK1 GeneCards CLK1 GenBank Gene Database L29219 GenBank Protein Database 632964 UniProtKB P49759 UniProt Accession CLK1_HUMAN CDC-like kinase 1 EC 2.7.12.1 >Dual specificity protein kinase CLK1 MRHSKRTYCPDWDDKDWDYGKWRSSSSHKRRKRSHSSAQENKRCKYNHSKMCDSHYLESR SINEKDYHSRRYIDEYRNDYTQGCEPGHRQRDHESRYQNHSSKSSGRSGRSSYKSKHRIH HSTSHRRSHGKSHRRKRTRSVEDDEEGHLICQSGDVLSARYEIVDTLGEGAFGKVVECID HKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIV FELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSD YTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPC DVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWD EHSSAGRYVSRACKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRITLREALKHPFFDLL KKSI >1455 bp ATGAGACACTCAAAGAGAACTTACTGTCCTGATTGGGATGACAAGGATTGGGATTATGGA AAATGGAGGAGCAGCAGCAGTCATAAAAGAAGGAAGAGATCACATAGCAGTGCCCAGGAG AACAAGCGCTGCAAATACAATCACTCTAAAATGTGTGATAGCCATTATTTGGAAAGCAGG TCTATAAATGAGAAAGATTATCATAGTCGACGCTACATTGATGAGTACAGAAATGACTAC ACTCAAGGATGTGAACCTGGACATCGCCAAAGAGACCATGAAAGCCGGTATCAGAACCAT AGTAGCAAGTCTTCTGGTAGAAGTGGAAGAAGTAGTTATAAAAGCAAACACAGGATTCAC CACAGTACTTCACATCGTCGTTCACATGGGAAGAGTCACCGAAGGAAAAGAACCAGGAGT GTAGAGGATGATGAGGAGGGTCACCTGATCTGTCAGAGTGGAGACGTACTAAGTGCAAGA TATGAAATTGTTGATACTTTAGGTGAAGGAGCTTTTGGAAAAGTTGTGGAGTGCATCGAT CATAAAGCGGGAGGTAGACATGTAGCAGTAAAAATAGTTAAAAATGTGGATAGATACTGT GAAGCTGCTCGCTCAGAAATACAAGTTCTGGAACATCTGAATACAACAGACCCCAACAGT ACTTTCCGCTGTGTCCAGATGTTGGAATGGTTTGAGCATCATGGTCACATTTGCATTGTT TTTGAACTATTGGGACTTAGTACTTACGACTTCATTAAAGAAAATGGTTTTCTACCATTT CGACTGGATCATATCAGAAAGATGGCATATCAGATATGCAAGTCTGTGAATTTTTTGCAC AGTAATAAGTTGACTCACACAGACTTAAAGCCTGAAAACATCTTATTTGTGCAGTCTGAC TACACAGAGGCGTATAATCCCAAAATAAAACGTGATGAACGCACCTTAATAAATCCAGAT ATTAAAGTTGTAGACTTTGGTAGTGCAACATATGATGACGAACATCACAGTACATTGGTA TCTACAAGACATTATAGAGCACCTGAAGTTATTTTAGCCCTAGGGTGGTCCCAACCATGT GATGTCTGGAGCATAGGATGCATTCTTATTGAATACTATCTTGGGTTTACCGTATTTCCA ACACACGATAGTAAGGAGCATTTAGCAATGATGGAAAGGATTCTTGGACCTCTACCAAAA CATATGATACAGAAAACCAGGAAACGTAAATATTTTCACCACGATCGATTAGACTGGGAT GAACACAGTTCTGCCGGCAGATATGTTTCAAGAGCCTGTAAACCTCTGAAGGAATTTATG CTTTCTCAAGATGTTGAACATGAGCGTCTCTTTGACCTCATTCAGAAAATGTTGGAGTAT GATCCAGCCAAAAGAATTACTCTCAGAGAAGCCTTAAAGCATCCTTTCTTTGACCTTCTG AAGAAAAGTATATAG PF00069 Pkinase function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding process physiological process process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification BE0004043 Dual specificity protein kinase CLK3 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dual specificity protein kinase CLK3 Involved in ATP binding Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates serines, threonines and tyrosines CLK3 15q24 Nucleus. Cytoplasm (By similarity). Cytoplasmic vesicle, secretory vesicle, acrosome (By similarity) None 10.37 73514.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:2071 GeneCards CLK3 GenBank Gene Database L29220 GenBank Protein Database 632970 UniProtKB P49761 UniProt Accession CLK3_HUMAN CDC-like kinase 3 >Dual specificity protein kinase CLK3 MPVLSARRRELADHAGSGRRSGPSPTARSGPHLSALRAQPARAAHLSGRGTYVRRDTAGG GPGQARPLGPPGTSLLGRGARRSGEGWCPGAFESGARAARPPSRVEPRLATAASREGAGL PRAEVAAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEG RLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPSFGEDYYGPSRSRHR RRSRERGPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWL QERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKD KENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALR FLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHT TIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGP IPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRM LEFDPAQRITLAEALLHPFFAGLTPEERSFHTSRNPSR >459 bp ATGCATCACTGTAAGCGATACCGCTCCCCTGAACCAGACCCGTACCTGAGCTACCGATGG AAGAGGAGGAGGTCCTACAGTCGGGAACATGAAGGGAGACTGCGATACCCGTCCCGAAGG GAGCCTCCCCCACGAAGATCTCGGTCCAGAAGCCATGACCGCCTGCCCTACCAGAGGAGG TACCGGGAGCGCCGTGACAGCGATACATACCGGTGTGAAGAGCGGAGCCCATCCTTTGGA GAGGACTACTATGGACCTTCACGTTCTCGTCATCGTCGGCGATCGCGGGAGAGGGGGCCA TACCGGACCCGCAAGCATGCCCACCACTGCCACAAACGCCGCACCAGGTCTTGTAGCAGC GCCTCCTCGATGAGATTGTGGGGAACCTGGGTGAAGGCACCTTTGGCAAGGTGGTGGAGT GCTTGGACCATGCCAGAGGGAAGTCTCAGGTTGCCCTGA PF00069 Pkinase function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism "
drug:ethyl 3-[(E)-2-amino-1-cyanoethenyl]-6,7-dichloro-1-methyl-1H-indole-2-carboxylaterdfs:label"ethyl 3-[(E)-2-amino-1-cyanoethenyl]-6,7-dichloro-1-methyl-1H-indole-2-carboxylate"
drug:ethyl 3-[(E)-2-amino-1-cyanoethenyl]-6,7-dichloro-1-methyl-1H-indole-2-carboxylaterdf:typedrugbank:drugs
drug:faropenem medoxomildrugbank:description"Faropenem medoxomil is an ester prodrug derivative of the beta-lactam antibiotic faropenem. The prodrug form of faropenem offers dramatically improved oral bioavailability and leads to higher systemic concentrations of the drug. Faropenem medoxomil is a broad-spectrum antibiotic that is highly resistant to beta-lactamase degradation. It is being developed jointly by Replidyne, Inc. and Forest Laboratories, Inc."
drug:faropenem medoxomildrugbank:drugCategorydrugcategory:Anti-Bacterial Agents
drug:faropenem medoxomilrdfs:label"faropenem medoxomil"
drug:faropenem medoxomilrdf:typedrugbank:drugs
drug:gabapentin enacarbildrugbank:description"Gabapentin enacarbil is marketed under the name Horizant®. It is a prodrug of gabapentin, and indicated in adults for the treatment of Restless Legs Syndrome (RLS) and postherpetic neuralgia (PHN). "
drug:gabapentin enacarbildrugbank:interactsWithdrug:Azelastine
drug:gabapentin enacarbildrugbank:interactsWithdrug:Ethanol
drug:gabapentin enacarbilrdfs:label"gabapentin enacarbil"
drug:gabapentin enacarbilowl:sameAsdrug:Azelastine
drug:gabapentin enacarbilowl:sameAsdrug:Ethanol
drug:gabapentin enacarbilrdf:typedrugbank:drugs
drug:gallium maltolatedrugbank:description"Gallium maltolate is Titan’s novel oral agent in development for the potential treatment of chronic bacterial infections, bone disease and cancer."
drug:gallium maltolaterdfs:label"gallium maltolate"
drug:gallium maltolaterdf:typedrugbank:drugs
drug:ginkgolide-Adrugbank:description"A highly active PAF antagonist cage molecule that is isolated from the leaves of the Ginkgo biloba tree. Shows potential in a wide variety of inflammatory and immunological disorders."
drug:ginkgolide-Ardfs:label"ginkgolide-A"
drug:ginkgolide-Ardf:typedrugbank:drugs
drug:ginkgolide-Bdrugbank:description" nutraceutical # Wang SJ, Chen HH: Ginkgolide B, a constituent of Ginkgo biloba, facilitates glutamate exocytosis from rat hippocampal nerve terminals. Eur J Pharmacol. 2005 May 9;514(2-3):141-9. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15910800 This compound belongs to the ginkgolides and bilobalides. These are diterpene lactones whose structure is based either on the gingkolide or the bilobalide skeleton. Ginkgolides and Bilobalides Organic Compounds Lipids Prenol Lipids Terpene Lactones Diterpenes Tricarboxylic Acids and Derivatives Furofurans Oxolanes Tertiary Alcohols Tetrahydrofurans Polyols Lactones Secondary Alcohols Carboxylic Acid Esters Cyclic Alcohols and Derivatives Polyamines Acetals diterpene tricarboxylic acid derivative furofuran gamma butyrolactone oxolane tertiary alcohol cyclic alcohol tetrahydrofuran lactone polyol secondary alcohol carboxylic acid ester ether carboxylic acid derivative polyamine acetal alcohol logP 0.49 ALOGPS logS -1.9 ALOGPS Water Solubility 5.21e+00 g/l ALOGPS logP -0.58 ChemAxon IUPAC Name (1R,3R,6R,7S,8S,10R,11R,12R,13S,16S,17R)-8-tert-butyl-6,12,17-trihydroxy-16-methyl-2,4,14,19-tetraoxahexacyclo[8.7.2.0^{1,11}.0^{3,7}.0^{7,11}.0^{13,17}]nonadecane-5,15,18-trione ChemAxon Traditional IUPAC Name (1R,3R,6R,7S,8S,10R,11R,12R,13S,16S,17R)-8-tert-butyl-6,12,17-trihydroxy-16-methyl-2,4,14,19-tetraoxahexacyclo[8.7.2.0^{1,11}.0^{3,7}.0^{7,11}.0^{13,17}]nonadecane-5,15,18-trione ChemAxon Molecular Weight 424.3986 ChemAxon Monoisotopic Weight 424.136946988 ChemAxon SMILES C[C@@H]1C(=O)O[C@H]2[C@H](O)[C@@]34[C@H]5C[C@@H](C(C)(C)C)[C@@]33[C@@H](O)C(=O)O[C@H]3O[C@@]4(C(=O)O5)[C@@]12O ChemAxon Molecular Formula C20H24O10 ChemAxon InChI InChI=1S/C20H24O10/c1-6-12(23)28-11-9(21)18-8-5-7(16(2,3)4)17(18)10(22)13(24)29-15(17)30-20(18,14(25)27-8)19(6,11)26/h6-11,15,21-22,26H,5H2,1-4H3/t6-,7+,8-,9+,10+,11+,15+,17+,18+,19-,20-/m1/s1 ChemAxon InChIKey InChIKey=SQOJOAFXDQDRGF-MMQTXUMRSA-N ChemAxon Polar Surface Area (PSA) 148.82 ChemAxon Refractivity 91.38 ChemAxon Polarizability 39.2 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 11.71 ChemAxon pKa (strongest basic) -3.5 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 6 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 6324617 PubChem Substance 99443280 ChemSpider 21105603 "
drug:ginkgolide-Brdfs:label"ginkgolide-B"
drug:ginkgolide-Brdf:typedrugbank:drugs
drug:ginkgolide-Cdrugbank:description" 15291-76-6 nutraceutical This compound belongs to the ginkgolides and bilobalides. These are diterpene lactones whose structure is based either on the gingkolide or the bilobalide skeleton. Ginkgolides and Bilobalides Organic Compounds Lipids Prenol Lipids Terpene Lactones Diterpenes Furofurans Tertiary Alcohols Tetrahydrofurans Oxolanes Secondary Alcohols Lactones Polyols Carboxylic Acid Esters Cyclic Alcohols and Derivatives Polyamines Acetals diterpene furofuran gamma butyrolactone oxolane tertiary alcohol cyclic alcohol tetrahydrofuran lactone polyol secondary alcohol carboxylic acid ester ether carboxylic acid derivative polyamine acetal alcohol logP 0.24 ALOGPS logS -1.7 ALOGPS Water Solubility 8.99e+00 g/l ALOGPS logP -1.6 ChemAxon IUPAC Name (1R,3R,6R,7S,8S,9R,10S,11R,12R,13S,16S,17R)-8-tert-butyl-6,9,12,17-tetrahydroxy-16-methyl-2,4,14,19-tetraoxahexacyclo[8.7.2.0^{1,11}.0^{3,7}.0^{7,11}.0^{13,17}]nonadecane-5,15,18-trione ChemAxon Traditional IUPAC Name (1R,3R,6R,7S,8S,9R,10S,11R,12R,13S,16S,17R)-8-tert-butyl-6,9,12,17-tetrahydroxy-16-methyl-2,4,14,19-tetraoxahexacyclo[8.7.2.0^{1,11}.0^{3,7}.0^{7,11}.0^{13,17}]nonadecane-5,15,18-trione ChemAxon Molecular Weight 440.398 ChemAxon Monoisotopic Weight 440.13186161 ChemAxon SMILES C[C@@H]1C(=O)O[C@H]2[C@H](O)[C@]34[C@@H]5OC(=O)[C@]3(O[C@@H]3OC(=O)[C@H](O)[C@]43[C@@H]([C@H]5O)C(C)(C)C)[C@@]12O ChemAxon Molecular Formula C20H24O11 ChemAxon InChI InChI=1S/C20H24O11/c1-5-12(24)28-11-8(22)18-10-6(21)7(16(2,3)4)17(18)9(23)13(25)30-15(17)31-20(18,14(26)29-10)19(5,11)27/h5-11,15,21-23,27H,1-4H3/t5-,6-,7+,8+,9+,10-,11+,15+,17+,18-,19-,20-/m1/s1 ChemAxon InChIKey InChIKey=AMOGMTLMADGEOQ-DTDWCABLSA-N ChemAxon Polar Surface Area (PSA) 169.05 ChemAxon Refractivity 92.67 ChemAxon Polarizability 40.09 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 8 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 11.7 ChemAxon pKa (strongest basic) -3.3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 6 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 9867869 PubChem Substance 99443281 "
drug:ginkgolide-Crdfs:label"ginkgolide-C"
drug:ginkgolide-Crdf:typedrugbank:drugs
drug:ginkgolide-Jdrugbank:description" 107438-79-9 nutraceutical This compound belongs to the ginkgolides and bilobalides. These are diterpene lactones whose structure is based either on the gingkolide or the bilobalide skeleton. Ginkgolides and Bilobalides Organic Compounds Lipids Prenol Lipids Terpene Lactones Diterpenes Furofurans Tertiary Alcohols Tetrahydrofurans Oxolanes Secondary Alcohols Lactones Polyols Carboxylic Acid Esters Cyclic Alcohols and Derivatives Polyamines Acetals diterpene furofuran gamma butyrolactone oxolane tertiary alcohol cyclic alcohol tetrahydrofuran lactone polyol secondary alcohol carboxylic acid ester ether carboxylic acid derivative polyamine acetal alcohol logP 0.23 ALOGPS logS -1.8 ALOGPS Water Solubility 6.96e+00 g/l ALOGPS logP -0.66 ChemAxon IUPAC Name (1R,3R,6R,7S,8S,9R,10S,11S,13S,16S,17R)-8-tert-butyl-6,9,17-trihydroxy-16-methyl-2,4,14,19-tetraoxahexacyclo[8.7.2.0^{1,11}.0^{3,7}.0^{7,11}.0^{13,17}]nonadecane-5,15,18-trione ChemAxon Traditional IUPAC Name (1R,3R,6R,7S,8S,9R,10S,11S,13S,16S,17R)-8-tert-butyl-6,9,17-trihydroxy-16-methyl-2,4,14,19-tetraoxahexacyclo[8.7.2.0^{1,11}.0^{3,7}.0^{7,11}.0^{13,17}]nonadecane-5,15,18-trione ChemAxon Molecular Weight 424.3986 ChemAxon Monoisotopic Weight 424.136946988 ChemAxon SMILES C[C@@H]1C(=O)O[C@H]2C[C@]34[C@@H]5OC(=O)[C@]3(O[C@@H]3OC(=O)[C@H](O)[C@]43[C@@H]([C@H]5O)C(C)(C)C)[C@@]12O ChemAxon Molecular Formula C20H24O10 ChemAxon InChI InChI=1S/C20H24O10/c1-6-12(23)27-7-5-17-11-8(21)9(16(2,3)4)18(17)10(22)13(24)29-15(18)30-20(17,14(25)28-11)19(6,7)26/h6-11,15,21-22,26H,5H2,1-4H3/t6-,7+,8-,9+,10+,11-,15+,17-,18+,19-,20-/m1/s1 ChemAxon InChIKey InChIKey=LMEHVEUFNRJAAV-UKWFQYJJSA-N ChemAxon Polar Surface Area (PSA) 148.82 ChemAxon Refractivity 91.46 ChemAxon Polarizability 39.26 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 11.76 ChemAxon pKa (strongest basic) -3.3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 6 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 11154476 PubChem Substance 99443282 "
drug:ginkgolide-Jrdfs:label"ginkgolide-J"
drug:ginkgolide-Jrdf:typedrugbank:drugs
drug:ginkgolide-Mdrugbank:description" 15291-78-8 nutraceutical This compound belongs to the ginkgolides and bilobalides. These are diterpene lactones whose structure is based either on the gingkolide or the bilobalide skeleton. Ginkgolides and Bilobalides Organic Compounds Lipids Prenol Lipids Terpene Lactones Diterpenes Furofurans Tetrahydrofurans Oxolanes Lactones Secondary Alcohols Polyols Carboxylic Acid Esters Cyclic Alcohols and Derivatives Polyamines Acetals diterpene furofuran gamma butyrolactone cyclic alcohol tetrahydrofuran oxolane lactone carboxylic acid ester secondary alcohol polyol ether acetal carboxylic acid derivative polyamine alcohol logP 0.6 ALOGPS logS -1.7 ALOGPS Water Solubility 7.96e+00 g/l ALOGPS logP -0.92 ChemAxon IUPAC Name (1S,3R,6R,7S,8S,9R,10S,11R,12R,13R,16S)-8-tert-butyl-6,9,12-trihydroxy-16-methyl-2,4,14,19-tetraoxahexacyclo[8.7.2.0^{1,11}.0^{3,7}.0^{7,11}.0^{13,17}]nonadecane-5,15,18-trione ChemAxon Traditional IUPAC Name (1S,3R,6R,7S,8S,9R,10S,11R,12R,13R,16S)-8-tert-butyl-6,9,12-trihydroxy-16-methyl-2,4,14,19-tetraoxahexacyclo[8.7.2.0^{1,11}.0^{3,7}.0^{7,11}.0^{13,17}]nonadecane-5,15,18-trione ChemAxon Molecular Weight 424.3986 ChemAxon Monoisotopic Weight 424.136946988 ChemAxon SMILES C[C@H]1C2[C@@H](OC1=O)[C@H](O)[C@]13[C@@H]4OC(=O)[C@]21O[C@@H]1OC(=O)[C@H](O)[C@]31[C@@H]([C@H]4O)C(C)(C)C ChemAxon Molecular Formula C20H24O10 ChemAxon InChI InChI=1S/C20H24O10/c1-5-6-8(27-13(5)24)10(22)19-12-7(21)9(17(2,3)4)18(19)11(23)14(25)29-16(18)30-20(6,19)15(26)28-12/h5-12,16,21-23H,1-4H3/t5-,6?,7+,8+,9-,10-,11-,12+,16-,18-,19+,20+/m0/s1 ChemAxon InChIKey InChIKey=KDKROYXEHCYLJQ-FJFAJXJPSA-N ChemAxon Polar Surface Area (PSA) 148.82 ChemAxon Refractivity 91.58 ChemAxon Polarizability 39.37 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 12.05 ChemAxon pKa (strongest basic) -3.3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 6 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 46937025 PubChem Substance 99443283 "
drug:ginkgolide-Mrdfs:label"ginkgolide-M"
drug:ginkgolide-Mrdf:typedrugbank:drugs
drug:ginsenoside Cdrugbank:description" 15291-76-6 nutraceutical This compound belongs to the steroidal glycosides. These are sterol lipids containing a carbohydrate moiety glycosidically linked to the steroid skeleton. Steroidal Glycosides Organic Compounds Lipids Steroids and Steroid Derivatives Steroidal Glycosides Tetrahexoses Triterpene Saponins Dammarane Triterpenes Hydroxysteroids O-glycosyl Compounds Alkyl Glycosides Cyclohexanols Oxanes 1,2-Diols Cyclic Alcohols and Derivatives Polyamines Acetals Primary Alcohols 12-hydroxy-steroid terpene glycoside tetrasaccharide o-glycosyl compound glycosyl compound alkyl glycoside cyclohexanol oxane saccharide cyclic alcohol secondary alcohol 1,2-diol polyol ether polyamine primary alcohol acetal alcohol logP -0.02 ALOGPS logS -3.1 ALOGPS Water Solubility 7.84e-01 g/l ALOGPS logP -0.92 ChemAxon IUPAC Name (2S,3R,4S,5S,6R)-2-{[(2S)-2-[(1R,2R,5S,7R,10R,11R,14S,15R,16R)-5-{[(2R,3R,4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-{[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy}oxan-2-yl]oxy}-16-hydroxy-2,6,6,10,11-pentamethyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadecan-14-yl]-6-methylhept-5-en-2-yl]oxy}-6-({[(2S,3R,4S,5R)-3,4,5-trihydroxyoxan-2-yl]oxy}methyl)oxane-3,4,5-triol ChemAxon Traditional IUPAC Name (2S,3R,4S,5S,6R)-2-{[(2S)-2-[(1R,2R,5S,7R,10R,11R,14S,15R,16R)-5-{[(2R,3R,4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-{[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy}oxan-2-yl]oxy}-16-hydroxy-2,6,6,10,11-pentamethyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadecan-14-yl]-6-methylhept-5-en-2-yl]oxy}-6-({[(2S,3R,4S,5R)-3,4,5-trihydroxyoxan-2-yl]oxy}methyl)oxane-3,4,5-triol ChemAxon Molecular Weight 1079.2685 ChemAxon Monoisotopic Weight 1078.592374564 ChemAxon SMILES CC(C)=CCC[C@](C)(O[C@@H]1O[C@H](CO[C@@H]2OC[C@@H](O)[C@H](O)[C@H]2O)[C@@H](O)[C@H](O)[C@H]1O)[C@H]1CC[C@]2(C)[C@@H]1[C@H](O)C[C@@H]1[C@@]3(C)CC[C@H](O[C@@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@H]4O[C@@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@H]4O)C(C)(C)[C@@H]3CC[C@@]21C ChemAxon Molecular Formula C53H90O22 ChemAxon InChI InChI=1S/C53H90O22/c1-23(2)10-9-14-53(8,75-47-43(67)39(63)37(61)29(72-47)22-69-45-41(65)34(58)26(57)21-68-45)24-11-16-52(7)33(24)25(56)18-31-50(5)15-13-32(49(3,4)30(50)12-17-51(31,52)6)73-48-44(40(64)36(60)28(20-55)71-48)74-46-42(66)38(62)35(59)27(19-54)70-46/h10,24-48,54-67H,9,11-22H2,1-8H3/t24-,25+,26+,27+,28+,29+,30-,31+,32-,33-,34-,35+,36+,37+,38-,39-,40-,41+,42+,43+,44+,45-,46-,47-,48-,50-,51+,52+,53-/m0/s1 ChemAxon InChIKey InChIKey=NODILNFGTFIURN-USYOXQFSSA-N ChemAxon Polar Surface Area (PSA) 357.06 ChemAxon Refractivity 260.93 ChemAxon Polarizability 117.65 ChemAxon Rotatable Bond Count 15 ChemAxon H Bond Acceptor Count 22 ChemAxon H Bond Donor Count 14 ChemAxon pKa (strongest acidic) 11.75 ChemAxon pKa (strongest basic) -3.6 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 8 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 12912363 PubChem Substance 99443284 ChemSpider 23327428 "
drug:ginsenoside Crdfs:label"ginsenoside C"
drug:ginsenoside Crdf:typedrugbank:drugs
drug:ginsenoside Rb1drugbank:description"Ginsenosides are a class of steroid glycosides, and triterpene saponins, found exclusively in the plant genus Panax (ginseng). Ginsenosides have been the target of research, as they are viewed as the active compounds behind the claims of ginseng's efficacy. Because ginsenosides appear to affect multiple pathways, their effects are complex and difficult to isolate. Rb1 appears to be most abundant in Panax quinquefolius (American Ginseng). Rb1 seems to affect the reproductive system in animal testicles. Recent research shows that Rb1 affects rat embryo development and has teratogenic effects, causing birth defects. Another study shows that Rb1 may increase testosterone production in male rats indirectly through the stimulation of the luteinizing hormone. Traditional Chinese medicine asserts that Panax quinquefolius promotes yin in the body. It also inhibits chemoinvasion and angiogenesis."
drug:ginsenoside Rb1rdfs:label"ginsenoside Rb1"
drug:ginsenoside Rb1rdf:typedrugbank:drugs
drug:golimumabdrugbank:description"Golimumab is a human IgG1қ monoclonal antibody derived from immunizing genetically engineered mice with human TNFα. Golimumab binds and inhibits soluble and transmembrane human TNFα. Increased TNFα is associated with chronic inflammation. Thus golimumab is indicated for use in adults (i) as an adjunct to methotrexate treatment in patients with moderate to severe active rheumatoid arthritis (RA), (ii) alone or as an adjunct to methotrexate treatment in patients with active psoriatic arthritis (PsA), (iii) as a single agent in patients with active ankylosing spondylitis (AS), and (iv) as a single agent in patients with moderate to severe ulcerative colitis (UC) who require chronic steroids or have experienced intolerance or only a partial response to previous medications. In the U.S. and Canada, golimumab is marketed under the brand name Simponi®. The FDA label includes a black box warning of serious infections and malignancy. Additionally in children and adolescents taking golimumab, there have been lymphoma and other malignancies observed. "
drug:golimumabdrugbank:drugCategorydrugcategory:Antipsoriatic Agents
drug:golimumabdrugbank:drugCategorydrugcategory:Monoclonal antibodies
drug:golimumabdrugbank:drugCategorydrugcategory:TNF inhibitor
drug:golimumabdrugbank:interactsWithdrug:Abatacept
drug:golimumabdrugbank:interactsWithdrug:Anakinra
drug:golimumabdrugbank:interactsWithdrug:Belimumab
drug:golimumabdrugbank:interactsWithdrug:Canakinumab
drug:golimumabdrugbank:interactsWithdrug:Certolizumab pegol
drug:golimumabdrugbank:interactsWithdrug:Infliximab
drug:golimumabdrugbank:interactsWithdrug:Natalizumab
drug:golimumabdrugbank:interactsWithdrug:Pimecrolimus
drug:golimumabdrugbank:interactsWithdrug:Rilonacept
drug:golimumabdrugbank:interactsWithdrug:Tacrolimus
drug:golimumabdrugbank:interactsWithdrug:Tocilizumab
drug:golimumabdrugbank:interactsWithdrug:Tofacitinib
drug:golimumabrdfs:label"golimumab"
drug:golimumabowl:sameAsdrug:Abatacept
drug:golimumabowl:sameAsdrug:Anakinra
drug:golimumabowl:sameAsdrug:Belimumab
drug:golimumabowl:sameAsdrug:Canakinumab
drug:golimumabowl:sameAsdrug:Certolizumab pegol
drug:golimumabowl:sameAsdrug:Infliximab
drug:golimumabowl:sameAsdrug:Natalizumab
drug:golimumabowl:sameAsdrug:Pimecrolimus
drug:golimumabowl:sameAsdrug:Rilonacept
drug:golimumabowl:sameAsdrug:Tacrolimus
drug:golimumabowl:sameAsdrug:Tocilizumab
drug:golimumabowl:sameAsdrug:Tofacitinib
drug:golimumabrdf:typedrugbank:drugs
drug:grass pollen extractdrugbank:description"Grass pollen extract is a novel vaccine for treatment of seasonal allergic reactions from grass, tree or ragweed pollen allergy. Its formualation combines chemically modified allergens adsorbed onto a L-tyrosine with addition of the immunostimulatory adjuvant monophosphoryl lipid A (MPL), to improve efficacy."
drug:grass pollen extractrdfs:label"grass pollen extract"
drug:grass pollen extractrdf:typedrugbank:drugs
drug:heat-activated liposome technologydrugbank:description"ThermoDox, a heat activated liposomal encapsulation of doxorubicin, is an investigative new drug currently in Phase I studies for liver cancer and loco-regionally advanced recurrent breast cancer."
drug:heat-activated liposome technologyrdfs:label"heat-activated liposome technology"
drug:heat-activated liposome technologyrdf:typedrugbank:drugs
drug:hepatitis B immune globulindrugbank:description"Long-term hepatitis B immune globulin (HBIG) has been shown to reduce hepatitis B virus (HBV) reinfection in patients transplanted for hepatitis B. Infection with hepatitis B may lead to hepatocellular carcinoma, a type of liver cancer. Therefore, the hepatitis-B vaccines are cancer-preventing vaccines. According to the Centers for Disease Control and Prevention (CDC), the hepatitis B vaccine was the first anti-cancer vaccine.[5]"
drug:hepatitis B immune globulinrdfs:label"hepatitis B immune globulin"
drug:hepatitis B immune globulinrdf:typedrugbank:drugs
drug:histamine dihydrochloridedrugbank:description"A depressor amine derived by enzymatic decarboxylation of histidine. It is a powerful stimulant of gastric secretion, a constrictor of bronchial smooth muscle, a vasodilator, and also a centrally acting neurotransmitter."
drug:histamine dihydrochloriderdfs:label"histamine dihydrochloride"
drug:histamine dihydrochloriderdf:typedrugbank:drugs
drug:humanized SMART Anti-IL-12 Antibodydrugbank:description"The humanized anti-IL-12 antibody is an important addition to PDL's already strong pipeline of humanized antibodies being developed for the treatment of autoimmune diseases. SMART Anti-IL-12 Antibody was humanized at PDL from a murine anti-IL-12 antibody that was licensed, together with certain intellectual property related to anti-IL-12 therapy, from Hoffmann-La Roche Inc. IL-12 is a cytokine that may have considerable potential as a target in the therapy of autoimmune diseases."
drug:humanized SMART Anti-IL-12 Antibodyrdfs:label"humanized SMART Anti-IL-12 Antibody"
drug:humanized SMART Anti-IL-12 Antibodyrdf:typedrugbank:drugs
drug:iCo-007drugbank:description"iCo-007 (formerly known as ISIS 13650) is a second generation antisense compound being developed by iCo for the treatment of various eye diseases caused by the formation of new blood vessels (angiogenesis) such as age-related macular degeneration (AMD) and diabetic retinopathy(DR)."
drug:iCo-007rdfs:label"iCo-007"
drug:iCo-007rdf:typedrugbank:drugs
drug:indane-5-sulfonamidedrugbank:description" experimental This compound belongs to the benzenesulfonamides. These are organic compounds containing a sulfonamide group that is S-linked to a benzene ring. Benzenesulfonamides Organic Compounds Benzenoids Benzene and Substituted Derivatives Benzenesulfonamides Indanes Sulfonamides Sulfonyls Polyamines sulfonyl sulfonamide sulfonic acid derivative polyamine logP 1.18 ALOGPS logS -2.4 ALOGPS Water Solubility 7.70e-01 g/l ALOGPS logP 1.59 ChemAxon IUPAC Name 2,3-dihydro-1H-indene-5-sulfonamide ChemAxon Traditional IUPAC Name 2,3-dihydro-1H-indene-5-sulfonamide ChemAxon Molecular Weight 197.254 ChemAxon Monoisotopic Weight 197.051049291 ChemAxon SMILES NS(=O)(=O)C1=CC=C2CCCC2=C1 ChemAxon Molecular Formula C9H11NO2S ChemAxon InChI InChI=1S/C9H11NO2S/c10-13(11,12)9-5-4-7-2-1-3-8(7)6-9/h4-6H,1-3H2,(H2,10,11,12) ChemAxon InChIKey InChIKey=XVQJTFMKKZBBSX-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 60.16 ChemAxon Refractivity 51.1 ChemAxon Polarizability 20.22 ChemAxon Rotatable Bond Count 1 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 10.46 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 96876 PubChem Substance 99444636 ChemSpider 87470 PDB MAJ BE0000322 Carbonic anhydrase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Carbonic anhydrase 2 Inorganic ion transport and metabolism Reversible hydration of carbon dioxide CA2 8q22 Cytoplasm None 7.47 29115.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1373 GenAtlas CA2 GeneCards CA2 GenBank Gene Database M77181 GenBank Protein Database 179780 UniProtKB P00918 UniProt Accession CAH2_HUMAN CA-II Carbonate dehydratase II Carbonic anhydrase C Carbonic anhydrase II EC 4.2.1.1 >Carbonic anhydrase 2 SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILN NGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLV HWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPR GLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV DNWRPAQPLKNRQIKASFK >783 bp ATGTCCCATCACTGGGGGTACGGCAAACACAACGGACCTGAGCACTGGCATAAGGACTTC CCCATTGCCAAGGGAGAGCGCCAGTCCCCTGTTGACATCGACACTCATACAGCCAAGTAT GACCCTTCCCTGAAGCCCCTGTCTGTTTCCTATGATCAAGCAACTTCCCTGAGGATCCTC AACAATGGTCATGCTTTCAACGTGGAGTTTGATGACTCTCAGGACAAAGCAGTGCTCAAG GGAGGACCCCTGGATGGCACTTACAGATTGATTCAGTTTCACTTTCACTGGGGTTCACTT GATGGACAAGGTTCAGAGCATACTGTGGATAAAAAGAAATATGCTGCAGAACTTCACTTG GTTCACTGGAACACCAAATATGGGGATTTTGGGAAAGCTGTGCAGCAACCTGATGGACTG GCCGTTCTAGGTATTTTTTTGAAGGTTGGCAGCGCTAAACCGGGCCTTCAGAAAGTTGTT GATGTGCTGGATTCCATTAAAACAAAGGGCAAGAGTGCTGACTTCACTAACTTCGATCCT CGTGGCCTCCTTCCTGAATCCTTGGATTACTGGACCTACCCAGGCTCACTGACCACCCCT CCTCTTCTGGAATGTGTGACCTGGATTGTGCTCAAGGAACCCATCAGCGTCAGCAGCGAG CAGGTGTTGAAATTCCGTAAACTTAACTTCAATGGGGAGGGTGAACCCGAAGAACTGATG GTGGACAACTGGCGCCCAGCTCAGCCACTGAAGAACAGGCAAATCAAAGCTTCCTTCAAA TAA PF00194 Carb_anhydrase function lyase activity function ion binding function cation binding function transition metal ion binding function zinc ion binding function carbon-oxygen lyase activity function binding function hydro-lyase activity function carbonate dehydratase activity function catalytic activity process physiological process process one-carbon compound metabolism process metabolism process cellular metabolism "
drug:indane-5-sulfonamiderdfs:label"indane-5-sulfonamide"
drug:indane-5-sulfonamiderdf:typedrugbank:drugs
drug:inhaled insulindrugbank:description"Inhaled insulin is effective, well tolerated, and well accepted in patients with type 2 diabetes and provides glycemic control comparable to a conventional subcutaneous regimen."
drug:inhaled insulinrdfs:label"inhaled insulin"
drug:inhaled insulinrdf:typedrugbank:drugs
drug:intranasal apomorphinedrugbank:description"Intranasal apomorphine is a nasal formulation of apomorphine developed by Nastech Pharmaceutical Co Inc for the potential treatment of erectile dysfunction and female sexual dysfunction."
drug:intranasal apomorphinerdfs:label"intranasal apomorphine"
drug:intranasal apomorphinerdf:typedrugbank:drugs
drug:intranasal morphinedrugbank:description"Rylomine (intranasal morphine), is currently in Phase 3 development in the United States, for moderate-to-severe pain in supervised healthcare settings. It employs the patented and proprietary, Chysis(R) drug-delivery platform to adhere and regularize the kinet"
drug:intranasal morphinerdfs:label"intranasal morphine"
drug:intranasal morphinerdf:typedrugbank:drugs
drug:iontophoretic acyclovirdrugbank:description"Acyclovir which has chemical name as acycloguanosine, is a guanine analogue antiviral drug, marketed under trade names such as Zovirax and Zovir (GSK). One of the most commonly-used antiviral drugs, it is primarily used for the treatment of herpes simplex virus infections, as well as in the treatment of herpes zoster (shingles)."
drug:iontophoretic acyclovirrdfs:label"iontophoretic acyclovir"
drug:iontophoretic acyclovirrdf:typedrugbank:drugs
drug:ketoprofen transdermal patchdrugbank:description"Ketoprofen transdermal patch antiinflammatory drug containing nonsteroidal antiinflammatory drug which is excellent in the dermal absorption and the skin adhesion, has hardly the skin stimulus. The ketoprofen patch was developed by APR Applied Pharma Research, a Swiss research and development company, with the German R&D company Labtec GmbH. The product has been licensed in Europe to Zambon Group."
drug:ketoprofen transdermal patchrdfs:label"ketoprofen transdermal patch"
drug:ketoprofen transdermal patchrdf:typedrugbank:drugs
drug:keyhole limpet hemocyanindrugbank:description"keyhole limpet hemocyanin is an immune modulators, given as a vaccine to help the body respond to cancer. A natural protein isolated from the marine mollusc keyhole limpet. Keyhole limpet hemocyanin is an immunogenic carrier protein that, in vivo, increases antigenic immune responses to haptens and other weak antigens such as idiotype proteins."
drug:keyhole limpet hemocyaninrdfs:label"keyhole limpet hemocyanin"
drug:keyhole limpet hemocyaninrdf:typedrugbank:drugs
drug:lidocaine patchdrugbank:description"The lidocaine patch is composed of an adhesive material containing 5% lidocaine that is applied to a polyester felt backing. When it is applied to the skin, lidocaine is released into the epidermal and dermal layers of the skin, reducing pain at the site of the dysfunctional nerves damaged by the prior herpes zoster infection. The lidocaine patch provides pain reduction without numbness of the affected skin."
drug:lidocaine patchrdfs:label"lidocaine patch"
drug:lidocaine patchrdf:typedrugbank:drugs
drug:liposomal prostaglandin E1drugbank:description"Liposome-encapsulated form of prostaglandin E1 (Liprostin) is known to be a potent vasodilator and platelet inhibitor as well as an anti-inflammatory and anti-thrombotic agent. The liposomal formulation of PGE-1 changes the drug’s dynamics and improve its therapeutic index in ways that PGE-1 alone could not achieve."
drug:liposomal prostaglandin E1rdfs:label"liposomal prostaglandin E1"
drug:liposomal prostaglandin E1rdf:typedrugbank:drugs
drug:lymphotoxin beta receptordrugbank:description"Lymphotoxin beta receptor is a receptor for lymphotoxin. The protein encoded by this gene is a member of the tumor necrosis factor (TNF) family of receptors. It is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. "
drug:lymphotoxin beta receptorrdfs:label"lymphotoxin beta receptor"
drug:lymphotoxin beta receptorrdf:typedrugbank:drugs
drug:mesenchymal stem cellsdrugbank:description"Mesenchymal stem cells (MSCs) from healthy donors improve cardiac function in experimental acute myocardial infarction (AMI) models. Osiris' stem cells are derived from human bone marrow. The source marrow is voluntarily donated by healthy adults between the ages of 18 and 30 years. Blood samples from the donor are screened prior to donation for transmissible diseases, including HIV and hepatitis, and the medical and social history of each donor is obtained to ascertain whether signs, symptoms or behaviors consistent with high risk for carrying a disease are present."
drug:mesenchymal stem cellsrdfs:label"mesenchymal stem cells"
drug:mesenchymal stem cellsrdf:typedrugbank:drugs
drug:methyl (1R,2S)-2-(hydroxycarbamoyl)-1-{4-[(2-methylquinolin-4-yl)methoxy]benzyl}cyclopropanecarboxylatedrugbank:description" experimental This compound belongs to the quinolines and derivatives. These are compounds containing a quinoline moiety, which consists of a benzene ring fused to a pyrimidine ring to form benzo[b]azabenzene. Quinolines and Derivatives Organic Compounds Heterocyclic Compounds Quinolines and Derivatives Phenol Ethers Alkyl Aryl Ethers Fatty Acid Esters Pyridines and Derivatives Cyclopropanecarboxylic Acids and Derivatives Hydroxamic Acids Carboxylic Acid Esters Polyamines Enolates phenol ether fatty acid ester alkyl aryl ether pyridine cyclopropanecarboxylic acid or derivative benzene hydroxamic acid carboxylic acid ester carboxamide group polyamine carboxylic acid derivative ether enolate organonitrogen compound amine logP 3.81 ALOGPS logS -5.3 ALOGPS Water Solubility 2.30e-03 g/l ALOGPS logP 3.11 ChemAxon IUPAC Name methyl (1R,2S)-2-(hydroxycarbamoyl)-1-({4-[(2-methylquinolin-4-yl)methoxy]phenyl}methyl)cyclopropane-1-carboxylate ChemAxon Traditional IUPAC Name methyl (1R,2S)-2-(hydroxycarbamoyl)-1-({4-[(2-methylquinolin-4-yl)methoxy]phenyl}methyl)cyclopropane-1-carboxylate ChemAxon Molecular Weight 420.4578 ChemAxon Monoisotopic Weight 420.168521888 ChemAxon SMILES [H][C@@]1(C[C@]1(CC1=CC=C(OCC2=CC(C)=NC3=C2C=CC=C3)C=C1)C(=O)OC)C(=O)NO ChemAxon Molecular Formula C24H24N2O5 ChemAxon InChI InChI=1S/C24H24N2O5/c1-15-11-17(19-5-3-4-6-21(19)25-15)14-31-18-9-7-16(8-10-18)12-24(23(28)30-2)13-20(24)22(27)26-29/h3-11,20,29H,12-14H2,1-2H3,(H,26,27)/t20-,24+/m1/s1 ChemAxon InChIKey InChIKey=HJWMYFBKJRVWJY-YKSBVNFPSA-N ChemAxon Polar Surface Area (PSA) 97.75 ChemAxon Refractivity 113.42 ChemAxon Polarizability 44.95 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 8.86 ChemAxon pKa (strongest basic) 5.02 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 24800833 PubChem Substance 99443618 ChemSpider 23325936 PDB 550 BE0003754 Disintegrin and metalloproteinase domain-containing protein 17 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Disintegrin and metalloproteinase domain-containing protein 17 Involved in integrin binding Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Also involved in the activation of Notch pathway (By similarity) ADAM17 2p25 Membrane 672-692 5.5 93020.2 Human HUGO Gene Nomenclature Committee (HGNC) GNC:195 GeneCards ADAM17 GenBank Gene Database U86755 GenBank Protein Database 1857673 UniProtKB P78536 UniProt Accession ADA17_HUMAN ADAM 17 CD156b antigen Snake venom-like protease TNF-alpha convertase TNF-alpha-converting enzyme >Disintegrin and metalloproteinase domain-containing protein 17 MRQSLLFLTSVVPFVLAPRPPDDPGFGPHQRLEKLDSLLSDYDILSLSNIQQHSVRKRDL QTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQDFFTGHVV GEPDSRVLAHIRDDDVIIRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKNVSRLQS PKVCGYLKVDNEELLPKGLVDREPPEELVHRVKRRADPDPMKNTCKLLVVADHRFYRYMG RGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNM AKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANS HGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGL AECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGN SRVDEGEECDPGIMYLNNDTCCNSDCTLKEGVQCSDRNSPCCKNCQFETAQKKCQEAINA TCKGVSYCTGNSSECPPPGNAEDDTVCLDLGKCKDGKCIPFCEREQQLESCACNETDNSC KVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWDFIDQLS INTFGKFLADNIVGSVLVFSLIFWIPFSILVHCVDKKLDKQYESLSLFHPSNVEMLSSMD SASVRIIKPFPAPQTPGRLQPAPVIPSAPAAPKLDHQRMDTIQEDPSTDSHMDEDGFEKD PFPNSSTAAKSFEDLTDHPVTRSEKAASFKLQRQNRVDSKETEC >2475 bp ATGAGGCAGTCTCTCCTATTCCTGACCAGCGTGGTTCCTTTCGTGCTGGCGCCGCGACCT CCGGATGACCCGGGCTTCGGCCCCCACCAGAGACTCGAGAAGCTTGATTCTTTGCTCTCA GACTACGATATTCTCTCTTTATCTAATATCCAGCAGCATTCGGTAAGAAAAAGAGATCTA CAGACTTCAACACATGTAGAAACACTACTAACTTTTTCAGCTTTGAAAAGGCATTTTAAA TTATACCTGACATCAAGTACTGAACGTTTTTCACAAAATTTCAAGGTCGTGGTGGTGGAT GGTAAAAACGAAAGCGAGTACACTGTAAAATGGCAGGACTTCTTCACTGGACACGTGGTT GGTGAGCCTGACTCTAGGGTTCTAGCCCACATAAGAGATGATGATGTTATAATCAGAATC AACACAGATGGGGCCGAATATAACATAGAGCCACTTTGGAGATTTGTTAATGATACCAAA GACAAAAGAATGTTAGTTTATAAATCTGAAGATATCAAGAATGTTTCACGTTTGCAGTCT CCAAAAGTGTGTGGTTATTTAAAAGTGGATAATGAAGAGTTGCTCCCAAAAGGGTTAGTA GACAGAGAACCACCTGAAGAGCTTGTTCATCGAGTGAAAAGAAGAGCTGACCCAGATCCC ATGAAGAACACGTGTAAATTATTGGTGGTAGCAGATCATCGCTTCTACAGATACATGGGC AGAGGGGAAGAGAGTACAACTACAAATTACTTAATAGAGCTAATTGACAGAGTTGATGAC ATCTATCGGAACACTTCATGGGATAATGCAGGTTTTAAAGGCTATGGAATACAGATAGAG CAGATTCGCATTCTCAAGTCTCCACAAGAGGTAAAACCTGGTGAAAAGCACTACAACATG GCAAAAAGTTACCCAAATGAAGAAAAGGATGCTTGGGATGTGAAGATGTTGCTAGAGCAA TTTAGCTTTGATATAGCTGAGGAAGCATCTAAAGTTTGCTTGGCACACCTTTTCACATAC CAAGATTTTGATATGGGAACTCTTGGATTAGCTTATGTTGGCTCTCCCAGAGCAAACAGC CATGGAGGTGTTTGTCCAAAGGCTTATTATAGCCCAGTTGGGAAGAAAAATATCTATTTG AATAGTGGTTTGACGAGCACAAAGAATTATGGTAAAACCATCCTTACAAAGGAAGCTGAC CTGGTTACAACTCATGAATTGGGACATAATTTTGGAGCAGAACATGATCCGGATGGTCTA GCAGAATGTGCCCCGAATGAGGACCAGGGAGGGAAATATGTCATGTATCCCATAGCTGTG AGTGGCGATCACGAGAACAATAAGATGTTTTCAAACTGCAGTAAACAATCAATCTATAAG ACCATTGAAAGTAAGGCCCAGGAGTGTTTTCAAGAACGCAGCAATAAAGTTTGTGGGAAC TCGAGGGTGGATGAAGGAGAAGAGTGTGATCCTGGCATCATGTATCTGAACAACGACACC TGCTGCAACAGCGACTGCACGTTGAAGGAAGGTGTCCAGTGCAGTGACAGGAACAGTCCT TGCTGTAAAAACTGTCAGTTTGAGACTGCCCAGAAGAAGTGCCAGGAGGCGATTAATGCT ACTTGCAAAGGCGTGTCCTACTGCACAGGTAATAGCAGTGAGTGCCCGCCTCCAGGAAAT GCTGAAGATGACACTGTTTGCTTGGATCTTGGCAAGTGTAAGGATGGGAAATGCATCCCT TTCTGCGAGAGGGAACAGCAGCTGGAGTCCTGTGCATGTAATGAAACTGACAACTCCTGC AAGGTGTGCTGCAGGGACCTTTCTGGCCGCTGTGTGCCCTATGTCGATGCTGAACAAAAG AACTTATTTTTGAGGAAAGGAAAGCCCTGTACAGTAGGATTTTGTGACATGAATGGCAAA TGTGAGAAACGAGTACAGGATGTAATTGAACGATTTTGGGATTTCATTGACCAGCTGAGC ATCAATACTTTTGGAAAGTTTTTAGCAGACAACATCGTTGGGTCTGTCCTGGTTTTCTCC TTGATATTTTGGATTCCTTTCAGCATTCTTGTCCATTGTGTGGATAAGAAATTGGATAAA CAGTATGAATCTCTGTCTCTGTTTCACCCCAGTAACGTCGAAATGCTGAGCAGCATGGAT TCTGCATCGGTTCGCATTATCAAACCCTTTCCTGCGCCCCAGACTCCAGGCCGCCTGCAG CCTGCCCCTGTGATCCCTTCGGCGCCAGCAGCTCCAAAACTGGACCACCAGAGAATGGAC ACCATCCAGGAAGACCCCAGCACAGACTCACATATGGACGAGGATGGGTTTGAGAAGGAC CCCTTCCCAAATAGCAGCACAGCTGCCAAGTCATTTGAGGATCTCACGGACCATCCGGTC ACCAGAAGTGAAAAGGCTGCCTCCTTTAAACTGCAGCGTCAGAATCGTGTTGACAGCAAA GAAACAGAGTGCTAA PF01421 Reprolysin PF00200 Disintegrin component extracellular matrix component extracellular matrix (sensu Metazoa) function catalytic activity function peptidase activity function hydrolase activity function endopeptidase activity function ion binding function metallopeptidase activity function cation binding function metalloendopeptidase activity function transition metal ion binding function zinc ion binding function binding process cellular protein metabolism process metabolism process macromolecule metabolism process proteolysis process physiological process process protein metabolism "
drug:methyl (1R,2S)-2-(hydroxycarbamoyl)-1-{4-[(2-methylquinolin-4-yl)methoxy]benzyl}cyclopropanecarboxylaterdfs:label"methyl (1R,2S)-2-(hydroxycarbamoyl)-1-{4-[(2-methylquinolin-4-yl)methoxy]benzyl}cyclopropanecarboxylate"
drug:methyl (1R,2S)-2-(hydroxycarbamoyl)-1-{4-[(2-methylquinolin-4-yl)methoxy]benzyl}cyclopropanecarboxylaterdf:typedrugbank:drugs
drug:methyl (3S)-3-[(tert-butoxycarbonyl)amino]-4-oxopentanoatedrugbank:description" experimental This compound belongs to the gamma keto-acids and derivatives. These are organic compounds containing an aldehyde substituted with a keto group on the C4 carbon atom. Gamma Keto-Acids and Derivatives Organic Compounds Organic Acids and Derivatives Keto-Acids and Derivatives Gamma Keto-Acids and Derivatives Fatty Acid Esters Dicarboxylic Acids and Derivatives Carboxylic Acid Esters Ketones Carbamic Acids and Derivatives Ethers Enolates Polyamines Keto Acids and Derivatives fatty acid ester keto acid dicarboxylic acid derivative carboxylic acid ester carbamic acid derivative ketone ether enolate polyamine carboxylic acid derivative amine carbonyl group organonitrogen compound logP 0.35 ALOGPS logS -2 ALOGPS Water Solubility 2.18e+00 g/l ALOGPS logP 0.75 ChemAxon IUPAC Name methyl (3S)-3-{[(tert-butoxy)carbonyl]amino}-4-oxopentanoate ChemAxon Traditional IUPAC Name methyl (3S)-3-[(tert-butoxycarbonyl)amino]-4-oxopentanoate ChemAxon Molecular Weight 245.2723 ChemAxon Monoisotopic Weight 245.126322723 ChemAxon SMILES [H][C@@](CC(=O)OC)(NC(=O)OC(C)(C)C)C(C)=O ChemAxon Molecular Formula C11H19NO5 ChemAxon InChI InChI=1S/C11H19NO5/c1-7(13)8(6-9(14)16-5)12-10(15)17-11(2,3)4/h8H,6H2,1-5H3,(H,12,15)/t8-/m0/s1 ChemAxon InChIKey InChIKey=QKEQESWFLCEUCV-QMMMGPOBSA-N ChemAxon Polar Surface Area (PSA) 81.7 ChemAxon Refractivity 59.73 ChemAxon Polarizability 24.88 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 13.48 ChemAxon pKa (strongest basic) -7 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937089 PubChem Substance 99444167 PDB DZE BE0001162 Caspase-3 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Caspase-3 Involved in caspase activity Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin CASP3 4q34 Cytoplasm None 6.51 31608.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1504 GenAtlas CASP3 GeneCards CASP3 GenBank Gene Database U13737 GenBank Protein Database 561666 UniProtKB P42574 UniProt Accession CASP3_HUMAN Apopain CASP-3 Caspase-3 precursor CPP-32 Cysteine protease CPP32 EC 3.4.22.56 SCA-1 SREBP cleavage activity 1 Yama protein >Caspase-3 precursor MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTG MTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLS HGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDD DMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVN RKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH >834 bp ATGGAGAACACTGAAAACTCAGTGGATTCAAAATCCATTAAAAATTTGGAACCAAAGATC ATACATGGAAGCGAATCAATGGACTCTGGAATATCCCTGGACAACAGTTATAAAATGGAT TATCCTGAGATGGGTTTATGTATAATAATTAATAATAAGAATTTTCATAAAAGCACTGGA ATGACATCTCGGTCTGGTACAGATGTCGATGCAGCAAACCTCAGGGAAACATTCAGAAAC TTGAAATATGAAGTCAGGAATAAAAATGATCTTACACGTGAAGAAATTGTGGAATTGATG CGTGATGTTTCTAAAGAAGATCACAGCAAAAGGAGCAGTTTTGTTTGTGTGCTTCTGAGC CATGGTGAAGAAGGAATAATTTTTGGAACAAATGGACCTGTTGACCTGAAAAAAATAACA AACTTTTTCAGAGGGGATCGTTGTAGAAGTCTAACTGGAAAACCCAAACTTTTCATTATT CAGGCCTGCCGTGGTACAGAACTGGACTGTGGCATTGAGACAGACAGTGGTGTTGATGAT GACATGGCGTGTCATAAAATACCAGTGGATGCCGACTTCTTGTATGCATACTCCACAGCA CCTGGTTATTATTCTTGGCGAAATTCAAAGGATGGCTCCTGGTTCATCCAGTCGCTTTGT GCCATGCTGAAACAGTATGCCGACAAGCTTGAATTTATGCACATTCTTACCCGGGTTAAC CGAAAGGTGGCAACAGAATTTGAGTCCTTTTCCTTTGACGCTACTTTTCATGCAAAGAAA CAGATTCCATGTATTGTTTCCATGCTCACAAAAGAACTCTATTTTTATCACTAA PF00656 Peptidase_C14 function peptidase activity function endopeptidase activity function cysteine-type endopeptidase activity function caspase activity function catalytic activity function hydrolase activity process protein metabolism process cellular protein metabolism process proteolysis process physiological process process metabolism process macromolecule metabolism "
drug:methyl (3S)-3-[(tert-butoxycarbonyl)amino]-4-oxopentanoaterdfs:label"methyl (3S)-3-[(tert-butoxycarbonyl)amino]-4-oxopentanoate"
drug:methyl (3S)-3-[(tert-butoxycarbonyl)amino]-4-oxopentanoaterdf:typedrugbank:drugs
drug:methyl 4-(2,3-dihydroxy-5-methylphenoxy)-2-hydroxy-6-methylbenzoatedrugbank:description" experimental This compound belongs to the diarylethers. These are organic compounds containing the dialkyl ether functional group, with the formula ROR', where R and R' are aryl groups. Diarylethers Organic Compounds Organooxygen Compounds Ethers Diarylethers Benzoic Acid Esters Salicylic Acid and Derivatives Benzylethers Benzoyl Derivatives Phenol Ethers Para Cresols Meta Cresols Catechols Toluenes Carboxylic Acid Esters Polyols Dialkyl Ethers Polyamines Enolates Enols benzylether benzoic acid or derivative phenol ether benzoyl p-cresol 1,2-diphenol m-cresol phenol derivative toluene benzene carboxylic acid ester polyol dialkyl ether enol polyamine enolate carboxylic acid derivative logP 2.89 ALOGPS logS -3.8 ALOGPS Water Solubility 5.15e-02 g/l ALOGPS logP 4.24 ChemAxon IUPAC Name methyl 4-(2,3-dihydroxy-5-methylphenoxy)-2-hydroxy-6-methylbenzoate ChemAxon Traditional IUPAC Name methyl 4-(2,3-dihydroxy-5-methylphenoxy)-2-hydroxy-6-methylbenzoate ChemAxon Molecular Weight 304.2946 ChemAxon Monoisotopic Weight 304.094688244 ChemAxon SMILES COC(=O)C1=C(C)C=C(OC2=C(O)C(O)=CC(C)=C2)C=C1O ChemAxon Molecular Formula C16H16O6 ChemAxon InChI InChI=1S/C16H16O6/c1-8-4-12(18)15(19)13(5-8)22-10-6-9(2)14(11(17)7-10)16(20)21-3/h4-7,17-19H,1-3H3 ChemAxon InChIKey InChIKey=BLXSEOJIXHWXQJ-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 96.22 ChemAxon Refractivity 80.35 ChemAxon Polarizability 30.84 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 8.79 ChemAxon pKa (strongest basic) -4.4 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 11779786 PubChem Substance 99444650 ChemSpider 9954468 PDB MGI BE0000962 Lactoylglutathione lyase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Lactoylglutathione lyase Amino acid transport and metabolism Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione GLO1 6p21.3-p21.1 None 4.92 20778.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:4323 GenAtlas GLO1 GeneCards GLO1 GenBank Gene Database D13315 GenBank Protein Database 219664 UniProtKB Q04760 UniProt Accession LGUL_HUMAN Aldoketomutase EC 4.4.1.5 Glx I Glyoxalase I Ketone-aldehyde mutase Methylglyoxalase S-D- lactoylglutathione methylglyoxal lyase >Lactoylglutathione lyase MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQK CDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNS DPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKM ATLM >555 bp ATGGCAGAACCGCAGCCCCCGTCCGGCGGCCTCACGGACGAGGCCGCCCTCAGTTGCTGC TCCGACGCGGACCCCAGTACCAAGGATTTTCTATTGCAGCAGACCATGCTACGAGTGAAG GATCCTAAGAAGTCACTGGATTTTTATACTAGAGTTCTTGGAATGACGCTAATCCAAAAA TGTGATTTTCCCATTATGAAGTTTTCACTCTACTTCTTGGCTTATGAGGATAAAAATGAC ATCCCTAAAGAAAAAGATGAAAAAATAGCCTGGGCGCTCTCCAGAAAAGCTACACTTGAG CTGACACACAATTGGGGCACTGAAGATGATGCGACCCAGAGTTACCACAATGGCAATTCA GACCCTCGAGGATTCGGTCATATTGGAATTGCTGTTCCTGATGTATACAGTGCTTGTAAA AGGTTTGAAGAACTGGGAGTCAAATTTGTGAAGAAACCTGATGATGGTAAAATGAAAGGC CTGGCATTTATTCAAGATCCTGATGGCTACTGGATTGAAATTTTGAATCCTAACAAAATG GCAACCTTAATGTAG PF00903 Glyoxalase function lyase activity function carbon-sulfur lyase activity function lactoylglutathione lyase activity function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process "
drug:methyl 4-(2,3-dihydroxy-5-methylphenoxy)-2-hydroxy-6-methylbenzoaterdfs:label"methyl 4-(2,3-dihydroxy-5-methylphenoxy)-2-hydroxy-6-methylbenzoate"
drug:methyl 4-(2,3-dihydroxy-5-methylphenoxy)-2-hydroxy-6-methylbenzoaterdf:typedrugbank:drugs
drug:methyl 4-bromo-N-[8-(hydroxyamino)-8-oxooctanoyl]-L-phenylalaninatedrugbank:description" experimental This compound belongs to the n-acyl-alpha amino acids and derivatives. These are compounds containing an alpha amino acid (or a derivative thereof) which bears an acyl group at his terminal nitrogen atom. N-acyl-alpha Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Alpha Amino Acid Esters N-acyl Amines Amphetamines and Derivatives Bromobenzenes Fatty Acid Esters Aryl Bromides Secondary Carboxylic Acid Amides Hydroxamic Acids Carboxylic Acid Esters Enolates Carboxylic Acids Polyamines Ethers Organobromides amphetamine or derivative fatty acid ester bromobenzene benzene aryl bromide aryl halide secondary carboxylic acid amide hydroxamic acid carboxamide group carboxylic acid ester enolate ether carboxylic acid polyamine organohalogen organobromide amine organonitrogen compound logP 2.44 ALOGPS logS -4.7 ALOGPS Water Solubility 7.78e-03 g/l ALOGPS logP 2.6 ChemAxon IUPAC Name methyl (2S)-3-(4-bromophenyl)-2-[7-(hydroxycarbamoyl)heptanamido]propanoate ChemAxon Traditional IUPAC Name methyl (2S)-3-(4-bromophenyl)-2-[7-(hydroxycarbamoyl)heptanamido]propanoate ChemAxon Molecular Weight 429.306 ChemAxon Monoisotopic Weight 428.094684567 ChemAxon SMILES [H][C@@](CC1=CC=C(Br)C=C1)(NC(=O)CCCCCCC(=O)NO)C(=O)OC ChemAxon Molecular Formula C18H25BrN2O5 ChemAxon InChI InChI=1S/C18H25BrN2O5/c1-26-18(24)15(12-13-8-10-14(19)11-9-13)20-16(22)6-4-2-3-5-7-17(23)21-25/h8-11,15,25H,2-7,12H2,1H3,(H,20,22)(H,21,23)/t15-/m0/s1 ChemAxon InChIKey InChIKey=UPYGSQPRAHMDPD-HNNXBMFYSA-N ChemAxon Polar Surface Area (PSA) 104.73 ChemAxon Refractivity 99.84 ChemAxon Polarizability 40.87 ChemAxon Rotatable Bond Count 12 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 8.91 ChemAxon pKa (strongest basic) -0.78 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 23640756 PubChem Substance 99444976 ChemSpider 23319843 PDB S17 BE0003985 Histone deacetylase-like amidohydrolase Alcaligenes sp. (strain DSM 11172) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Histone deacetylase-like amidohydrolase Chromatin structure and dynamics Exhibits significant levels of protein deacetylase activity comparable to those of eukaryotic HDACs in assays both with fluorogenic peptidic substrates and acetate-radiolabeled histones. Accepts proteins with epsilon-acetylated lysine residues and tritiated-acetate-prelabeled chicken histones as substrates. The natural substrate protein is not yet known hdaH None 6.19 39423.4 Alcaligenes sp. (strain DSM 11172) GeneCards hdaH GenBank Gene Database AJ580773 GenBank Protein Database 37496190 UniProtKB Q70I53 UniProt Accession HDAH_ALCSD HDAC-like amidohydrolase HDAH >Histone deacetylase-like amidohydrolase MAIGYVWNTLYGWVDTGTGSLAAANLTARMQPISHHLAHPDTKRRFHELVCASGQIEHLT PIAAVAATDADILRAHSAAHLENMKRVSNLPTGGDTGDGITMMGNGGLEIARLSAGGAVE LTRRVATGELSAGYALVNPPGHHAPHNAAMGFCIFNNTSVAAGYARAVLGMERVAILDWD VHHGNGTQDIWWNDPSVLTISLHQHLCFPPDSGYSTERGAGNGHGYNINVPLPPGSGNAA YLHAMDQVVLHALRAYRPQLIIVGSGFDASMLDPLARMMVTADGFRQMARRTIDCAADIC DGRIVFVQEGGYSPHYLPFCGLAVIEELTGVRSLPDPYHEFLAGMGGNTLLDAERAAIEE IVPLLADIR >1110 bp ATGGCCATCGGATATGTTTGGAATACGCTTTACGGCTGGGTAGATACCGGCACCGGCAGC CTGGCCGCTGCCAACCTGACGGCGCGCATGCAGCCCATCAGCCATCACCTGGCGCATCCT GACACCAAGCGCAGGTTTCACGAACTGGTCTGCGCCTCCGGTCAGATCGAGCATCTGACG CCGATCGCTGCCGTCGCCGCCACGGATGCGGATATTCTGCGCGCCCATTCCGCCGCGCAC CTGGAAAACATGAAACGCGTCAGCAATCTGCCCACGGGCGGGGATACTGGCGACGGCATC ACCATGATGGGCAACGGTGGCCTGGAAATCGCCCGGCTGTCTGCCGGTGGGGCCGTTGAG CTGACGCGCCGGGTTGCAACAGGCGAACTGAGTGCCGGTTATGCACTGGTCAATCCGCCC GGGCACCATGCGCCGCACAACGCCGCCATGGGTTTTTGCATCTTCAACAATACCTCGGTA GCGGCTGGCTATGCCCGCGCAGTCCTGGGCATGGAGCGAGTCGCCATCCTCGACTGGGAT GTGCATCATGGCAACGGCACCCAGGATATCTGGTGGAACGATCCCTCCGTCTTGACCATT TCGCTGCACCAGCATCTGTGCTTTCCGCCCGACTCCGGCTACAGCACCGAACGCGGCGCA GGCAACGGACATGGCTATAACATCAACGTACCCCTGCCTCCCGGCAGCGGCAATGCCGCC TATCTCCATGCCATGGATCAGGTCGTCCTGCATGCCCTGCGCGCCTACCGGCCGCAACTC ATCATTGTCGGTTCCGGTTTCGATGCCAGCATGCTGGATCCGCTGGCGCGCATGATGGTG ACCGCCGATGGCTTCCGTCAAATGGCACGCCGGACCATCGACTGCGCAGCGGATATCTGC GATGGACGCATCGTATTCGTCCAGGAAGGCGGCTATAGCCCCCACTACCTGCCTTTCTGC GGGCTGGCCGTCATCGAGGAGCTGACCGGCGTACGCAGCCTGCCCGATCCTTACCACGAG TTCCTGGCGGGCATGGGTGGCAATACGCTGCTGGATGCCGAACGCGCCGCCATCGAGGAG ATCGTACCGCTGCTGGCGGATATCCGCTGA PF00850 Hist_deacetyl "
drug:methyl 4-bromo-N-[8-(hydroxyamino)-8-oxooctanoyl]-L-phenylalaninaterdfs:label"methyl 4-bromo-N-[8-(hydroxyamino)-8-oxooctanoyl]-L-phenylalaninate"
drug:methyl 4-bromo-N-[8-(hydroxyamino)-8-oxooctanoyl]-L-phenylalaninaterdf:typedrugbank:drugs
drug:methyl L-phenylalaninatedrugbank:description" experimental This compound belongs to the alpha amino acid esters. These are ester derivatives of alpha amino acids. Alpha Amino Acid Esters Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Amphetamines and Derivatives Fatty Acid Esters Carboxylic Acid Esters Ethers Enolates Polyamines Monoalkylamines amphetamine or derivative fatty acid ester benzene carboxylic acid ester polyamine ether enolate primary amine primary aliphatic amine amine organonitrogen compound logP 0.8 ALOGPS logS -1.8 ALOGPS Water Solubility 3.11e+00 g/l ALOGPS logP 1.22 ChemAxon IUPAC Name methyl (2S)-2-amino-3-phenylpropanoate ChemAxon Traditional IUPAC Name methyl (2S)-2-amino-3-phenylpropanoate ChemAxon Molecular Weight 179.2157 ChemAxon Monoisotopic Weight 179.094628665 ChemAxon SMILES [H][C@](N)(CC1=CC=CC=C1)C(=O)OC ChemAxon Molecular Formula C10H13NO2 ChemAxon InChI InChI=1S/C10H13NO2/c1-13-10(12)9(11)7-8-5-3-2-4-6-8/h2-6,9H,7,11H2,1H3/t9-/m0/s1 ChemAxon InChIKey InChIKey=VSDUZFOSJDMAFZ-VIFPVBQESA-N ChemAxon Polar Surface Area (PSA) 52.32 ChemAxon Refractivity 49.89 ChemAxon Polarizability 19.38 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 6.97 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 736234 PubChem Substance 99443309 ChemSpider 643364 PDB 0A9 BE0001713 Fimbrial protein Neisseria gonorrhoeae # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Fimbrial protein Cell motility This protein is the predominant Neisseria surface antigen, which allows adhesion of the bacterium to various host cells pilE1 None 7.4 17945.0 Neisseria gonorrhoeae GenBank Gene Database K02078 GenBank Protein Database 150288 UniProtKB P02974 UniProt Accession FMM1_NEIGO Fimbrial protein precursor MS11 antigen Pilin >Fimbrial protein precursor MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLN HGKWPENNTSAGVASPPSDIKGKYVKEVEVKNGVVTATMLSSGVNNEIKGKKLSLWARRE NGSVKWFCGQPVTRTDDDTVADAKDGKEIDTKHLPSTCRDNFDAK >501 bp ATGAATACCCTTCAAAAAGGCTTTACCCTTATCGAGCTGATGATTGTGATCGCTATCGTC GGCATTTTGGCGGCAGTCGCCCTTCCCGCCTACCAAGACTACACCGCCCGCGCGCAAGTT TCCGAAGCCATCCTTTTGGCCGAAGGTCAAAAATCAGCCGTCACCGAGTATTACCTGAAT CACGGCAAATGGCCGGAAAACAACACTTCTGCCGGCGTGGCATCCCCCCCCTCCGACATC AAAGGCAAATATGTTAAAGAGGTTGAAGTTAAAAACGGCGTCGTTACCGCCACAATGCTT TCAAGCGGCGTAAACAATGAAATCAAAGGCAAAAAACTCTCCCTGTGGGCCAGGCGTGAA AACGGTTCGGTAAAATGGTTCTGCGGACAGCCGGTTACGCGCACCGACGACGACACCGTT GCCGACGCCAAAGACGGCAAAGAAATCGACACCAAGCACCTGCCGTCAACCTGCCGCGAT AAGGCATCTGATGCCAAATGA PF07963 N_methyl PF00114 Pilin component organelle component protein complex component fimbrium component type II protein secretion system complex component non-membrane-bound organelle component intracellular non-membrane-bound organelle function protein transporter activity function transporter activity process type II protein secretion system process cellular process process cell adhesion process localization process establishment of localization process physiological process process establishment of protein localization process protein secretion BE0000048 Prothrombin Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Prothrombin Involved in blood clotting cascade Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C F2 11p11-q12 Secreted protein; extracellular space None 5.7 70037.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3535 GenAtlas F2 GeneCards F2 GenBank Gene Database M17262 GenBank Protein Database 339641 UniProtKB P00734 UniProt Accession THRB_HUMAN Activated Factor II [IIa] Coagulation factor II EC 3.4.21.5 Prothrombin precursor Thrombin >Prothrombin precursor MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY GFYTHVFRLKKWIQKVIDQFGE >1869 bp ATGGCGCACGTCCGAGGCTTGCAGCTGCCTGGCTGCCTGGCCCTGGCTGCCCTGTGTAGC CTTGTGCACAGCCAGCATGTGTTCCTGGCTCCTCAGCAAGCACGGTCGCTGCTCCAGCGG GTCCGGCGAGCCAACACCTTCTTGGAGGAGGTGCGCAAGGGCAACCTAGAGCGAGAGTGC GTGGAGGAGACGTGCAGCTACGAGGAGGCCTTCGAGGCTCTGGAGTCCTCCACGGCTACG GATGTGTTCTGGGCCAAGTACACAGCTTGTGAGACAGCGAGGACGCCTCGAGATAAGCTT GCTGCATGTCTGGAAGGTAACTGTGCTGAGGGTCTGGGTACGAACTACCGAGGGCATGTG AACATCACCCGGTCAGGCATTGAGTGCCAGCTATGGAGGAGTCGCTACCCACATAAGCCT GAAATCAACTCCACTACCCATCCTGGGGCCGACCTACAGGAGAATTTCTGCCGCAACCCC GACAGCAGCACCACGGGACCCTGGTGCTACACTACAGACCCCACCGTGAGGAGGCAGGAA TGCAGCATCCCTGTCTGTGGCCAGGATCAAGTCACTGTAGCGATGACTCCACGCTCCGAA GGCTCCAGTGTGAATCTGTCACCTCCATTGGAGCAGTGTGTCCCTGATCGGGGGCAGCAG TACCAGGGGCGCCTGGCGGTGACCACACATGGGCTCCCCTGCCTGGCCTGGGCCAGCGCA CAGGCCAAGGCCCTGAGCAAGCACCAGGACTTCAACTCAGCTGTGCAGCTGGTGGAGAAC TTCTGCCGCAACCCAGACGGGGATGAGGAGGGCGTGTGGTGCTATGTGGCCGGGAAGCCT GGCGACTTTGGGTACTGCGACCTCAACTATTGTGAGGAGGCCGTGGAGGAGGAGACAGGA GATGGGCTGGATGAGGACTCAGACAGGGCCATCGAAGGGCGTACCGCCACCAGTGAGTAC CAGACTTTCTTCAATCCGAGGACCTTTGGCTCGGGAGAGGCAGACTGTGGGCTGCGACCT CTGTTCGAGAAGAAGTCGCTGGAGGACAAAACCGAAAGAGAGCTCCTGGAATCCTACATC GACGGGCGCATTGTGGAGGGCTCGGATGCAGAGATCGGCATGTCACCTTGGCAGGTGATG CTTTTCCGGAAGAGTCCCCAGGAGCTGCTGTGTGGGGCCAGCCTCATCAGTGACCGCTGG GTCCTCACCGCCGCCCACTGCCTCCTGTACCCGCCCTGGGACAAGAACTTCACCGAGAAT GACCTTCTGGTGCGCATTGGCAAGCACTCCCGCACAAGGTACGAGCGAAACATTGAAAAG ATATCCATGTTGGAAAAGATCTACATCCACCCCAGGTACAACTGGCGGGAGAACCTGGAC CGGGACATTGCCCTGATGAAGCTGAAGAAGCCTGTTGCCTTCAGTGACTACATTCACCCT GTGTGTCTGCCCGACAGGGAGACGGCAGCCAGCTTGCTCCAGGCTGGATACAAGGGGCGG GTGACAGGCTGGGGCAACCTGAAGGAGACGTGGACAGCCAACGTTGGTAAGGGGCAGCCC AGTGTCCTGCAGGTGGTGAACCTGCCCATTGTGGAGCGGCCGGTCTGCAAGGACTCCACC CGGATCCGCATCACTGACAACATGTTCTGTGCTGGTTACAAGCCTGATGAAGGGAAACGA GGGGATGCCTGTGAAGGTGACAGTGGGGGACCCTTTGTCATGAAGAGCCCCTTTAACAAC CGCTGGTATCAAATGGGCATCGTCTCATGGGGTGAAGGCTGTGACCGGGATGGGAAATAT GGCTTCTACACACATGTGTTCCGCCTGAAGAAGTGGATACAGAAGGTCATTGATCAGTTT GGAGAGTAG PF00594 Gla PF00051 Kringle PF00089 Trypsin component extracellular region function catalytic activity function thrombin activity function hydrolase activity function calcium ion binding function peptidase activity function ion binding function endopeptidase activity function cation binding function serine-type endopeptidase activity function binding process blood coagulation process metabolism process macromolecule metabolism process protein metabolism process proteolysis process cellular protein metabolism process organismal physiological process process regulation of body fluids process physiological process process hemostasis "
drug:methyl L-phenylalaninaterdfs:label"methyl L-phenylalaninate"
drug:methyl L-phenylalaninaterdf:typedrugbank:drugs
drug:methyl [(1E,5R)-5-{(3S)-3-[(2E,4E)-2,5-dimethylocta-2,4-dienoyl]-2,4-dioxo-3,4-dihydro-2H-pyran-6-yl}hexylidene]carbamatedrugbank:description" experimental This compound belongs to the dihydropyranones. These are compounds containing an hydrogenated pyran ring which bears a ketone, and contains one double bond. Dihydropyranones Organic Compounds Heterocyclic Compounds Pyrans Pyranones and Derivatives Dicarboxylic Acids and Derivatives Acryloyl Compounds Enones Shiff Bases Carboxylic Acid Esters Polyamines Enolates Ethers Enols dicarboxylic acid derivative acryloyl-group enone carboxylic acid ester aldimine ketone shiff base ether enolate enol polyamine carboxylic acid derivative amine carbonyl group imine organonitrogen compound logP 4.39 ALOGPS logS -5.4 ALOGPS Water Solubility 1.73e-03 g/l ALOGPS logP 4.54 ChemAxon IUPAC Name methyl N-[(1E,5R)-5-[(3S)-3-[(2E,4E)-2,5-dimethylocta-2,4-dienoyl]-2,4-dioxo-3,4-dihydro-2H-pyran-6-yl]hexylidene]carbamate ChemAxon Traditional IUPAC Name methyl N-[(1E,5R)-5-[(5S)-5-[(2E,4E)-2,5-dimethylocta-2,4-dienoyl]-4,6-dioxo-5H-pyran-2-yl]hexylidene]carbamate ChemAxon Molecular Weight 417.4953 ChemAxon Monoisotopic Weight 417.215137729 ChemAxon SMILES [H][C@@](C)(CCC\C=N\C(=O)OC)C1=CC(=O)[C@@]([H])(C(=O)C(\C)=C\C=C(/C)CCC)C(=O)O1 ChemAxon Molecular Formula C23H31NO6 ChemAxon InChI InChI=1S/C23H31NO6/c1-6-9-15(2)11-12-17(4)21(26)20-18(25)14-19(30-22(20)27)16(3)10-7-8-13-24-23(28)29-5/h11-14,16,20H,6-10H2,1-5H3/b15-11+,17-12+,24-13+/t16-,20+/m1/s1 ChemAxon InChIKey InChIKey=LTDLIPXLSBMTFP-HQCMHGIWSA-N ChemAxon Polar Surface Area (PSA) 99.1 ChemAxon Refractivity 116.4 ChemAxon Polarizability 45.49 ChemAxon Rotatable Bond Count 11 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest acidic) 0.98 ChemAxon pKa (strongest basic) -2.5 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937136 PubChem Substance 99444737 PDB NE6 BE0004261 DNA-directed RNA polymerase subunit alpha Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown DNA-directed RNA polymerase subunit alpha Transcription DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates rpoA Cytoplasmic None 4.64 35012.9 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) GeneCards rpoA GenBank Gene Database AB024328 GenBank Protein Database 4519419 UniProtKB Q5SHR6 UniProt Accession RPOA_THET8 RNA polymerase subunit alpha RNAP subunit alpha Transcriptase subunit alpha >DNA-directed RNA polymerase subunit alpha MLDSKLKAPVFTVRTQGREYGEFVLEPLERGFGVTLGNPLRRILLSSIPGTAVTSVYIED VLHEFSTIPGVKEDVVEIILNLKELVVRFLNPSLQTVTLLLKAEGPKEVKARDFLPVADV EIMNPDLHIATLEEGGRLNMEVRVDRGVGYVPAEKHGIKDRINAIPVDAVFSPVRRVAFQ VEDTRLGQRTDLDKLTLRIWTDGSVTPLEALNQAVEILREHLTYFSNPQAAAVAAPEEAK EPEAPPEQEEELDLPLEELGLSTRVLHSLKEEGIESVRALLALNLKDLKNIPGIGERSLE EIKEALEKKGFTLKE >114 bp ATGAAGGTGCGCGCGTCGGTCAAGAGGATCTGCGACAAGTGCAAGGTGATCCGCCGGCAC GGGCGGGTCTACGTCATCTGCGAGAACCCCAAGCATAAGCAGCGGCAGGGTTAG PF01000 RNA_pol_A_bac PF03118 RNA_pol_A_CTD PF01193 RNA_pol_L component cell component intracellular function protein binding function protein dimerization activity function transferase activity function transferase activity, transferring phosphorus-containing groups function nucleic acid binding function binding function DNA binding function catalytic activity function nucleotidyltransferase activity function DNA-directed RNA polymerase activity process transcription, DNA-dependent process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process physiological process process metabolism process cellular metabolism process transcription BE0003367 DNA-directed RNA polymerase subunit beta Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown DNA-directed RNA polymerase subunit beta Involved in DNA binding DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates rpoB Cytoplasmic None 5.73 125266.0 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) GenBank Gene Database AB083789 UniProtKB Q8RQE9 UniProt Accession RPOB_THET8 EC 2.7.7.6 RNA polymerase subunit beta RNAP beta subunit Transcriptase beta chain >DNA-directed RNA polymerase beta chain MEIKRFGRIREVIPLPPLTEIQVESYRRALQADVPPEKRENVGIQAAFRETFPIEEEDKG KGGLVLDFLEYRLGEPPFPQDECREKDLTYQAPLYARLQLIHKDTGLIKEDEVFLGHIPL MTEDGSFIINGADRVIVSQIHRSPGVYFTPDPARPGRYIASIIPLPKRGPWIDLEVEPNG VVSMKVNKRKFPLVLLLRVLGYDQETLARELGAYGELVQGLMDESVFAMRPEEALIRLFT LLRPGDPPKRDKAVAYVYGLIADPRRYDLGEAGRYKAEEKLGIRLSGRTLARFEDGEFKD EVFLPTLRYLFALTAGVPGHEVDDIDHLGNRRIRTVGELMTDQFRVGLARLARGVRERML MGSEDSLTPAKLVNSRPLEAAIREFFSRSQLSQFKDETNPLSSLRHKRRISALGPGGLTR ERAGFDVRDVHRTHYGRICPVETPEGANIGLITSLAAYARVDELGFIRTPYRRVVGGVVT DEVVYMTATEEDRYTIAQANTPLEGNRIAAERVVARRKGEPVIVSPEEVEFMDVSPKQVF SVNTNLIPFLEHDDANRALMGSNMQTQAVPLIRAQAPVVMTGLEERVVRDSLAALYAEED GEVAKVDGNRIVVRYEDGRLVEYPLRRFYRSNQGTALDQRPRVVVGQRVRKGDLLADGPA SENGFLALGQNVLVAIMPFDGYNFEDAIVISEELLKRDFYTSIHIERYEIEARDTKLGPE RITRDIPHLSEAALRDLDEEGVVRIGAEVKPGDILVGRTSFKGESEPTPEERLLRSIFGE KARDVKDTSLRVPPGEGGIVVRTVRLRRGDPGVELKPGVREVVRVYVAQKRKLQVGDKLA NRHGNKGVVAKILPVEDMPHLPDGTPVDVILNPLGVPSRMNLGQILETHLGLAGYFLGQR YISPIFDGAKEPEIKELLAQAFEVYFGKRKGEGFGVDKREVEVLRRAEKLGLVTPGKTPE EQLKELFLQGKVVLYDGRTGEPIEGPIVVGQMFIMKLYHMVEDKMHARSTGPYSLITQQP LGGKAQFGGQRFGEMEVWALEAYGAAHTLQEMLTLKSDDIEGRNAAYEAIIKGEDVPEPS VPESFRVLVKELQALALDVQTLDEKDNPVDIFEGLASKR >3360 bp ATGGAGATCAAGCGGTTCGGTCGCATCCGAGAGGTTATCCCCCTTCCACCCCTCACCGAG ATCCAGGTGGAGTCCTACCGCAGGGCCCTGCAGGCCGACGTCCCCCCGGAGAAGCGGGAG AACGTCGGCATCCAGGCGGCCTTCCGGGAGACCTTCCCCATTGAGGAGGAGGACAAGGGC AAGGGCGGTTTGGTGCTGGACTTCCTGGAGTACCGCCTGGGCGAGCCCCCCTTCCCCCAG GACGAGTGCCGGGAGAAGGACCTCACCTACCAGGCCCCCCTCTACGCCCGGCTCCAGCTC ATCCACAAGGACACGGGCCTCATCAAGGAGGACGAGGTCTTCCTGGGGCACATCCCCCTG ATGACCGAGGACGGCTCCTTCATCATCAACGGGGCCGACCGGGTCATCGTCTCCCAGATC CACCGCTCCCCCGGGGTCTACTTCACCCCCGACCCCGCCCGGCCCGGGCGCTACATCGCC AGCATCATCCCCCTGCCCAAGCGGGGCCCCTGGATTGACCTGGAGGTGGAGCCGAACGGC GTCGTCTCCATGAAGGTCAACAAGCGGAAGTTCCCCCTGGTCCTCCTCCTTCGGGTCCTG GGGTACGACCAGGAGACCCTGGCCCGGGAGCTTGGGGCCTACGGGGAGCTGGTCCAGGGC CTCATGGACGAGAGCGTCTTCGCCATGCGCCCCGAGGAGGCTCTGATCCGCCTCTTCACC CTCCTCCGCCCCGGGGACCCGCCCAAGCGGGACAAGGCCGTGGCCTACGTCTACGGCCTC ATCGCCGACCCCAGGCGGTACGACCTGGGCGAGGCCGGGCGGTACAAGGCGGAGGAGAAG CTGGGGATCCGCCTCTCGGGCCGCACCCTGGCCCGCTTTGAGGACGGGGAGTTCAAGGAC GAGGTCTTCCTCCCCACCCTCCGCTACCTCTTCGCCCTCACCGCCGGGGTCCCGGGCCAC GAGGTGGACGACATTGACCACCTGGGCAACCGCCGCATCCGCACCGTGGGGGAGCTCATG ACCGACCAGTTCCGGGTGGGGCTCGCCCGCCTCGCCCGGGGGGTGCGGGAGCGGATGCTC ATGGGCTCGGAGGACAGCCTCACCCCGGCCAAGCTGGTGAACAGCCGCCCCTTGGAGGCC GCCATCCGGGAGTTCTTCAGCCGCAGCCAGCTTTCCCAGTTCAAGGACGAGACCAACCCC CTCTCCTCCCTGCGCCACAAGCGGCGGATCTCCGCCCTGGGCCCGGGCGGCCTCACCCGG GAGCGGGCGGGGTTTGACGTGCGCGACGTCCACCGCACCCACTACGGGCGCATCTGCCCC GTGGAGACCCCCGAGGGCGCCAACATCGGCCTCATCACCTCCTTGGCGGCCTACGCCCGG GTGGACGAGCTGGGCTTCATCCGCACCCCCTACCGCCGGGTGGTGGGCGGGGTGGTCACC GACGAGGTGGTCTACATGACGGCCACCGAGGAGGACCGCTACACCATCGCCCAGGCCAAC ACCCCCCTGGAGGGGAACCGGATCGCGGCCGAGCGGGTGGTGGCCCGGAGGAAGGGGGAG CCCGTGATCGTGAGCCCGGAAGAGGTGGAGTTCATGGACGTCTCCCCCAAGCAGGTCTTC TCCGTGAACACCAACCTCATTCCCTTCCTGGAGCACGACGACGCCAACCGGGCCCTCATG GGCTCCAACATGCAGACCCAGGCCGTGCCCCTCATCCGGGCCCAGGCCCCCGTGGTGATG ACGGGCCTCGAGGAGCGGGTGGTGCGGGACTCCCTGGCCGCCCTCTACGCCGAGGAGGAC GGGGAGGTGGCCAAGGTGGACGGCAACCGCATCGTCGTGCGCTACGAGGACGGCCGCCTG GTGGAGTACCCCTTGCGCCGCTTCTACCGCTCCAACCAGGGTACGGCCCTGGACCAGCGC CCCCGGGTGGTGGTGGGGCAGCGGGTGCGCAAAGGGGACCTCCTCGCCGACGGCCCCGCC TCCGAGAACGGCTTCCTGGCCCTGGGGCAGAACGTCCTCGTGGCCATCATGCCCTTTGAC GGGTACAACTTTGAGGACGCCATCGTCATCAGCGAGGAGCTCCTCAAGCGGGACTTCTAC ACCTCCATCCACATTGAGCGCTACGAGATTGAGGCCCGGGACACCAAGCTTGGCCCCGAG CGGATCACCCGGGACATCCCCCACCTCTCCGAGGCCGCCCTAAGGGACCTGGACGAGGAG GGCGTGGTGCGCATCGGCGCCGAGGTGAAGCCCGGGGACATCCTCGTGGGGCGGACCAGC TTCAAGGGCGAGTCCGAGCCCACCCCCGAGGAGAGGCTCCTCCGCTCCATCTTCGGCGAG AAGGCCCGGGACGTGAAGGACACCTCCCTCCGGGTGCCGCCCGGCGAAGGGGGGATCGTG GTCCGCACCGTCCGGCTGCGGCGGGGCGACCCCGGGGTGGAGCTCAAGCCCGGGGTGCGG GAGGTGGTCCGGGTCTACGTGGCCCAGAAGCGCAAGCTCCAGGTGGGGGACAAGCTCGCC AACCGCCACGGGAACAAGGGGGTGGTGGCCAAGATCCTCCCCGTGGAGGACATGCCCCAC CTGCCCGACGGCACCCCCGTGGACGTGATCCTGAACCCCCTGGGCGTCCCCAGCCGGATG AACCTGGGGCAGATCCTGGAGACCCACCTGGGCCTCGCCGGGTACTTCCTGGGCCAGCGC TACATCTCCCCCATCTTTGACGGGGCCAAGGAGCCCGAGATCAAGGAGCTCCTCGCCCAG GCCTTTGAGGTCTACTTCGGCAAGCGCAAGGGCGAGGGCTTCGGCGTGGACAAGCGGGAG GTGGAGGTCCTCCGCCGGGCGGAGAAGCTCGGCCTCGTCACCCCGGGCAAGACCCCGGAG GAGCAGCTTAAGGAGCTCTTCCTCCAGGGCAAGGTGGTCCTCTACGACGGCCGCACGGGC GAGCCCATTGAGGGCCCCATCGTGGTGGGACAGATGTTCATCATGAAGCTCTACCACATG GTGGAGGACAAGATGCACGCCCGCTCCACGGGGCCCTACTCCCTCATCACCCAGCAGCCC CTGGGCGGGAAGGCCCAGTTCGGCGGCCAGCGCTTCGGGGAGATGGAGGTCTGGGCCCTC GAGGCCTATGGGGCGGCCCACACCCTCCAGGAGATGCTCACCCTTAAGTCCGACGACATT GAGGGCAGGAACGCCGCCTACGAGGCCATCATCAAGGGGGAGGACGTTCCCGAGCCCAGC GTCCCCGAGTCCTTCCGCGTGCTGGTGAAGGAGCTCCAGGCCTTGGCCTTGGACGTGCAG ACCCTGGACGAGAAGGACAACCCCGTGGACATCTTTGAGGGGTTGGCCTCCAAGCGGTGA PF04563 RNA_pol_Rpb2_1 PF04561 RNA_pol_Rpb2_2 PF04565 RNA_pol_Rpb2_3 PF00562 RNA_pol_Rpb2_6 PF04560 RNA_pol_Rpb2_7 function catalytic activity function transferase activity function transferase activity, transferring phosphorus-containing groups function nucleic acid binding function DNA binding function nucleotidyltransferase activity function binding function DNA-directed RNA polymerase activity process metabolism process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process physiological process process transcription BE0003368 DNA-directed RNA polymerase subunit beta' Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown DNA-directed RNA polymerase subunit beta' Involved in DNA binding DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates rpoC Cytoplasmic None 6.32 170759.0 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) GenBank Gene Database AB083790 UniProtKB Q8RQE8 UniProt Accession RPOC_THET8 EC 2.7.7.6 RNA polymerase beta' subunit RNAP beta' subunit Transcriptase beta' chain >DNA-directed RNA polymerase beta' chain MKKEVRKVRIALASPEKIRSWSYGEVEKPETINYRTLKPERDGLFDERIFGPIKDYECAC GKYKRQRFEGKVCERCGVEVTKSIVRRYRMGHIELATPAAHIWFVKDVPSKIGTLLDLSA TELEQVLYFSKYIVLDPKGAILNGVPVEKRQLLTDEEYRELRYGKQETYPLPPGVDALVK DGEEVVKGQELAPGVVSRLDGVALYRFPRRVRVEYVKKERAGLRLPLAAWVEKEAYKPGE ILAELPEPYLFRAEEEGVVELKELEEGAFLVLRREDEPVATYFLPVGMTPLVVHGEIVEK GQPLAEAKGLLRMPRQVRAAQVEAEEEGETVYLTLFLEWTEPKDYRVQPHMNVVVPEGAR VEAGDKIVAAIDPEEEVIAEAEGVVHLHEPASILVVKARVYPFEDDVEVSTGDRVAPGDV LADGGKVKSDVYGRVEVDLVRNVVRVVESYDIDARMGAEAIQQLLKELDLEALEKELLEE MKHPSRARRAKARKRLEVVRAFLDSGNRPEWMILEAVPVLPPDLRPMVQVDGGRFATSDL NDLYRRLINRNNRLKKLLAQGAPEIIIRNEKRMLQEAVDALLDNGRRGAPVTNPGSDRPL RSLTDILSGKQGRFRQNLLGKRVDYSGRSVIVVGPQLKLHQCGLPKRMALELFKPFLLKK MEEKGIAPNVKAARRMLERQRDIKDEVWDALEEVIHGKVVLLNRAPTLHRLGIQAFQPVL VEGQSIQLHPLVCEAFNADFDGDQMAVHVPLSSFAQAEARIQMLSAHNLLSPASGEPLAK PSRDIILGLYYITQVRKEKKGAGLEFATPEEALAAHERGEVALNAPIKVAGRETSVGRLK YVFANPDEALLAVAHGIVDLQDVVTVRYMGKRLETSPGRILFARIVAEAVEDEKVAWELI QLDVPQEKNSLKDLVYQAFLRLGMEKTARLLDALKYYGFTFSTTSGITIGIDDAVIPEEK KQYLEEADRKLLQIEQAYEMGFLTDRERYDQILQLWTETTEKVTQAVFKNFEENYPFNPL YVMAQSGARGNPQQIRQLCGLRGLMQKPSGETFEVPVRSSFREGLTVLEYFISSHGARKG GADTALRTADSGYLTRKLVDVTHEIVVREADCGTTNYISVPLFQPDEVTRSLRLRKRADI EAGLYGRVLAREVEVLGVRLEEGRYLSMDDVHLLIKAAEAGEIQEVPVRSPLTCQTRYGV CQKCYGYDLSMARPVSIGEAVGIVAAQSIGEPGTQLTMRTFHTGGVAGAADITQGLPRVI ELFEARRPKAKAVISEIDGVVRIEETEEKLSVFVESEGFSKEYKLPKEARLLVKDGDYVE AGQPLTRGAIDPHQLLEAKGPEAVERYLVEEIQKVYRAQGVKLHDKHIEIVVRQMMKYVE VTDPGDSRLLEGQVLEKWDVEALNERLIAEGKTPVAWKPLLMGVTKSALSTKSWLSAASF QNTTHVLTEAAIAGKKDELIGLKENVILGRLIPAGTGSDFVRFTQVVDQKTLKAIEEARK EAVEAKERPAARRGVKREQPGKQA >4575 bp ATGAAAAAAGAGGTTCGTAAGGTTCGCATCGCTTTGGCCTCCCCGGAGAAGATCCGCTCC TGGAGCTACGGGGAGGTGGAGAAGCCCGAGACCATCAACTACCGCACCCTCAAGCCCGAG CGGGACGGCCTCTTTGACGAGCGCATCTTCGGCCCCATCAAGGACTACGAGTGCGCCTGC GGCAAGTACAAGCGCCAGCGCTTTGAGGGCAAGGTGTGCGAGCGGTGTGGCGTGGAGGTG ACGAAGAGCATCGTCCGCCGCTACCGCATGGGGCACATTGAGCTCGCCACCCCCGCCGCC CACATCTGGTTCGTCAAGGACGTCCCCTCCAAGATCGGGACCCTCCTGGACCTTTCCGCC ACCGAGCTGGAGCAGGTCCTCTACTTCAGCAAGTACATCGTCTTGGATCCCAAGGGGGCC ATCCTGAACGGGGTCCCGGTGGAGAAGCGCCAGCTCCTCACCGACGAGGAGTACCGGGAG CTCCGCTACGGCAAGCAGGAGACCTACCCCCTGCCCCCCGGGGTGGACGCGCTGGTGAAG GACGGGGAGGAGGTGGTAAAGGGCCAGGAGCTTGCCCCCGGGGTGGTGAGCCGCCTGGAC GGCGTGGCCCTCTACCGCTTCCCCCGCCGCGTCCGGGTGGAGTACGTGAAGAAGGAGCGG GCCGGGCTCAGGCTTCCCCTCGCCGCCTGGGTGGAGAAGGAGGCCTACAAGCCCGGCGAA ATCCTCGCCGAGCTCCCCGAGCCCTACCTCTTCCGGGCCGAGGAGGAGGGCGTGGTGGAG CTTAAGGAGCTGGAGGAAGGGGCTTTCCTCGTCCTCCGCCGGGAGGACGAGCCGGTGGCC ACCTACTTCCTCCCCGTGGGCATGACGCCCCTCGTGGTCCACGGGGAGATCGTGGAGAAG GGCCAGCCCCTGGCCGAGGCCAAGGGCCTTCTCCGCATGCCCCGCCAGGTCCGGGCCGCC CAGGTGGAGGCGGAGGAGGAGGGGGAGACGGTCTACCTCACCCTCTTCCTGGAGTGGACG GAGCCCAAGGACTACCGCGTCCAGCCCCACATGAACGTGGTGGTCCCCGAGGGGGCCCGG GTGGAGGCGGGGGACAAGATCGTGGCCGCCATTGACCCCGAGGAGGAGGTCATCGCCGAG GCCGAGGGGGTGGTCCACCTCCACGAGCCCGCCAGCATCCTGGTGGTCAAGGCCCGGGTC TACCCCTTTGAGGACGACGTGGAGGTTTCCACCGGGGACCGGGTGGCCCCGGGGGACGTC CTCGCCGACGGGGGCAAGGTCAAAAGCGACGTCTACGGCCGGGTGGAGGTGGACCTGGTC CGCAACGTGGTCCGGGTGGTGGAGTCCTACGACATTGACGCCCGCATGGGGGCCGAGGCC ATCCAGCAGCTCCTCAAGGAGCTGGACCTCGAGGCCCTGGAGAAGGAGCTTCTGGAGGAG ATGAAGCACCCCTCCCGGGCCCGGCGGGCCAAGGCCAGGAAGCGCCTGGAGGTGGTGCGG GCCTTCCTGGACTCGGGGAACCGGCCCGAGTGGATGATCCTCGAGGCCGTCCCCGTCCTT CCCCCGGACCTCCGGCCCATGGTCCAGGTGGACGGCGGCCGCTTCGCCACGAGCGACCTC AACGACCTCTACCGCCGCCTCATCAACCGCAACAACCGGCTGAAGAAGCTCTTGGCCCAG GGGGCCCCCGAGATCATCATCCGCAACGAGAAGCGGATGCTCCAGGAGGCGGTGGACGCC CTCCTGGACAACGGCCGCCGCGGCGCTCCCGTGACCAACCCCGGCTCCGACCGGCCCCTC CGTAGCCTCACCGACATCCTCTCCGGCAAGCAGGGCCGCTTCCGCCAGAACCTCTTGGGC AAGCGGGTGGACTACTCGGGCCGGAGCGTGATCGTGGTGGGGCCCCAGCTCAAGCTCCAC CAGTGCGGCCTGCCCAAGCGGATGGCCCTGGAGCTCTTCAAGCCCTTCCTCCTCAAGAAG ATGGAGGAGAAGGGCATCGCCCCCAACGTCAAGGCGGCGCGGCGCATGCTGGAGCGCCAG CGGGACATCAAGGACGAGGTGTGGGACGCCTTGGAGGAGGTGATCCACGGCAAGGTGGTC CTCTTGAACCGCGCCCCCACCCTGCACCGCTTGGGCATCCAGGCCTTCCAGCCCGTCTTG GTGGAGGGGCAGTCCATCCAGCTCCACCCCCTGGTCTGCGAGGCCTTCAACGCCGACTTT GACGGGGACCAGATGGCCGTCCACGTCCCCCTCTCCTCCTTCGCCCAGGCCGAGGCCCGC ATCCAGATGCTCTCCGCCCACAACCTCCTCTCCCCGGCCTCCGGGGAGCCCCTGGCCAAG CCCAGCCGGGACATCATCCTGGGCCTCTACTACATCACCCAGGTGCGCAAGGAGAAGAAG GGGGCGGGCCTGGAGTTCGCCACCCCCGAGGAGGCCCTGGCCGCCCACGAGCGGGGAGAG GTGGCCCTGAACGCCCCCATCAAGGTGGCGGGCAGGGAGACCAGCGTGGGCCGGCTCAAG TACGTCTTCGCCAACCCCGACGAGGCCCTCCTCGCCGTGGCCCACGGCATCGTGGACCTG CAGGACGTGGTCACCGTCCGCTACATGGGCAAGCGGCTGGAGACGAGCCCGGGCCGCATC CTCTTCGCCCGCATCGTGGCCGAGGCGGTGGAGGACGAGAAGGTGGCCTGGGAGCTCATC CAGCTGGACGTGCCCCAGGAGAAGAACTCCCTCAAGGACCTGGTCTACCAGGCCTTCCTC CGCCTGGGGATGGAGAAGACCGCCAGGCTCCTGGACGCCCTCAAGTACTACGGCTTCACC TTCTCCACCACGAGCGGCATCACCATCGGCATTGACGACGCCGTGATCCCGGAGGAGAAG AAGCAGTACCTGGAGGAGGCCGACCGCAAGCTCCTCCAGATTGAGCAGGCCTACGAGATG GGCTTCCTCACCGACCGGGAGCGGTACGACCAGATCCTCCAGCTCTGGACCGAGACCACG GAGAAGGTCACCCAGGCGGTCTTCAAGAACTTTGAGGAGAACTACCCCTTCAACCCCCTC TACGTCATGGCCCAGTCCGGGGCCCGGGGCAACCCGCAGCAGATCCGCCAGCTCTGCGGC CTGCGCGGCCTCATGCAGAAGCCCTCGGGCGAGACCTTTGAGGTGCCGGTGCGCTCCTCC TTCCGCGAGGGCCTCACCGTCTTGGAGTACTTCATCTCCAGCCACGGGGCCCGTAAGGGC GGGGCGGACACCGCCCTCCGCACCGCCGACTCCGGCTACCTCACCCGCAAGCTCGTGGAC GTGACCCACGAGATCGTGGTGCGGGAGGCGGACTGCGGCACCACCAACTACATCTCCGTT CCCCTCTTCCAGCCCGACGAGGTGACCCGCTCCTTGCGCCTGAGGAAGCGCGCGGACATT GAGGCGGGCCTCTACGGGCGCGTCCTGGCCCGGGAGGTGGAGGTCCTGGGGGTGCGCCTC GAGGAGGGCCGCTACCTCTCCATGGACGACGTCCACCTCCTCATCAAGGCCGCCGAGGCC GGGGAGATCCAGGAGGTGCCCGTCCGCAGCCCCCTCACCTGCCAGACCCGCTACGGGGTC TGCCAGAAGTGCTACGGGTACGACCTCTCCATGGCCCGGCCCGTCTCCATCGGCGAGGCG GTGGGCATCGTGGCCGCCCAGTCCATCGGCGAGCCCGGCACCCAGCTCACCATGCGCACC TTCCACACGGGCGGCGTGGCCGGGGCCGCGGACATCACCCAGGGTCTGCCCCGCGTCATT GAGCTCTTTGAGGCCCGGCGCCCCAAGGCCAAGGCGGTGATCTCCGAGATTGACGGGGTG GTGCGCATTGAGGAGACGGAGGAGAAGCTCTCCGTCTTCGTGGAGTCCGAGGGCTTCTCC AAGGAGTACAAGCTCCCCAAGGAGGCGCGCCTTCTCGTCAAGGACGGGGACTACGTGGAG GCGGGCCAGCCCCTCACCCGCGGGGCCATTGACCCCCACCAGCTCTTGGAGGCCAAGGGC CCCGAGGCGGTGGAGCGCTACCTGGTGGAGGAGATCCAGAAGGTCTACCGGGCCCAGGGC GTGAAGCTGCACGACAAGCACATTGAGATCGTGGTCCGGCAGATGATGAAGTACGTGGAG GTCACCGACCCCGGGGACAGCCGCCTCCTCGAGGGCCAGGTCCTGGAGAAGTGGGACGTG GAGGCCCTGAACGAGAGGCTCATCGCCGAGGGCAAGACCCCGGTGGCCTGGAAGCCCCTC CTCATGGGGGTCACGAAGAGCGCCCTCTCCACCAAGAGCTGGCTCTCCGCCGCCAGCTTC CAGAACACCACCCACGTCCTCACCGAGGCGGCCATCGCCGGGAAGAAGGACGAGCTCATC GGCCTCAAGGAGAACGTCATCCTGGGCCGCCTGATCCCGGCGGGCACGGGTTCGGACTTC GTCCGCTTCACCCAGGTGGTGGACCAGAAGACCCTGAAGGCCATTGAGGAGGCCCGCAAG GAGGCGGTGGAGGCCAAGGAGCGGCCCGCCGCCCGGCGCGGGGTCAAGCGGGAGCAGCCC GGCAAGCAGGCTTAA PF04997 RNA_pol_Rpb1_1 PF00623 RNA_pol_Rpb1_2 PF04983 RNA_pol_Rpb1_3 PF05000 RNA_pol_Rpb1_4 PF04998 RNA_pol_Rpb1_5 component intracellular membrane-bound organelle component nucleus component organelle component membrane-bound organelle function transferase activity, transferring phosphorus-containing groups function nucleic acid binding function binding function DNA binding function catalytic activity function nucleotidyltransferase activity function DNA-directed RNA polymerase activity function transferase activity process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process physiological process process metabolism process cellular metabolism process transcription BE0003369 DNA-directed RNA polymerase subunit omega Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown DNA-directed RNA polymerase subunit omega Involved in DNA-directed RNA polymerase activity Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity) rpoZ Cytoplasmic None 4.96 11518.0 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) GenBank Gene Database AB083791 UniProtKB Q8RQE7 UniProt Accession RPOZ_THET8 EC 2.7.7.6 RNA polymerase omega subunit RNAP omega subunit Transcriptase omega chain >DNA-directed RNA polymerase omega chain MAEPGIDKLFGMVDSKYRLTVVVAKRAQQLLRHGFKNTVLEPEERPKMQTLEGLFDDPNA VTWAMKELLTGRLVFGENLVPEDRLQKEMERLYPVEREE >300 bp ATGGCGGAACCGGGCATTGACAAGCTCTTCGGCATGGTGGACTCCAAGTACCGGCTCACC GTGGTGGTGGCCAAAAGGGCGCAGCAGCTCCTCCGCCACGGCTTCAAGAACACGGTCTTG GAGCCGGAAGAGAGGCCCAAGATGCAGACCCTCGAGGGGCTTTTTGACGACCCCAACGCC GAGACCTGGGCCATGAAGGAGCTCCTCACGGGCCGGTTGGTCTTCGGGGAGAACCTGGTG CCCGAGGACCGGCTGCAAAAGGAGATGGAGCGGATCTACCCGGGGGAGCGAGAGGAGTAA PF01192 RNA_pol_Rpb6 function transferase activity function transferase activity, transferring phosphorus-containing groups function nucleic acid binding function DNA binding function nucleotidyltransferase activity function binding function DNA-directed RNA polymerase activity function catalytic activity process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process physiological process process transcription process transcription, DNA-dependent process metabolism process cellular metabolism BE0003370 RNA polymerase sigma factor Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown RNA polymerase sigma factor Involved in catalytic activity TTHA0532 Cytoplasmic None 4.77 48525.0 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) GenBank Gene Database AP008226 UniProtKB Q5SKW1 UniProt Accession Q5SKW1_THET8 RpoD >RNA polymerase pricipal sigma factor MKKSKRKNAQAQEAQETEVLVQEEAEELPEFPEGEPDPDLEDPDLTLEDDLLDLPEEGEG LDLEEEEEDLPIPKISTSDPVRQYLHEIGQVPLLTLEEEVELARKVEEGMEAIKKLSEIT GLDPDLIREVVRAKILGSARVRHIPGLKETLDPKTVEEIDQKLKSLPKEHKRYLHIAREG EAARQHLIEANLRLVVSIAKKYTGRGLSFLDLIQEGNQGLIRAVEKFEYKRRFKFSTYAT WWIRQAINRAIADQARTIRIPVHMVETINKLSRTARQLQQELGREPTYEEIAEAMGPGWD AKRVEETLKIAQEPVSLETPIGDEKDSFYGDFIPDEHLPSPVDAATQSLLSEELEKALSK LSEREAMVLKLRKGLIDGREHTLEEVGAFFGVTRERIRQIENKALRKLKYHESRTRKLRD FLD >1272 bp TTAGTCCAGGAAGTCCCTGAGCTTCCGCGTGCGGGACTCGTGGTACTTGAGCTTGCGGAG GGCCTTGTTCTCAATCTGCCGGATCCTTTCCCGGGTGACGCCGAAGAAGGCCCCCACCTC CTCCAGGGTGTGCTCCCGCCCGTCAATGAGCCCTTTCCGGAGCTTCAGGACCATGGCCTC GCGCTCGGAGAGCTTGGACAGGGCCTTCTCCAGCTCCTCGGAGAGGAGGCTCTGGGTGGC GGCGTCCACCGGGGAGGGGAGGTGCTCGTCGGGGATGAAGTCCCCGTAGAAGCTGTCCTT CTCGTCGCCGATGGGGGTCTCCAGGGAGACGGGCTCCTGGGCGATCTTGAGGGTTTCCTC CACCCGCTTGGCGTCCCAGCCCGGCCCCATGGCCTCGGCGATCTCCTCGTAGGTGGGTTC CCGGCCGAGCTCCTGCTGCAGCTGCCTTGCGGTGCGGGAGAGCTTGTTGATGGTCTCCAC CATGTGGACCGGGATGCGGATGGTGCGGGCCTGGTCGGCGATGGCCCGGTTGATGGCCTG CCGGATCCACCAGGTGGCGTAGGTGGAGAACTTGAAGCGCCGCTTGTACTCAAACTTCTC CACCGCCCGGATCAGGCCCTGGTTTCCCTCCTGGATGAGGTCCAGGAAGGAGAGGCCCCG CCCCGTGTACTTCTTGGCGATGGAGACCACGAGCCGGAGGTTGGCCTCAATGAGGTGCTG CCGGGCCGCCTCCCCTTCCCGGGCGATGTGGAGGTAGCGCTTGTGCTCCTTGGGGAGGCT TTTGAGCTTCTGGTCAATCTCCTCCACGGTCTTGGGGTCCAGGGTCTCCTTGAGGCCGGG GATGTGCCGCACCCGGGCCGAGCCCAGAATCTTGGCCCGGACCACCTCCCGGATGAGGTC GGGGTCAAGGCCGGTGATCTCGGAGAGCTTCTTGATGGCCTCCATCCCCTCCTCCACCTT CCGGGCGAGCTCCACCTCCTCCTCCAGGGTGAGGAGGGGGACCTGGCCGATCTCGTGCAG GTACTGGCGCACGGGGTCGGAGGTGGAGATCTTGGGGATGGGGAGGTCTTCTTCCTCCTC CTCCAGGTCCAGCCCCTCGCCCTCCTCGGGCAGGTCCAGGAGGTCGTCCTCCAGGGTGAG GTCCGGGTCCTCGAGGTCGGGGTCGGGCTCCCCCTCGGGGAACTCGGGGAGTTCCTCCGC CTCCTCCTGGACCAGGACCTCGGTCTCCTGGGCCTCCTGGGCCTGGGCGTTCTTGCGCTT GCTCTTCTTCAA PF00140 Sigma70_r1_2 PF04542 Sigma70_r2 PF04539 Sigma70_r3 PF04545 Sigma70_r4 function adenyl nucleotide binding function ATP binding function nucleic acid binding function transcription factor activity function transcription regulator activity function binding function DNA binding function transcription initiation factor activity function sigma factor activity function nucleotide binding function purine nucleotide binding process regulation of transcription process regulation of transcription, DNA-dependent process transcription process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process transcription, DNA-dependent process physiological process process regulation of biological process process metabolism process regulation of physiological process process transcription initiation process cellular metabolism process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism "
drug:methyl [(1E,5R)-5-{(3S)-3-[(2E,4E)-2,5-dimethylocta-2,4-dienoyl]-2,4-dioxo-3,4-dihydro-2H-pyran-6-yl}hexylidene]carbamaterdfs:label"methyl [(1E,5R)-5-{(3S)-3-[(2E,4E)-2,5-dimethylocta-2,4-dienoyl]-2,4-dioxo-3,4-dihydro-2H-pyran-6-yl}hexylidene]carbamate"
drug:methyl [(1E,5R)-5-{(3S)-3-[(2E,4E)-2,5-dimethylocta-2,4-dienoyl]-2,4-dioxo-3,4-dihydro-2H-pyran-6-yl}hexylidene]carbamaterdf:typedrugbank:drugs
drug:molecular iodinedrugbank:description"Molecualar iodine has been developed by Symbollon Pharmaceuticals. It is a potential treatment for moderate to severe cyclic pain and tenderness (clinical mastalgia) associated with fibrocystic breast disease (FBD). "
drug:molecular iodinedrugbank:drugCategorydrugcategory:Trace Elements
drug:molecular iodinerdfs:label"molecular iodine"
drug:molecular iodinerdf:typedrugbank:drugs
drug:motexafin gadoliniumdrugbank:description"Motexafin gadolinium is studied in the treatment of cancer by Pharmacyclics. It may make tumor cells more sensitive to radiation therapy, improve tumor images using magnetic resonance imaging (MRI), and kill cancer cells. It belongs to the family of drugs called metalloporphyrin complexes. Also called gadolinium texaphyrin."
drug:motexafin gadoliniumrdfs:label"motexafin gadolinium"
drug:motexafin gadoliniumrdf:typedrugbank:drugs
drug:motexafin lutetiumdrugbank:description"Motexafin lutetium (MLu) is a second-generation photosensitizer for photodynamic therapy (PDT) of cancer. It belongs to the family of drugs called metallotexaphyrins. Also called lutetium texaphyrin. Motexafin lutetium is a pentadentate aromatic metallotexaphyrin with photosensitizing properties. "
drug:motexafin lutetiumrdfs:label"motexafin lutetium"
drug:motexafin lutetiumrdf:typedrugbank:drugs
drug:naltrexone depotdrugbank:description"Naltrexone depot produced statistically significant blockade of opiate effects for six weeks as measured by subjective rating scales and measurement of pupil size."
drug:naltrexone depotrdfs:label"naltrexone depot"
drug:naltrexone depotrdf:typedrugbank:drugs
drug:naphthalene-1,2,4,5,7-pentoldrugbank:description" experimental This compound belongs to the naphthols and derivatives. These are hydroxylated naphthalenes. Naphthols and Derivatives Organic Compounds Benzenoids Acenes and Derivatives Naphthalenes Hydroxyquinols and Derivatives Catechols Hydroquinones Polyols Enols Polyamines hydroxyquinol derivative hydroquinone 1,2-diphenol phenol derivative benzene polyol enol polyamine logP 0.66 ALOGPS logS -2.1 ALOGPS Water Solubility 1.65e+00 g/l ALOGPS logP 1.44 ChemAxon IUPAC Name naphthalene-1,2,4,5,7-pentol ChemAxon Traditional IUPAC Name naphthalene-1,2,4,5,7-pentol ChemAxon Molecular Weight 208.1675 ChemAxon Monoisotopic Weight 208.037173366 ChemAxon SMILES OC1=CC(O)=C2C(O)=CC(O)=C(O)C2=C1 ChemAxon Molecular Formula C10H8O5 ChemAxon InChI InChI=1S/C10H8O5/c11-4-1-5-9(6(12)2-4)7(13)3-8(14)10(5)15/h1-3,11-15H ChemAxon InChIKey InChIKey=IISYZEMBGRNYTH-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 101.15 ChemAxon Refractivity 52.41 ChemAxon Polarizability 19.17 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 8.48 ChemAxon pKa (strongest basic) -5.7 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 448669 PubChem Substance 99443386 ChemSpider 395397 PDB 226 "
drug:naphthalene-1,2,4,5,7-pentolrdfs:label"naphthalene-1,2,4,5,7-pentol"
drug:naphthalene-1,2,4,5,7-pentolrdf:typedrugbank:drugs
drug:nocodazoledrugbank:description" experimental This compound belongs to the benzimidazoles. These are organic compounds containing a benzene ring fused to an imidazole ring (five member ring containing a nitrogen atom, 4 carbon atoms, and two double bonds). Benzimidazoles Organic Compounds Heterocyclic Compounds Benzimidazoles Acetophenones Thiophene Carboxylic Acids and Derivatives Benzoyl Derivatives Aminoimidazoles Ketones Carbamic Acids and Derivatives Polyamines Ethers Enolates thiophene carboxylic acid or derivative benzoyl aminoimidazole benzene azole thiophene imidazole carbamic acid derivative ketone polyamine ether enolate amine carbonyl group organonitrogen compound logP 2.84 ALOGPS logS -4.2 ALOGPS Water Solubility 1.85e-02 g/l ALOGPS logP 3.17 ChemAxon IUPAC Name methyl N-{6-[(thiophen-2-yl)carbonyl]-1H-1,3-benzodiazol-2-yl}carbamate ChemAxon Traditional IUPAC Name nocodazole ChemAxon Molecular Weight 301.32 ChemAxon Monoisotopic Weight 301.052111923 ChemAxon SMILES COC(=O)NC1=NC2=CC=C(C=C2N1)C(=O)C1=CC=CS1 ChemAxon Molecular Formula C14H11N3O3S ChemAxon InChI InChI=1S/C14H11N3O3S/c1-20-14(19)17-13-15-9-5-4-8(7-10(9)16-13)12(18)11-3-2-6-21-11/h2-7H,1H3,(H2,15,16,17,19) ChemAxon InChIKey InChIKey=KYRVNWMVYQXFEU-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 84.08 ChemAxon Refractivity 78.39 ChemAxon Polarizability 30.93 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 8.34 ChemAxon pKa (strongest basic) 3.9 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon ChEBI 34892 PubChem Compound 4122 PubChem Substance 99444784 ChemSpider 3979 PDB NZO BE0001167 Hematopoietic prostaglandin D synthase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Hematopoietic prostaglandin D synthase Involved in prostaglandin-D synthase activity Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation HPGDS Cytoplasm None 5.64 23344.0 Human GenBank Gene Database D82073 GenBank Protein Database 3046817 UniProtKB O60760 UniProt Accession HPGDS_HUMAN EC 5.3.99.2 Glutathione-dependent PGD synthetase H-PGDS Hematopoietic prostaglandin D synthase Prostaglandin-H2 D-isomerase >Glutathione-requiring prostaglandin D synthase MPNYKLTYFNMRGRAEIIRYIFAYLDIQYEDHRIEQADWPEIKSTLPFGKIPILEVDGLT LHQSLAIARYLTKNTDLAGNTEMEQCHVDAIVDTLDDFMSCFPWAEKKQDVKEQMFNELL TYNAPHLMQDLDTYLGGREWLIGNSVTWADFYWEICSTTLLVFKPDLLDNHPRLVTLRKK VQAIPAVANWIKRRPQTKL >600 bp ATGCCAAACTACAAACTCACTTATTTTAATATGAGGGGGAGAGCAGAAATTATTCGTTAC ATATTTGCTTATTTGGACATACAGTATGAAGACCACAGAATAGAACAAGCTGACTGGCCT GAAATCAAATCAACTCTCCCATTTGGAAAAATCCCCATTTTGGAAGTTGATGGACTTACT CTTCACCAGAGCCTAGCAATAGCAAGATATTTGACCAAAAACACAGATTTGGCTGGAAAC ACAGAAATGGAACAATGTCATGTTGATGCTATTGTGGACACTCTGGATGATTTCATGTCA TGTTTTCCTTGGGCAGAGAAAAAGCAAGATGTGAAAGAGCAGATGTTCAATGAGCTGCTC ACGTATAATGCGCCTCATCTTATGCAAGACTTGGACACATATTTAGGGGGGAGAGAATGG CTTATTGGTAACTCTGTAACTTGGGCAGACTTCTACTGGGAGATTTGCAGTACCACACTT TTGGTCTTTAAGCCTGACCTGTTAGACAACCATCCAAGGCTGGTGACTTTACGGAAGAAA GTCCAAGCCATTCCTGCCGTCGCTAACTGGATAAAACGAAGGCCCCAAACCAAACTCTAG PF00043 GST_C PF02798 GST_N "
drug:nocodazolerdfs:label"nocodazole"
drug:nocodazolerdf:typedrugbank:drugs
drug:octyl 3-amino-3-deoxy-2-O-(2,6-dideoxy-alpha-L-lyxo-hexopyranosyl)-beta-D-galactopyranosidedrugbank:description" experimental This compound belongs to the alkyl glycosides. These are lipids containing a glycosyl moiety (one or several units) linked to the hydroxyl group of a fatty alcohol. Alkyl Glycosides Organic Compounds Lipids Alkyl Glycosides Dihexoses O-glycosyl Compounds Amino Sugars Oxanes 1,2-Diols Secondary Alcohols 1,2-Aminoalcohols Polyamines Primary Alcohols Acetals Monoalkylamines amino sugar oxane saccharide 1,2-aminoalcohol 1,2-diol secondary alcohol primary alcohol ether polyamine acetal amine primary aliphatic amine alcohol primary amine organonitrogen compound logP 0.26 ALOGPS logS -2 ALOGPS Water Solubility 4.43e+00 g/l ALOGPS logP 0.88 ChemAxon IUPAC Name (2S,3S,4S,6S)-6-{[(2R,3R,4S,5R,6R)-4-amino-5-hydroxy-6-(hydroxymethyl)-2-(octyloxy)oxan-3-yl]oxy}-2-methyloxane-3,4-diol ChemAxon Traditional IUPAC Name (2S,3S,4S,6S)-6-{[(2R,3R,4S,5R,6R)-4-amino-5-hydroxy-6-(hydroxymethyl)-2-(octyloxy)oxan-3-yl]oxy}-2-methyloxane-3,4-diol ChemAxon Molecular Weight 421.5256 ChemAxon Monoisotopic Weight 421.267567229 ChemAxon SMILES [H][C@]1(O)C[C@]([H])(O[C@]2([H])[C@@]([H])(N)[C@@]([H])(O)[C@@]([H])(CO)O[C@@]2([H])OCCCCCCCC)O[C@@]([H])(C)[C@@]1([H])O ChemAxon Molecular Formula C20H39NO8 ChemAxon InChI InChI=1S/C20H39NO8/c1-3-4-5-6-7-8-9-26-20-19(16(21)18(25)14(11-22)28-20)29-15-10-13(23)17(24)12(2)27-15/h12-20,22-25H,3-11,21H2,1-2H3/t12-,13-,14+,15-,16-,17+,18-,19+,20+/m0/s1 ChemAxon InChIKey InChIKey=GHTLMVRROQXELT-HTYYFBMYSA-N ChemAxon Polar Surface Area (PSA) 143.86 ChemAxon Refractivity 103.97 ChemAxon Polarizability 46.71 ChemAxon Rotatable Bond Count 11 ChemAxon H Bond Acceptor Count 9 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 12.96 ChemAxon pKa (strongest basic) 8.7 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937064 PubChem Substance 99443812 PDB AD7 BE0000214 Histo-blood group ABO system transferase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Histo-blood group ABO system transferase Involved in transferase activity, transferring hexosyl groups This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens:A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity ABO 9q34.1-q34.2 Golgi apparatus; Golgi stack; Golgi stack membrane; single-pass type II membrane protein. Membrane-b 33-53 9.24 40934.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:79 GenAtlas ABO GeneCards ABO GenBank Gene Database J05175 GenBank Protein Database 340078 UniProtKB P16442 UniProt Accession BGAT_HUMAN A transferase) EC 2.4.1.37 EC 2.4.1.40 Fucosylglycoprotein 3-alpha- galactosyltransferase Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha- galactosyltransferase Histo-blood group A transferase Histo-blood group B transferase NAGAT >Histo-blood group ABO system transferase MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDH LQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTV FAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKR WQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSS REAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVW HDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP >1062 bp ATGGCCGAGGTGTTGCGGACGCTGGCCGGAAAACCAAAATGCCACGCACTTCGACCTATG ATCCTTTTCCTAATAATGCTTGTCTTGGTCTTGTTTGGTTACGGGGTCCTAAGCCCCAGA AGTCTAATGCCAGGAAGCCTGGAACGGGGGTTCTGCATGGCTGTTAGGGAACCTGACCAT CTGCAGCGCGTCTCGTTGCCAAGGATGGTCTACCCCCAGCCAAAGGTGCTGACACCGTGG AAGGATGTCCTCGTGGTGACCCCTTGGCTGGCTCCCATTGTCTGGGAGGGCACATTCAAC ATCGACATCCTCAACGAGCAGTTCAGGCTCCAGAACACCACCATTGGGTTAACTGTGTTT GCCATCAAGAAATACGTGGCTTTCCTGAAGCTGTTCCTGGAGACGGCGGAGAAGCACTTC ATGGTGGGCCACCGTGTCCACTACTATGTCTTCACCGACCAGCTGGCCGCGGTGCCCCGC GTGACGCTGGGGACCGGTCGGCAGCTGTCAGTGCTGGAGGTGCGCGCCTACAAGCGCTGG CAGGACGTGTCCATGCGCCGCATGGAGATGATCAGTGACTTCTGCGAGCGGCGCTTCCTC AGCGAGGTGGATTACCTGGTGTGCGTGGACGTGGACATGGAGTTCCGCGACCACGTGGGC GTGGAGATCCTGACTCCGCTGTTCGGCACCCTGCACCCCGGCTTCTACGGAAGCAGCCGG GAGGCCTTCACCTACGAGCGCCGGCCCCAGTCCCAGGCCTACATCCCCAAGGACGAGGGC GATTTCTACTACCTGGGGGGGTTCTTCGGGGGGTCGGTGCAAGAGGTGCAGCGGCTCACC AGGGCCTGCCACCAGGCCATGATGGTCGACCAGGCCAACGGCATCGAGGCCGTGTGGCAC GACGAGAGCCACCTGAACAAGTACCTGCTGCGCCACAAACCCACCAAGGTGCTCTCCCCC GAGTACTTGTGGGACCAGCAGCTGCTGGGCTGGCCCGCCGTCCTGAGGAAGCTGAGGTTC ACTGCGGTGCCCAAGAACCACCAGGCGGTCCGGAACCCGTGA PF03414 Glyco_transf_6 component cell component membrane function transferase activity function transferase activity, transferring glycosyl groups function transferase activity, transferring hexosyl groups function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process "
drug:octyl 3-amino-3-deoxy-2-O-(2,6-dideoxy-alpha-L-lyxo-hexopyranosyl)-beta-D-galactopyranosiderdfs:label"octyl 3-amino-3-deoxy-2-O-(2,6-dideoxy-alpha-L-lyxo-hexopyranosyl)-beta-D-galactopyranoside"
drug:octyl 3-amino-3-deoxy-2-O-(2,6-dideoxy-alpha-L-lyxo-hexopyranosyl)-beta-D-galactopyranosiderdf:typedrugbank:drugs
drug:octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranosidedrugbank:description" experimental This compound belongs to the alkyl glycosides. These are lipids containing a glycosyl moiety (one or several units) linked to the hydroxyl group of a fatty alcohol. Alkyl Glycosides Organic Compounds Lipids Alkyl Glycosides Dihexoses O-glycosyl Compounds Oxanes Secondary Alcohols 1,2-Diols Primary Alcohols Acetals Polyamines oxane saccharide polyol secondary alcohol 1,2-diol primary alcohol polyamine acetal ether alcohol logP 0.75 ALOGPS logS -1.9 ALOGPS Water Solubility 5.72e+00 g/l ALOGPS logP 0.78 ChemAxon IUPAC Name (2S,3S,4R,5S,6S)-2-{[(2R,3R,5R,6R)-5-hydroxy-6-(hydroxymethyl)-2-(octyloxy)oxan-3-yl]oxy}-6-methyloxane-3,4,5-triol ChemAxon Traditional IUPAC Name (2S,3S,4R,5S,6S)-2-{[(2R,3R,5R,6R)-5-hydroxy-6-(hydroxymethyl)-2-(octyloxy)oxan-3-yl]oxy}-6-methyloxane-3,4,5-triol ChemAxon Molecular Weight 422.5103 ChemAxon Monoisotopic Weight 422.251582814 ChemAxon SMILES [H][C@@]1(O)C[C@@]([H])(O[C@]2([H])O[C@@]([H])(C)[C@@]([H])(O)[C@@]([H])(O)[C@]2([H])O)[C@]([H])(OCCCCCCCC)O[C@]1([H])CO ChemAxon Molecular Formula C20H38O9 ChemAxon InChI InChI=1S/C20H38O9/c1-3-4-5-6-7-8-9-26-19-14(10-13(22)15(11-21)29-19)28-20-18(25)17(24)16(23)12(2)27-20/h12-25H,3-11H2,1-2H3/t12-,13+,14+,15+,16+,17+,18-,19+,20-/m0/s1 ChemAxon InChIKey InChIKey=FBVFDKBCZLMLQT-PPCMOIRNSA-N ChemAxon Polar Surface Area (PSA) 138.07 ChemAxon Refractivity 102.72 ChemAxon Polarizability 46.19 ChemAxon Rotatable Bond Count 11 ChemAxon H Bond Acceptor Count 9 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 12.22 ChemAxon pKa (strongest basic) -3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937084 PubChem Substance 99444104 PDB DA8 BE0000214 Histo-blood group ABO system transferase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Histo-blood group ABO system transferase Involved in transferase activity, transferring hexosyl groups This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens:A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity ABO 9q34.1-q34.2 Golgi apparatus; Golgi stack; Golgi stack membrane; single-pass type II membrane protein. Membrane-b 33-53 9.24 40934.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:79 GenAtlas ABO GeneCards ABO GenBank Gene Database J05175 GenBank Protein Database 340078 UniProtKB P16442 UniProt Accession BGAT_HUMAN A transferase) EC 2.4.1.37 EC 2.4.1.40 Fucosylglycoprotein 3-alpha- galactosyltransferase Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha- galactosyltransferase Histo-blood group A transferase Histo-blood group B transferase NAGAT >Histo-blood group ABO system transferase MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDH LQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTV FAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKR WQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSS REAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVW HDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP >1062 bp ATGGCCGAGGTGTTGCGGACGCTGGCCGGAAAACCAAAATGCCACGCACTTCGACCTATG ATCCTTTTCCTAATAATGCTTGTCTTGGTCTTGTTTGGTTACGGGGTCCTAAGCCCCAGA AGTCTAATGCCAGGAAGCCTGGAACGGGGGTTCTGCATGGCTGTTAGGGAACCTGACCAT CTGCAGCGCGTCTCGTTGCCAAGGATGGTCTACCCCCAGCCAAAGGTGCTGACACCGTGG AAGGATGTCCTCGTGGTGACCCCTTGGCTGGCTCCCATTGTCTGGGAGGGCACATTCAAC ATCGACATCCTCAACGAGCAGTTCAGGCTCCAGAACACCACCATTGGGTTAACTGTGTTT GCCATCAAGAAATACGTGGCTTTCCTGAAGCTGTTCCTGGAGACGGCGGAGAAGCACTTC ATGGTGGGCCACCGTGTCCACTACTATGTCTTCACCGACCAGCTGGCCGCGGTGCCCCGC GTGACGCTGGGGACCGGTCGGCAGCTGTCAGTGCTGGAGGTGCGCGCCTACAAGCGCTGG CAGGACGTGTCCATGCGCCGCATGGAGATGATCAGTGACTTCTGCGAGCGGCGCTTCCTC AGCGAGGTGGATTACCTGGTGTGCGTGGACGTGGACATGGAGTTCCGCGACCACGTGGGC GTGGAGATCCTGACTCCGCTGTTCGGCACCCTGCACCCCGGCTTCTACGGAAGCAGCCGG GAGGCCTTCACCTACGAGCGCCGGCCCCAGTCCCAGGCCTACATCCCCAAGGACGAGGGC GATTTCTACTACCTGGGGGGGTTCTTCGGGGGGTCGGTGCAAGAGGTGCAGCGGCTCACC AGGGCCTGCCACCAGGCCATGATGGTCGACCAGGCCAACGGCATCGAGGCCGTGTGGCAC GACGAGAGCCACCTGAACAAGTACCTGCTGCGCCACAAACCCACCAAGGTGCTCTCCCCC GAGTACTTGTGGGACCAGCAGCTGCTGGGCTGGCCCGCCGTCCTGAGGAAGCTGAGGTTC ACTGCGGTGCCCAAGAACCACCAGGCGGTCCGGAACCCGTGA PF03414 Glyco_transf_6 component cell component membrane function transferase activity function transferase activity, transferring glycosyl groups function transferase activity, transferring hexosyl groups function catalytic activity process metabolism process macromolecule metabolism process carbohydrate metabolism process physiological process "
drug:octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranosiderdfs:label"octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranoside"
drug:octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranosiderdf:typedrugbank:drugs
drug:octyl alpha-L-altropyranosidedrugbank:description" experimental This compound belongs to the alkyl glycosides. These are lipids containing a glycosyl moiety (one or several units) linked to the hydroxyl group of a fatty alcohol. Alkyl Glycosides Organic Compounds Lipids Alkyl Glycosides O-glycosyl Compounds Hexoses Oxanes Secondary Alcohols 1,2-Diols Primary Alcohols Acetals Polyamines oxane saccharide monosaccharide polyol secondary alcohol 1,2-diol primary alcohol polyamine acetal ether alcohol logP 1.13 ALOGPS logS -1.3 ALOGPS Water Solubility 1.60e+01 g/l ALOGPS logP 0.81 ChemAxon IUPAC Name (2S,3R,4S,5R,6R)-2-(hydroxymethyl)-6-(octyloxy)oxane-3,4,5-triol ChemAxon Traditional IUPAC Name (2S,3R,4S,5R,6R)-2-(hydroxymethyl)-6-(octyloxy)oxane-3,4,5-triol ChemAxon Molecular Weight 292.3685 ChemAxon Monoisotopic Weight 292.188588628 ChemAxon SMILES [H][C@]1(O)[C@@]([H])(O)[C@]([H])(CO)O[C@@]([H])(OCCCCCCCC)[C@]1([H])O ChemAxon Molecular Formula C14H28O6 ChemAxon InChI InChI=1S/C14H28O6/c1-2-3-4-5-6-7-8-19-14-13(18)12(17)11(16)10(9-15)20-14/h10-18H,2-9H2,1H3/t10-,11-,12-,13+,14+/m0/s1 ChemAxon InChIKey InChIKey=HEGSGKPQLMEBJL-QSLWVIQJSA-N ChemAxon Polar Surface Area (PSA) 99.38 ChemAxon Refractivity 72.95 ChemAxon Polarizability 32.57 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 12.21 ChemAxon pKa (strongest basic) -3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 46937109 PubChem Substance 99444394 PDB HSG BE0003818 Aquaporin Z Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aquaporin Z Carbohydrate transport and metabolism Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity aqpZ Cell inner membrane 9-29 34-54 82-102 131-151 156-176 202-222 7.63 23702.6 Escherichia coli (strain K12) GeneCards aqpZ GenBank Gene Database U38664 GenBank Protein Database 1051283 UniProtKB P60844 UniProt Accession AQPZ_ECOLI Bacterial nodulin-like intrinsic protein >Aquaporin Z MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGG HFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNG YGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPV TNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRD PF00230 MIP component cell component intrinsic to membrane component integral to membrane component membrane function transporter activity process physiological process process cellular physiological process process transport "
drug:octyl alpha-L-altropyranosiderdfs:label"octyl alpha-L-altropyranoside"
drug:octyl alpha-L-altropyranosiderdf:typedrugbank:drugs
drug:octyl beta-D-galactopyranosidedrugbank:description" experimental This compound belongs to the alkyl glycosides. These are lipids containing a glycosyl moiety (one or several units) linked to the hydroxyl group of a fatty alcohol. Alkyl Glycosides Organic Compounds Lipids Alkyl Glycosides O-glycosyl Compounds Hexoses Oxanes Secondary Alcohols 1,2-Diols Primary Alcohols Acetals Polyamines oxane saccharide monosaccharide polyol secondary alcohol 1,2-diol primary alcohol polyamine acetal ether alcohol logP 1.13 ALOGPS logS -1.3 ALOGPS Water Solubility 1.60e+01 g/l ALOGPS logP 0.81 ChemAxon IUPAC Name (2R,3R,4S,5R,6R)-2-(hydroxymethyl)-6-(octyloxy)oxane-3,4,5-triol ChemAxon Traditional IUPAC Name (2R,3R,4S,5R,6R)-2-(hydroxymethyl)-6-(octyloxy)oxane-3,4,5-triol ChemAxon Molecular Weight 292.3685 ChemAxon Monoisotopic Weight 292.188588628 ChemAxon SMILES [H][C@]1(O)[C@@]([H])(O)[C@@]([H])(CO)O[C@@]([H])(OCCCCCCCC)[C@]1([H])O ChemAxon Molecular Formula C14H28O6 ChemAxon InChI InChI=1S/C14H28O6/c1-2-3-4-5-6-7-8-19-14-13(18)12(17)11(16)10(9-15)20-14/h10-18H,2-9H2,1H3/t10-,11+,12+,13-,14-/m1/s1 ChemAxon InChIKey InChIKey=HEGSGKPQLMEBJL-MBJXGIAVSA-N ChemAxon Polar Surface Area (PSA) 99.38 ChemAxon Refractivity 72.95 ChemAxon Polarizability 32.27 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 12.21 ChemAxon pKa (strongest basic) -3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 9549264 PubChem Substance 99444395 ChemSpider 7828180 PDB HSH BE0003818 Aquaporin Z Escherichia coli (strain K12) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aquaporin Z Carbohydrate transport and metabolism Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity aqpZ Cell inner membrane 9-29 34-54 82-102 131-151 156-176 202-222 7.63 23702.6 Escherichia coli (strain K12) GeneCards aqpZ GenBank Gene Database U38664 GenBank Protein Database 1051283 UniProtKB P60844 UniProt Accession AQPZ_ECOLI Bacterial nodulin-like intrinsic protein >Aquaporin Z MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGG HFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNG YGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPV TNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRD PF00230 MIP component cell component intrinsic to membrane component integral to membrane component membrane function transporter activity process physiological process process cellular physiological process process transport "
drug:octyl beta-D-galactopyranosiderdfs:label"octyl beta-D-galactopyranoside"
drug:octyl beta-D-galactopyranosiderdf:typedrugbank:drugs
drug:oglufanide disodiumdrugbank:description"Oglufanide disodium is a synthetic dipeptide immunomodulator in development for the treatment of chronic hepatitis C viral infection. Oglufanide disodium was originally developed to treat severe infectious disease in Russia (where it is a registered pharmaceutical), and was extensively studied in cancer clinical trials in the United States before being acquired by Implicit Bioscience in 2005. Oglufanide disodium works as a regulator of the body's immune response, is being given by intranasal administration to patients with chronic hepatitis C viral infection."
drug:oglufanide disodiumrdfs:label"oglufanide disodium"
drug:oglufanide disodiumrdf:typedrugbank:drugs
drug:omega interferondrugbank:description"Human interferon omega 1 (IFN-omega 1 = IFN-alpha II1) is a recently discovered protein structurally related to IFN-alpha and -beta. It occurs naturally in the human body and is currently being manufactured by Intarcia through genetic engineering. There are multiple routes for administration of omega interferon: injection, an implantable subcutaneous drug delivery system, and an oral formulation. It has been investigated both in single and combination treatment. The biological activities of IFN-omega 1 and its physiological role are not known to date. "
drug:omega interferonrdfs:label"omega interferon"
drug:omega interferonrdf:typedrugbank:drugs
drug:oportuzumab monatoxdrugbank:description"VB4-845 is studied in the treatment of certain types of head and neck cancer. VB4-845 is made by linking a monoclonal antibody fragment to a toxic protein that may kill cancer cells. VB4-845 is a fusion protein containing humanized scFv specific for the epithelial cell adhesion molecule, Ep-CAM, a tumor cell-associated target highly expressed on carcinoma cells of epithelial origin and a truncated portion of Pseudomonas exotoxin A."
drug:oportuzumab monatoxrdfs:label"oportuzumab monatox"
drug:oportuzumab monatoxrdf:typedrugbank:drugs
drug:parecoxibdrugbank:description" experimental This compound belongs to the stilbenes. These are organic compounds containing a 1,2-diphenylethylene moiety. Stilbenes (C6-C2-C6 ) are derived from the common phenylpropene (C6-C3) skeleton building block. The introduction of one or more hydroxyl groups to a phenyl ring lead to stilbenoids. Stilbenes Organic Compounds Phenylpropanoids and Polyketides Stilbenes Benzenesulfonamides Isoxazoles Sulfonyls Sulfonamides Enolates Carboxylic Acid Amides Polyamines benzenesulfonamide benzene sulfonyl azole isoxazole sulfonamide sulfonic acid derivative carboxamide group polyamine carboxylic acid derivative enolate amine organonitrogen compound MUSCULO-SKELETAL SYSTEM ANTIINFLAMMATORY AND ANTIRHEUMATIC PRODUCTS ANTIINFLAMMATORY AND ANTIRHEUMATIC PRODUCTS, NON-STEROIDS Coxibs logP 3.42 ALOGPS logS -4.4 ALOGPS Water Solubility 1.62e-02 g/l ALOGPS logP 3.51 ChemAxon IUPAC Name N-{[4-(5-methyl-3-phenyl-1,2-oxazol-4-yl)benzene]sulfonyl}propanamide ChemAxon Traditional IUPAC Name N-[4-(5-methyl-3-phenyl-1,2-oxazol-4-yl)benzenesulfonyl]propanamide ChemAxon Molecular Weight 370.422 ChemAxon Monoisotopic Weight 370.098727764 ChemAxon SMILES CCC(=O)NS(=O)(=O)C1=CC=C(C=C1)C1=C(C)ON=C1C1=CC=CC=C1 ChemAxon Molecular Formula C19H18N2O4S ChemAxon InChI InChI=1S/C19H18N2O4S/c1-3-17(22)21-26(23,24)16-11-9-14(10-12-16)18-13(2)25-20-19(18)15-7-5-4-6-8-15/h4-12H,3H2,1-2H3,(H,21,22) ChemAxon InChIKey InChIKey=TZRHLKRLEZJVIJ-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 89.27 ChemAxon Refractivity 98.9 ChemAxon Polarizability 38 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 4.24 ChemAxon pKa (strongest basic) 0.42 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 119828 PubChem Substance 99444910 ChemSpider 106990 PDB PXB BE0000994 Lactotransferrin Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Lactotransferrin Involved in ferric iron binding The lactotransferrin peptidase S60 domain 1 functions as a serine protease that cuts arginine rich regions. This function contributes to the antimicrobial activity LTF 3q21-q23 Secreted protein None 8.17 78182.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6720 GenAtlas LTF GeneCards LTF GenBank Gene Database X53961 GenBank Protein Database 34416 UniProtKB P02788 UniProt Accession TRFL_HUMAN EC 3.4.21.- Lactoferrin Lactotransferrin precursor Talalactoferrin alfa >Lactotransferrin precursor MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDS PIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKG GSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGA DKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDE AERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKD KSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAAR RARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYT AGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHT AVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNS NERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRK PVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNL LFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK >2136 bp ATGAAACTTGTCTTCCTCGTCCTGCTGTTCCTCGGGGCCCTCGGACTGTGTCTGGCTGGC CGTAGGAGAAGGAGTGTTCAGTGGTGCGCCGTATCCCAACCCGAGGCCACAAAATGCTTC CAATGGCAAAGGAATATGAGAAAAGTGCGTGGCCCTCCTGTCAGCTGCATAAAGAGAGAC TCCCCCATCCAGTGTATCCAGGCCATTGCGGAAAACAGGGCCGATGCTGTGACCCTTGAT GGTGGTTTCATATACGAGGCAGGCCTGGCCCCCTACAAACTGCGACCTGTAGCGGCGGAA GTCTACGGGACCGAAAGACAGCCACGAACTCACTATTATGCCGTGGCTGTGGTGAAGAAG GGCGGCAGCTTTCAGCTGAACGAACTGCAAGGTCTGAAGTCCTGCCACACAGGCCTTCGC AGGACCGCTGGATGGAATGTCCCTACAGGGACACTTCGTCCATTCTTGAATTGGACGGGT CCACCTGAGCCCATTGAGGCAGCTGTGGCCAGGTTCTTCTCAGCCAGCTGTGTTCCCGGT GCAGATAAAGGACAGTTCCCCAACCTGTGTCGCCTGTGTGCGGGGACAGGGGAAAACAAA TGTGCCTTCTCCTCCCAGGAACCGTACTTCAGCTACTCTGGTGCCTTCAAGTGTCTGAGA GACGGGGCTGGAGACGTGGCTTTTATCAGAGAGAGCACAGTGTTTGAGGACCTGTCAGAC GAGGCTGAAAGGGACGAGTATGAGTTACTCTGCCCAGACAACACTCGGAAGCCAGTGGAC AAGTTCAAAGACTGCCATCTGGCCCGGGTCCCTTCTCATGCCGTTGTGGCACGAAGTGTG AATGGCAAGGAGGATGCCATCTGGAATCTTCTCCGCCAGGCACAGGAAAAGTTTGGAAAG GACAAGTCACCGAAATTCCAGCTCTTTGGCTCCCCTAGTGGGCAGAAAGATCTGCTGTTC AAGGACTCTGCCATTGGGTTTTCGAGGGTGCCCCCGAGGATAGATTCTGGGCTGTACCTT GGCTCCGGCTACTTCACTGCCATCCAGAACTTGAGGAAAAGTGAGGAGGAAGTGGCTGCC CGGCGTGCGCGGGTCGTGTGGTGTGCGGTGGGCGAGCAGGAGCTGCGCAAGTGTAACCAG TGGAGTGGCTTGAGCGAAGGCAGCGTGACCTGCTCCTCGGCCTCCACCACAGAGGACTGC ATCGCCCTGGTGCTGAAAGGAGAAGCTGATGCCATGAGTTTGGATGGAGGATATGTGTAC ACTGCATGCAAATGTGGTTTGGTGCCTGTCCTGGCAGAGAACTACAAATCCCAACAAAGC AGTGACCCTGATCCTAACTGTGTGGATAGACCTGTGGAAGGATATCTTGCTGTGGCGGTG GTTAGGAGATCAGACACTAGCCTTACCTGGAACTCTGTGAAAGGCAAGAAGTCCTGCCAC ACCGCCGTGGACAGGACTGCAGGCTGGAATATCCCCATGGGCCTGCTCTTCAACCAGACG GGCTCCTGCAAATTTGATGAATATTTCAGTCAAAGCTGTGCCCCTGGGTCTGACCCGAGA TCTAATCTCTGTGCTCTGTGTATTGGCGACGAGCAGGGTGAGAATAAGTGCGTGCCCAAC AGCAACGAGAGATACTACGGCTACACTGGGGCTTTCCGGTGCCTGGCTGAGAATGCTGGA GACGTTGCATTTGTGAAAGATGTCACTGTCTTGCAGAACACTGATGGAAATAACAATGAG GCATGGGCTAAGGATTTGAAGCTGGCAGACTTTGCGCTGCTGTGCCTCGATGGCAAACGG AAGCCTGTGACTGAGGCTAGAAGCTGCCATCTTGCCATGGCCCCGAATCATGCCGTGGTG TCTCGGATGGATAAGGTGGAACGCCTGAAACAGGTGCTGCTCCACCAACAGGCTAAATTT GGGAGAAATGGATCTGACTGCCCGGACAAGTTTTGCTTATTCCAGTCTGAAACCAAAAAC CTTCTGTTCAATGACAACACTGAGTGTCTGGCCAGACTCCATGGCAAAACAACATATGAA AAATATTTGGGACCACAGTATGTCGCAGGCATTACTAATCTGAAAAAGTGCTCAACCTCC CCCCTCCTGGAAGCCTGTGAATTCCTCAGGAAGTAA PF00405 Transferrin component extracellular region function ion binding function cation binding function transition metal ion binding function iron ion binding function binding function ferric iron binding process cellular physiological process process homeostasis process cell homeostasis process cell ion homeostasis process cation homeostasis process di-, tri-valent inorganic cation homeostasis process transport process iron ion homeostasis process ion transport process transition metal ion transport process cation transport process iron ion transport process di-, tri-valent inorganic cation transport process physiological process "
drug:parecoxibrdfs:label"parecoxib"
drug:parecoxibrdf:typedrugbank:drugs
drug:personalized immunotherapydrugbank:description"Personalized Immunotherapy is an investigational treatment based on the unique genetic makeup of a patient's tumor and is designed to activate a patient's immune system to identify and attack cancer cells. Personalized Immunotherapy is commonly referred to as a patient-specific or personalized immunotherapy, an active idiotype immunotherapy, or a patient-specific or personalized cancer vaccine. "
drug:personalized immunotherapyrdfs:label"personalized immunotherapy"
drug:personalized immunotherapyrdf:typedrugbank:drugs
drug:phenyl ethenesulfonatedrugbank:description" experimental This compound belongs to the benzene and substituted derivatives. These are aromatic compounds containing at least one benzene ring. Benzene and Substituted Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Sulfonyls Organic Sulfites Sulfonic Acids and Derivatives Polyamines sulfonyl organic sulfite sulfonic acid derivative polyamine logP 1.6 ALOGPS logS -2.4 ALOGPS Water Solubility 6.91e-01 g/l ALOGPS logP 1.81 ChemAxon IUPAC Name phenyl ethene-1-sulfonate ChemAxon Traditional IUPAC Name phenyl ethenesulfonate ChemAxon Molecular Weight 184.212 ChemAxon Monoisotopic Weight 184.019414812 ChemAxon SMILES C=CS(=O)(=O)OC1=CC=CC=C1 ChemAxon Molecular Formula C8H8O3S ChemAxon InChI InChI=1S/C8H8O3S/c1-2-12(9,10)11-8-6-4-3-5-7-8/h2-7H,1H2 ChemAxon InChIKey InChIKey=CILDJVVXNMDAGY-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 43.37 ChemAxon Refractivity 44.95 ChemAxon Polarizability 17.26 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 2 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest basic) -9.7 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 564920 PubChem Substance 99444904 ChemSpider 491061 PDB PSY BE0001352 Tyrosine-protein phosphatase YopH Yersinia enterocolitica # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Tyrosine-protein phosphatase YopH Involved in protein tyrosine phosphatase activity Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of yopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages yopH Secreted protein. Note=Secreted via type III secretion system None 8.84 50940.0 Yersinia enterocolitica UniProtKB P15273 UniProt Accession YOPH_YEREN EC 3.1.3.48 Virulence protein >Tyrosine-protein phosphatase yopH MNLSLSDLHRQVSRLVQQESGDCTGKLRGNVAANKETTFQGLTIASGARESEKVFAQTVL SHVANIVLTQEDTAKLLQSTVKHNLNNYELRSVGNGNSVLVSLRSDQMTLQDAKVLLEAA LRQESGARGHVSSHSHSVLHAPGTPVREGLRSHLDPRTPPLPPRERPHTSGHHGAGEARA TAPSTVSPYGPEARAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNRFRDIQCCRQTAV RADLNANYIQVGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPD YFRQSGTYGSITVESKMTQQVGLGDGIMADMYTLTIREAGQKTISVPVVHVGNWPDQTAV SSEVTKALASLVDQTAETKRNMYESKGSSAVADDSKLRPVIHCRAGVGRTAQLIGAMCMN DSRNSQLSVEDMVSQMRVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS >1407 bp ATGAACTTATCATTAAGCGATCTTCATCGTCAGGTATCTCGATTGGTGCAGCAAGAGAGC GGTGATTGTACCGGGAAATTAAGAGGTAACGTTGCTGCCAATAAAGAAACTACCTTTCAA GGTTTGACCATAGCCAGTGGTGCCAGAGAGTCAGAAAAAGTATTTGCTCAAACTGTACTA AGCCACGTAGCAAATATTGTTCTAACTCAAGAAGATACCGCTAAGCTATTGCAAAGCACG GTAAAGCATAATTTGAATAATTATGAATTAAGAAGTGTCGGCAATGGTAATAGTGTACTT GTCAGTTTACGTAGTGACCAAATGACACTACAAGACGCCAAAGTGCTGTTGGAGGCTGCA TTGCGACAAGAGTCGGGAGCGAGGGGGCATGTATCATCTCATTCACATTCAGTCCTTCAC GCACCGGGAACCCCGGTGCGTGAAGGACTGCGTTCACATCTAGACCCCAGAACACCACCG TTGCCACCGCGTGAACGACCACACACTTCTGGCCATCACGGGGCTGGCGAAGCCAGAGCC ACCGCACCAAGCACTGTTTCTCCTTATGGCCCAGAAGCGCGCGCAGAACTCAGCAGCCGC CTCACCACATTGCGCAATACGCTGGCGCCAGCAACGAATGATCCGCGTTACTTACAAGCC TGCGGCGGTGAAAAGCTAAACCGATTTAGAGATATTCAATGCTGTCGGCAAACCGCAGTA CGCGCCGATCTTAATGCCAATTACATCCAGGTCGGTAACACTCGTACCATAGCGTGCCAG TATCCGCTACAATCTCAACTTGAAAGCCATTTCCGTATGCTGGCAGAAAACCGAACGCCA GTGTTGGCTGTTTTAGCGTCCAGTTCTGAGATAGCCAATCAAAGATTCGGTATGCCAGAT TATTTCCGCCAGAGTGGTACCTATGGCAGTATCACTGTAGAGTCTAAAATGACTCAGCAA GTTGGTCTCGGTGACGGGATTATGGCAGATATGTATACTTTAACGATTCGTGAAGCGGGT CAAAAAACAATTTCTGTTCCTGTGGTTCATGTTGGCAATTGGCCCGATCAGACCGCAGTC AGCTCTGAAGTTACCAAGGCACTCGCTTCACTGGTAGATCAAACAGCAGAAACAAAACGC AATATGTATGAAAGCAAAGGAAGTTCAGCGGTAGCAGATGACTCCAAATTACGGCCGGTA ATACATTGCCGTGCGGGTGTTGGCCGTACTGCGCAACTGATTGGCGCAATGTGCATGAAT GATAGTCGTAATAGTCAGTTAAGCGTAGAAGATATGGTCAGCCAAATGCGAGTACAAAGA AATGGTATTATGGTACAAAAAGATGAGCAACTTGATGTTCTGATTAAGTTGGCTGAAGGA CAAGGGCGACCATTATTAAATAGCTAA PF00102 Y_phosphatase PF09013 YopH_N function hydrolase activity function hydrolase activity, acting on ester bonds function phosphoric ester hydrolase activity function phosphoric monoester hydrolase activity function phosphoprotein phosphatase activity function catalytic activity function protein tyrosine phosphatase activity process metabolism process protein amino acid dephosphorylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification process physiological process "
drug:phenyl ethenesulfonaterdfs:label"phenyl ethenesulfonate"
drug:phenyl ethenesulfonaterdf:typedrugbank:drugs
drug:pimagedine HCldrugbank:description"It has been developed by Synvista Therapeutics, Inc for the treatment of diabetic kidney disease.Pimagedine HCl is an advanced glycation end products inhibitor which manages diabetic nephropathy, either alone or in combination with other therapies. It is beneficial in treating patients with diabetic nephropathy."
drug:pimagedine HClrdfs:label"pimagedine HCl"
drug:pimagedine HClrdf:typedrugbank:drugs
drug:polyacrylic aciddrugbank:description"Polyacrylic acid is developed by ReProtect. It is a gel that may help both block the spread of sexually transmitted diseases and reduce unwanted pregnancies. The compound, known as BufferGel, is currently in advanced clinical trials for its ability to prevent pregnancy. "
drug:polyacrylic aciddrugbank:drugCategorydrugcategory:Tissue Adhesives
drug:polyacrylic acidrdfs:label"polyacrylic acid"
drug:polyacrylic acidrdf:typedrugbank:drugs
drug:pradefovir mesylatedrugbank:description" Pradefovir mesilate (previously known as MB-06886, Hepavir B and remofovir mesylate) is an orally administered small molecule compound that belongs to a novel series of phosphate and phosphonate prodrugs of adefovir. Adefovir (Hepsera) is an acyclic phosphonate analogue of adenine that is used to treat hepatitis B virus. As adefovir is poorly absorbed and associated with a high level of nephrotoxicity, pradefovir mesilate was designed to specifically target the liver and reduce risks to external tissue, especially the kidneys, while improving results of adefovir. Pradefovir is activated through oxidation that is mediated by cytochrome P-450 (CYP) 3A4, which is predominantly expressed in the liver. The novel prodrug is highly stable in both plasma and tissues and demonstrated potent preclinical and clinical anti-HBV activity. Pradefovir is undergoing phase II development for the treatment of chronic hepatitis B. "
drug:pradefovir mesylaterdfs:label"pradefovir mesylate"
drug:pradefovir mesylaterdf:typedrugbank:drugs
drug:rGLP-1drugbank:description"rGLP-1 is a continuous infusion of glucagon-like peptide 1, or GLP-1, targeted for the treatment of congestive heart failure (CHF) in patients ineligible for transplant. GLP-1 is a naturally occurring hormone produced in the intestines in response to food intake."
drug:rGLP-1rdfs:label"rGLP-1"
drug:rGLP-1rdf:typedrugbank:drugs
drug:ragweed pollen extractdrugbank:description"Ragweed pollen extract has been developed by Curalogic. The company has initiated a phase III trial with its product for oral immunotherapy of ragweed allergy. While traditional disease-modifying immunotherapeutics are administered by subcutaneous injection, Curalogic has developed a more convenient orally administered drug. "
drug:ragweed pollen extractrdfs:label"ragweed pollen extract"
drug:ragweed pollen extractrdf:typedrugbank:drugs
drug:recombinant human GM-CSFdrugbank:description"Human GM-CSF (Granulocyte/Monocyte-Colony Stimulating Factor) is a differentially glycosylated factor produced mainly by activated T cells and macrophages. Endothelial cells and fibroblasts can also produce GM-CSF after exposure to TNF-α, IL-1, IL-2 and IFN-γ. GM-CSF is found associated with extracellular matrix and in membrane-bound formats too. GM-CSF stimulates proliferation, activation and differentiation of macrophages and granulocytes and their progenitors. "
drug:recombinant human GM-CSFrdfs:label"recombinant human GM-CSF"
drug:recombinant human GM-CSFrdf:typedrugbank:drugs
drug:recombinant human relaxindrugbank:description"Recombinant human relaxin is a hormone produced during pregnancy that facilitates the birth process by causing a softening and lengthening of the cervix and the pubic symphysis (the place where the pubic bones come together).It is a heterodimer protein secreted by the corpus luteum and placenta during pregnancy."
drug:recombinant human relaxinrdfs:label"recombinant human relaxin"
drug:recombinant human relaxinrdf:typedrugbank:drugs
drug:rhGAD65drugbank:description"rhGAD65 (recombinant human glutamic acid decarboxylase) is a vaccine being developed to treat insulin dependent type 1 diabetes."
drug:rhGAD65drugbank:drugCategorydrugcategory:Vaccines
drug:rhGAD65rdfs:label"rhGAD65"
drug:rhGAD65rdf:typedrugbank:drugs
drug:rhIGFBP-3drugbank:description"rhIGFBP-3 (recombinant human insulin-like growth factor binding protein-3) is Insmed’s proprietary anti-cancer compound that has demonstrated significant decreases in cancerous growth in several models of human. It is developed by Insmed and is currently under phase I of the clinical trail."
drug:rhIGFBP-3rdfs:label"rhIGFBP-3"
drug:rhIGFBP-3rdf:typedrugbank:drugs
drug:rhMBLdrugbank:description"rhMBL is a protein therapeutic being developed by Enzon for the prevention and treatment of severe infections in individuals with low levels of Mannose-Binding Lectin (MBL). Over 10 percent of the general population is estimated to be MBL-deficient. Natural MBL has an oligomeric structure (400-700 kDa), built of subunits that contain three identical peptide chains of 32 kDa each. Although MBL can form several oligomeric forms, there are indications that dimers and trimers are not biologically active and at least a tetramer form is needed for activation of complement."
drug:rhMBLdrugbank:drugCategorydrugcategory:Immunosuppressive Agents
drug:rhMBLrdfs:label"rhMBL"
drug:rhMBLrdf:typedrugbank:drugs
drugcategory:sodium-glucose cotransporter 2 inhibitor rdfs:label"sodium-glucose cotransporter 2 inhibitor "
drug:substance Pdrugbank:description"Homspera is a generic name used by the Company to describe the synthetic peptide Sar9, Met (O2)11-Substance P. Sar9, Met (O2)11-Substance P is an analog of the naturally occurring human neuropeptide Substance P, which can be found throughout the body, including in the airways of humans and many other species. All of the Company's research and development efforts are in early, pre-clinical stages and Homspera, also known as Viprovex and Radilex, has only undergone exploratory studies to evaluate its biological activity in small animals."
drug:substance Prdfs:label"substance P"
drug:substance Prdf:typedrugbank:drugs
drug:talactoferrin alphadrugbank:description"Talactoferrin alfa is a novel immunomodulatory 80 kD protein with demonstrated oral anti-tumor properties. Lactoferrin, a protein found in breast milk is developed by Agennix. It increases body’s immune power and also works as a natural antioxidant, helping to control cell and tissue damage caused by oxidation."
drug:talactoferrin alphardfs:label"talactoferrin alpha"
drug:talactoferrin alphardf:typedrugbank:drugs
drug:tert-butyl 4-(3-thiophen-2-yl-1,2,4-oxadiazol-5-yl)piperidine-1-carboxylatedrugbank:description" experimental This compound belongs to the piperidinecarboxylic acids. These are compounds containing a piperidine ring which bears a carboxylic acid group. Piperidinecarboxylic Acids Organic Compounds Heterocyclic Compounds Piperidines Piperidinecarboxylic Acids and Derivatives Thiophenes Oxadiazoles Tertiary Amines Carbamic Acids and Derivatives Ethers Polyamines thiophene oxadiazole azole carbamic acid derivative tertiary amine polyamine ether amine organonitrogen compound logP 3.77 ALOGPS logS -3.7 ALOGPS Water Solubility 6.87e-02 g/l ALOGPS logP 3.26 ChemAxon IUPAC Name tert-butyl 4-[3-(thiophen-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxylate ChemAxon Traditional IUPAC Name tert-butyl 4-[3-(thiophen-2-yl)-1,2,4-oxadiazol-5-yl]piperidine-1-carboxylate ChemAxon Molecular Weight 335.421 ChemAxon Monoisotopic Weight 335.130362243 ChemAxon SMILES CC(C)(C)OC(=O)N1CCC(CC1)C1=NC(=NO1)C1=CC=CS1 ChemAxon Molecular Formula C16H21N3O3S ChemAxon InChI InChI=1S/C16H21N3O3S/c1-16(2,3)21-15(20)19-8-6-11(7-9-19)14-17-13(18-22-14)12-5-4-10-23-12/h4-5,10-11H,6-9H2,1-3H3 ChemAxon InChIKey InChIKey=METBQPRXNZHZMB-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 68.46 ChemAxon Refractivity 98.84 ChemAxon Polarizability 36.66 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest basic) -3.3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 18690028 PubChem Substance 99444940 ChemSpider 13704102 PDB RF1 BE0002743 HTH-type transcriptional regulator EthR Mycobacterium tuberculosis # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown HTH-type transcriptional regulator EthR Involved in DNA binding ethR Cytoplasmic None 4.93 23757.0 Mycobacterium tuberculosis GenBank Gene Database BX842584 UniProtKB P96222 UniProt Accession ETHR_MYCTU TETR-FAMILY) ETHR Transcriptional regulator, TetR family >TRANSCRIPTIONAL REGULATORY REPRESSOR PROTEIN MTTSAASQASLPRGRRTARPSGDDRELAILATAENLLEDRPLADISVDDLAKGAGISRPT FYFYFPSKEAVLLTLLDRVVNQADMALQTLAENPADTDRENMWRTGINVFFETFGSHKAV TRAGQAARATSVEVAELWSTFMQKWIAYTAAVIDAERDRGAAPRTLPAHELATALNLMNE RTLFASFAGEQPSVPEARVLDTLVHIWVTSIYGENR >651 bp GTGACCACCTCCGCGGCCAGTCAGGCTTCGCTGCCTAGGGGCCGGCGCACCGCGCGGCCG TCCGGCGACGATCGTGAACTGGCGATCCTCGCCACCGCCGAGAACCTTCTCGAGGACCGT CCGCTGGCCGATATCTCGGTCGACGATCTGGCCAAGGGCGCCGGTATCTCGAGGCCGACG TTCTACTTCTATTTCCCATCCAAGGAAGCGGTGCTGCTGACCCTGCTGGACCGGGTGGTC AATCAAGCCGACATGGCCCTACAGACCCTTGCCGAGAATCCCGCCGACACCGACCGCGAG AACATGTGGCGCACCGGGATCAACGTGTTCTTCGAGACATTCGGGTCGCACAAGGCGGTA ACCCGAGCCGGTCAGGCCGCCAGGGCAACCAGTGTCGAAGTCGCCGAACTGTGGTCGACG TTTATGCAGAAGTGGATCGCCTACACGGCCGCCGTGATCGACGCCGAACGCGACCGAGGC GCGGCGCCGCGCACCCTGCCGGCCCATGAACTGGCCACAGCGCTCAACCTGATGAACGAG CGGACGCTGTTCGCGTCATTCGCCGGCGAACAGCCCTCGGTGCCGGAAGCCCGCGTGCTG GATACGCTGGTGCACATCTGGGTGACCAGCATTTACGGCGAGAACCGCTAA PF00440 TetR_N function binding function nucleic acid binding function transcription factor activity function DNA binding process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent process regulation of biological process process regulation of physiological process "
drug:tert-butyl 4-(3-thiophen-2-yl-1,2,4-oxadiazol-5-yl)piperidine-1-carboxylaterdfs:label"tert-butyl 4-(3-thiophen-2-yl-1,2,4-oxadiazol-5-yl)piperidine-1-carboxylate"
drug:tert-butyl 4-(3-thiophen-2-yl-1,2,4-oxadiazol-5-yl)piperidine-1-carboxylaterdf:typedrugbank:drugs
drug:tert-butyl [(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl]carbamatedrugbank:description" experimental This compound belongs to the pyrrolopyrimidines. These are compounds containing a pyrrolopyrimidine moiety, which consists of a pyrrole ring fused to a pyrimidine. Pyrrolopyrimidines Organic Compounds Heterocyclic Compounds Pyrrolopyrimidines Pyrimidones Substituted Pyrroles Primary Aromatic Amines Carbamic Acids and Derivatives Ethers Polyamines pyrimidone primary aromatic amine substituted pyrrole pyrimidine pyrrole carbamic acid derivative polyamine ether amine primary amine organonitrogen compound logP 0.42 ALOGPS logS -3 ALOGPS Water Solubility 2.53e-01 g/l ALOGPS logP 0.28 ChemAxon IUPAC Name tert-butyl N-({2-amino-4-oxo-3H,4H,7H-pyrrolo[2,3-d]pyrimidin-5-yl}methyl)carbamate ChemAxon Traditional IUPAC Name tert-butyl N-({2-amino-4-oxo-3H,7H-pyrrolo[2,3-d]pyrimidin-5-yl}methyl)carbamate ChemAxon Molecular Weight 279.2951 ChemAxon Monoisotopic Weight 279.133139435 ChemAxon SMILES CC(C)(C)OC(=O)NCC1=CNC2=C1C(=O)NC(N)=N2 ChemAxon Molecular Formula C12H17N5O3 ChemAxon InChI InChI=1S/C12H17N5O3/c1-12(2,3)20-11(19)15-5-6-4-14-8-7(6)9(18)17-10(13)16-8/h4H,5H2,1-3H3,(H,15,19)(H4,13,14,16,17,18) ChemAxon InChIKey InChIKey=RXVQMCMIOHBKNE-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 121.6 ChemAxon Refractivity 73.55 ChemAxon Polarizability 28.51 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 11.03 ChemAxon pKa (strongest basic) 5.45 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 25113137 PubChem Substance 99443952 PDB BPQ BE0001405 Queuine tRNA-ribosyltransferase Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Queuine tRNA-ribosyltransferase Translation, ribosomal structure and biogenesis Exchanges the guanine residue with 7-aminomethyl-7- deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis- dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) tgt None 6.85 42843.0 Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) GenBank Gene Database L33777 GenBank Protein Database 498141 UniProtKB P28720 UniProt Accession TGT_ZYMMO EC 2.4.2.29 Guanine insertion enzyme tRNA-guanine transglycosylase >Queuine tRNA-ribosyltransferase MVEATAQETDRPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATVKALKPETVR ATGADIILGNTYHLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGYQVMSLSSLTKQSEE GVTFKSHLDGSRHMLSPERSIEIQHLLGSDIVMAFDECTPYPATPSRAASSMERSMRWAK RSRDAFDSRKEQAENAALFGIQQGSVFENLRQQSADALAEIGFDGYAVGGLAVGEGQDEM FRVLDFSVPMLPDDKPHYLMGVGKPDDIVGAVERGIDMFDCVLPTRSGRNGQAFTWDGPI NIRNARFSEDLTPLDSECHCAVCQKWSRAYIHHLIRAGEILGAMLMTEHNIAFYQQLMQK IRDSISEGRFSQFAQDFRARYFARNS >1200 bp ATGAGCTTGGAAATGATGACGGCAGTCAAAGGAAGAAATGTGGTAGAAGCAACAGCGCAA GAGACCGATCGTCCGCGTTTTTCTTTTTCAATCGCGGCAAGGGAAGGAAAAGCCCGCACC GGCACTATCGAAATGAAGCGGGGCGTTATCCGAACCCCTGCCTTTATGCCGGTTGGCACG GCAGCTACCGTAAAGGCTTTAAAGCCGGAAACAGTTCGGGCAACTGGCGCTGATATTATC TTGGGGAATACCTATCATCTGATGCTTCGTCCGGGTGCCGAACGGATAGCTAAGCTGGGC GGATTACATTCTTTTATGGGGTGGGATCGGCCTATTTTGACGGATAGCGGCGGGTATCAG GTGATGAGCCTATCTTCTTTGACGAAGCAGAGCGAAGAGGGCGTTACCTTTAAAAGTCAC CTTGACGGTTCCCGCCATATGCTGTCGCCGGAACGTTCTATCGAAATCCAGCATTTACTA GGCAGTGATATCGTAATGGCCTTTGACGAATGCACGCCTTATCCAGCAACGCCTTCGCGC GCGGCCTCGTCAATGGAACGCTCGATGCGGTGGGCGAAAAGATCACGGGATGCCTTTGAT AGCCGAAAAGAACAGGCAGAAAATGCGGCTTTGTTCGGAATTCAACAAGGTTCTGTTTTT GAAAATCTGCGGCAACAATCGGCGGATGCTCTGGCTGAAATCGGCTTTGATGGCTATGCT GTTGGGGGATTGGCTGTGGGTGAAGGACAGGATGAAATGTTCCGTGTCCTTGATTTTTCT GTGCCGATGCTGCCCGATGACAAACCTCATTATCTTATGGGCGTTGGTAAGCCTGATGAT ATCGTTGGAGCGGTTGAACGCGGCATTGATATGTTCGATTGCGTCTTGCCGACACGTTCC GGTCGGAATGGGCAAGCCTTTACATGGGATGGGCCTATCAATATCAGAAATGCCCGTTTT TCAGAAGATTTGAAGCCGTTGGATAGTGAATGTCATTGTGCCGTTTGCCAGAAATGGAGC CGCGCCTATATCCATCATTTAATTCGGGCGGGTGAGATCTTGGGGGCTATGCTGATGACA GAGCATAATATCGCCTTTTATCAACAGCTTATGCAAAAAATACGGGACTCTATTTCGGAG GGGCGTTTTTCGCAATTTGCTCAGGATTTCAGAGCGCGCTATTTCGCACGGAATAGCTAG PF01702 TGT function catalytic activity function transferase activity function transferase activity, transferring glycosyl groups function transferase activity, transferring pentosyl groups function queuine tRNA-ribosyltransferase activity process queuosine biosynthesis process metabolism process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process RNA metabolism process tRNA metabolism process physiological process process tRNA modification "
drug:tert-butyl [(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl]carbamaterdfs:label"tert-butyl [(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl]carbamate"
drug:tert-butyl [(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl]carbamaterdf:typedrugbank:drugs
drug:trans NV-04drugbank:description"trans NV-04 is a cardiovascular drug which shows a significant reduction in blood pressure and arterial stiffness."
drug:trans NV-04rdfs:label"trans NV-04"
drug:trans NV-04rdf:typedrugbank:drugs
drug:trans-2-hydroxycinnamic aciddrugbank:description" 614-60-8 experimental This compound belongs to the coumaric acids. These are aromatic compounds containing a cinnamic acid moiety hydroxylated at the C4 carbon atom of the benzene ring. Coumaric Acids Organic Compounds Phenylpropanoids and Polyketides Cinnamic Acids and Derivatives Hydroxycinnamic Acids and Derivatives Hydroxycinnamic Acids Cinnamic Acids Phenylpropenes Styrenes Phenols and Derivatives Enones Enols Enolates Polyamines Carboxylic Acids phenylpropene styrene phenol derivative benzene enone enolate polyamine enol carboxylic acid carboxylic acid derivative (2E)-3-(2-Hydroxyphenyl)-2-propenoic acid (2E)-3-(2-HYDROXYPHENYL)ACRYLIC ACID (2E)-3-(2-hydroxyphenyl)prop-2-enoic acid (E)-3-(2-Hydroxyphenyl)-2-propenoic acid (e)-o-hydroxycinnamic acid 2-Coumarate 2-Coumaric acid 2-Hydroxycinnamate 2-Hydroxycinnamic acid 3-(2-hydroxyphenyl)acrylic acid 3-(2-hydroxyphenyl)prop-2-enoic acid O-Coumaric Acid O-hydroxy-trans-cinnamic acid O-hydroxycinnamic acid Ortho-hydroxycinnamic acid trans-2-Hydroxycinnamate Trans-o-coumaric acid Trans-o-hydroxycinnamic acid logP 1.9 ALOGPS logS -2.1 ALOGPS Water Solubility 1.15e+00 g/l ALOGPS logP 1.83 ChemAxon IUPAC Name (2E)-3-(2-hydroxyphenyl)prop-2-enoic acid ChemAxon Traditional IUPAC Name O-coumaric acid ChemAxon Molecular Weight 164.158 ChemAxon Monoisotopic Weight 164.047344122 ChemAxon SMILES OC(=O)\C=C\C1=CC=CC=C1O ChemAxon Molecular Formula C9H8O3 ChemAxon InChI InChI=1S/C9H8O3/c10-8-4-2-1-3-7(8)5-6-9(11)12/h1-6,10H,(H,11,12)/b6-5+ ChemAxon InChIKey InChIKey=PMOWTIHVNWZYFI-AATRIKPKSA-N ChemAxon Polar Surface Area (PSA) 57.53 ChemAxon Refractivity 45.04 ChemAxon Polarizability 16.11 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 4.04 ChemAxon pKa (strongest basic) -6 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon Melting Point 217 dec °C PhysProp ChEBI 18125 PubChem Compound 637540 PubChem Substance 46505688 KEGG Compound C01772 ChemSpider 553146 PDB 2HC BE0001226 Major NAD(P)H-flavin oxidoreductase Vibrio fischeri # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Major NAD(P)H-flavin oxidoreductase Energy production and conversion Involved in bioluminescence. It is a good supplier of reduced flavin mononucleotide (FMNH2) to the bioluminescence reaction. Major FMN reductase. It is capable of using both NADH and NADPH as electron donors. As electron acceptor, FMN is the most effective, FAD is considerably effective, and riboflavin is the least effective None 6.12 24721.0 Vibrio fischeri GenBank Gene Database D17743 GenBank Protein Database 6539550 UniProtKB P46072 UniProt Accession FRA1_VIBFI EC 1.6.99.- FRASE I >Major NAD(P)H-flavin oxidoreductase MTHPIIHDLENRYTSKKYDPSKKVSQEDLAVLLEALRLSASSINSQPWKFIVIESDAAKQ RMHDSFANMHQFNQPHIKACSHVILFANKLSYTRDDYDVVLSKAVADKRITEEQKEAAFA SFKFVELNCDENGEHKAWTKPQAYLALGNALHTLARLNIDSTTMEGIDPELLSEIFADEL KGYECHVALAIGYHHPSEDYNASLPKSRKAFEDVITIL >657 bp ATGACGCATCCAATTATTCATGATCTTGAAAATCGTTATACATCAAAAAAATATGACCCA TCAAAGAAAGTATCTCAAGAAGATTTAGCGGTTTTGCTTGAGGCTCTGCGTTTATCTGCT TCTTCAATTAATTCACAGCCTTGGAAATTCATTGTTATTGAATCCGATGCAGCGAAGCAA CGTATGCATGATTCGTTTGCAAATATGCATCAGTTTAATCAACCTCACATCAAAGCGTGT TCTCATGTGATTTTATTTGCAAATAAGCTTTCGTATACACGAGATGATTATGATGTGGTT TTATCTAAAGCGGTTGCTGACAAGCGTATTACTGAAGAGCAAAAAGAAGCTGCTTTTGCT TCGTTTAAGTTTGTAGAATTGAACTGTGATGAAAATGGTGAGCATAAAGCATGGACTAAG CCTCAAGCTTATTTAGCTCTTGGTAATGCTCTGCATACATTAGCTAGACTGAACATTGAC TCAACAACAATGGAAGGCATTGATCCTGAATTATTGAGTGAAATTTTTGCTGATGAATTA AAAGGGTATGAATGTCATGTTGCTTTAGCCATTGGTTATCATCATCCAAGCGAAGATTAT AATGCCTCTTTGCCTAAGTCTCGTAAGGCATTTGAAGACGTAATTACCATCCTTTAG PF00881 Nitroreductase function catalytic activity function oxidoreductase activity process electron transport process physiological process process metabolism process cellular metabolism process generation of precursor metabolites and energy BE0003645 Solute carrier family 22 member 8 Human inhibitor # Deguchi T, Ohtsuki S, Otagiri M, Takanaga H, Asaba H, Mori S, Terasaki T: Major role of organic anion transporter 3 in the transport of indoxyl sulfate in the kidney. Kidney Int. 2002 May;61(5):1760-8. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11967025 unknown Solute carrier family 22 member 8 Carbohydrate transport and metabolism Plays an important role in the excretion/detoxification of endogenous and exogenous organic anions, especially from the brain and kidney. Involved in the transport basolateral of steviol, fexofenadine. Transports benzylpenicillin (PCG), estrone- 3-sulfate (E1S), cimetidine (CMD), 2,4-dichloro-phenoxyacetate (2,4-D), p-amino-hippurate (PAH), acyclovir (ACV) and ochratoxin (OTA) SLC22A8 11q11 Basolateral cell membrane 10-30 124-144 155-175 177-197 213-233 237-257 328-348 355-375 387-407 412-432 472-492 9.05 59855.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:10972 GeneCards SLC22A8 GenBank Gene Database AF097491 GenBank Protein Database 4378059 UniProtKB Q8TCC7 UniProt Accession S22A8_HUMAN hOAT3 Organic anion transporter 3 >Solute carrier family 22 member 8 MTFSEILDRVGSMGHFQFLHVAILGLPILNMANHNLLQIFTAATPVHHCRPPHNASTGPW VLPMGPNGKPERCLRFVHPPNASLPNDTQRAMEPCLDGWVYNSTKDSIVTEWDLVCNSNK LKEMAQSIFMAGILIGGLVLGDLSDRFGRRPILTCSYLLLAASGSGAAFSPTFPIYMVFR FLCGFGISGITLSTVILNVEWVPTRMRAIMSTALGYCYTFGQFILPGLAYAIPQWRWLQL TVSIPFFVFFLSSWWTPESIRWLVLSGKSSKALKILRRVAVFNGKKEEGERLSLEELKLN LQKEISLAKAKYTASDLFRIPMLRRMTFCLSLAWFATGFAYYSLAMGVEEFGVNLYILQI IFGGVDVPAKFITILSLSYLGRHTTQAAALLLAGGAILALTFVPLDLQTVRTVLAVFGKG CLSSSFSCLFLYTSELYPTVIRQTGMGVSNLWTRVGSMVSPLVKITGEVQPFIPNIIYGI TALLGGSAALFLPETLNQPLPETIEDLENWSLRAKKPKQEPEVEKASQRIPLQPHGPGLG SS PF07690 MFS_1 component cell component intrinsic to membrane component integral to membrane component membrane function transporter activity function ion transporter activity process physiological process process cellular physiological process process transport process ion transport "
drug:trans-2-hydroxycinnamic acidrdfs:label"trans-2-hydroxycinnamic acid"
drug:trans-2-hydroxycinnamic acidowl:sameAsdrug:EXPT00123
drug:trans-2-hydroxycinnamic acidrdf:typedrugbank:drugs
drug:trans-4-(7-carbamoyl-1H-benzimidazol-2-yl)-1-propylpiperidiniumdrugbank:description" experimental This compound belongs to the benzimidazoles. These are organic compounds containing a benzene ring fused to an imidazole ring (five member ring containing a nitrogen atom, 4 carbon atoms, and two double bonds). Benzimidazoles Organic Compounds Heterocyclic Compounds Benzimidazoles Benzamides Benzoyl Derivatives Piperidines Imidazoles Tertiary Amines Primary Carboxylic Acid Amides Carboxylic Acids Enolates Polyamines benzoyl piperidine benzene imidazole azole carboxamide group tertiary amine primary carboxylic acid amide polyamine carboxylic acid derivative enolate carboxylic acid amine organonitrogen compound logP 2.02 ALOGPS logS -2.9 ALOGPS Water Solubility 3.39e-01 g/l ALOGPS logP 1.24 ChemAxon IUPAC Name 2-(1-propylpiperidin-4-yl)-1H-1,3-benzodiazole-7-carboxamide ChemAxon Traditional IUPAC Name 2-(1-propylpiperidin-4-yl)-3H-1,3-benzodiazole-4-carboxamide ChemAxon Molecular Weight 286.3721 ChemAxon Monoisotopic Weight 286.179361346 ChemAxon SMILES CCCN1CCC(CC1)C1=NC2=C(N1)C(=CC=C2)C(N)=O ChemAxon Molecular Formula C16H22N4O ChemAxon InChI InChI=1S/C16H22N4O/c1-2-8-20-9-6-11(7-10-20)16-18-13-5-3-4-12(15(17)21)14(13)19-16/h3-5,11H,2,6-10H2,1H3,(H2,17,21)(H,18,19) ChemAxon InChIKey InChIKey=KXSIHXHEHABEJX-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 75.01 ChemAxon Refractivity 83.49 ChemAxon Polarizability 32.7 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 9.95 ChemAxon pKa (strongest basic) 9.56 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 9925908 PubChem Substance 99443801 ChemSpider 8101543 PDB AAI BE0001717 Poly [ADP-ribose] polymerase 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Poly [ADP-ribose] polymerase 1 Involved in DNA binding Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks PARP1 1q41-q42 Nucleus None 9.34 113085.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:270 GenAtlas PARP1 GeneCards PARP1 GenBank Gene Database X16674 GenBank Protein Database 1017423 UniProtKB P09874 UniProt Accession PARP1_HUMAN ADPRT EC 2.4.2.30 NAD(+) ADP-ribosyltransferase 1 PARP-1 Poly[ADP-ribose] synthetase 1 >Poly [ADP-ribose] polymerase 1 MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKV GHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKS NRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQ LKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKA QNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSG QLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPE TSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLT GTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSP WGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLE HSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNK LEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPG TKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAV SQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRG GSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIE REGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSA NISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW >3045 bp ATGGCGGAGTCTTCGGATAAGCTCTATCGAGTCGAGTACGCCAAGAGCGGGCGCGCCTCT TGCAAGAAATGCAGCGAGAGCATCCCCAAGGACTCGCTCCGGATGGCCATCATGGTGCAG TCGCCCATGTTTGATGGAAAAGTCCCACACTGGTACCACTTCTCCTGCTTCTGGAAGGTG GGCCACTCCATCCGGCACCCTGACGTTCAGGTGGATGGGTTCTCTGAGCTTCGGTGGGAT GACCAGCAGAAAGTCAAGAAGACAGCGGAAGCTGGAGGAGTGACAGGCAAAGGCCAGGAT GGAATTGGTAGCAAGGCAGAGAAGACTCTGGGTGACTTTGCAGCAGAGTATGCCAAGTCC AACAGAAGTACGTGCAAGGGGTGTATGGAGAAGATAGAAAAGGGCCAGGTGCGCCTGTCC AAGAAGATGGTGGACCCGGAGAAGCCACAGCTAGGCATGATTGACCGCTGGTACCATCCA GGCTGCTTTGTCAAGAACAGGGAGGAGCTGGGTTTCCGGCCCGAGTACAGTGCGAGTCAG CTCAAGGGCTTCAGCCTCCTTGCTACAGAGGATAAAGAAGCCCTGAAGAAGCAGCTCCCA GGAGTCAAGAGTGAAGGAAAGAGAAAAGGCGATGAGGTGGATGGAGTGGATGAAGTGGCG AAGAAGAAATCTAAAAAAGAAAAAGACAAGGATAGTAAGCTTGAAAAAGCCCTAAAGGCT CAGAACGACCTGATCTGGAACATCAAGGACGAGCTAAAGAAAGTGTGTTCAACTAATGAC CTGAAGGAGCTACTCATCTTCAACAAGCAGCAAGTGCCTTCTGGGGAGTCGGCGATCTTG GACCGAGTAGCTGATGGCATGGTGTTCGGTGCCCTCCTTCCCTGCGAGGAATGCTCGGGT CAGCTGGTCTTCAAGAGCGATGCCTATTACTGCACTGGGGACGTCACTGCCTGGACCAAG TGTATGGTCAAGACACAGACACCCAACCGGAAGGAGTGGGTAACCCCAAAGGAATTCCGA GAAATCTCTTACCTCAAGAAATTGAAGGTTAAAAAGCAGGACCGTATATTCCCCCCAGAA ACCAGCGCCTCCGTGGCGGCCACGCCTCCGCCCTCCACAGCCTCGGCTCCTGCTGCTGTG AACTCCTCTGCTTCAGCAGATAAGCCATTATCCAACATGAAGATCCTGACTCTCGGGAAG CTGTCCCGGAACAAGGATGAAGTGAAGGCCATGATTGAGAAACTCGGGGGGAAGTTGACG GGGACGGCCAACAAGGCTTCCCTGTGCATCAGCACCAAAAAGGAGGTGGAAAAGATGAAT AAGAAGATGGAGGAAGTAAAGGAAGCCAACATCCGAGTTGTGTCTGAGGACTTCCTCCAG GACGTCTCCGCCTCCACCAAGAGCCTTCAGGAGTTGTTCTTAGCGCACATCTTGTCCCCT TGGGGGGCAGAGGTGAAGGCAGAGCCTGTTGAAGTTGTGGCCCCAAGAGGGAAGTCAGGG GCTGCGCTCTCCAAAAAAAGCAAGGGCCAGGTCAAGGAGGAAGGTATCAACAAATCTGAA AAGAGAATGAAATTAACTCTTAAAGGAGGAGCAGCTGTGGATCCTGATTCTGGACTGGAA CACTCTGCGCATGTCCTGGAGAAAGGTGGGAAGGTCTTCAGTGCCACCCTTGGCCTGGTG GACATCGTTAAAGGAACCAACTCCTACTACAAGCTGCAGCTTCTGGAGGACGACAAGGAA AACAGGTATTGGATATTCAGGTCCTGGGGCCGTGTGGGTACGGTGATCGGTAGCAACAAA CTGGAACAGATGCCGTCCAAGGAGGATGCCATTGAGCACTTCATGAAATTATATGAAGAA AAAACCGGGAACGCTTGGCACTCCAAAAATTTCACGAAGTATCCCAAAAAGTTCTACCCC CTGGAGATTGACTATGGCCAGGATGAAGAGGCAGTGAAGAAGCTGACAGTAAATCCTGGC ACCAAGTCCAAGCTCCCCAAGCCAGTTCAGGACCTCATCAAGATGATCTTTGATGTGGAA AGTATGAAGAAAGCCATGGTGGAGTATGAGATCGACCTTCAGAAGATGCCCTTGGGGAAG CTGAGCAAAAGGCAGATCCAGGCCGCATACTCCATCCTCAGTGAGGTCCAGCAGGCGGTG TCTCAGGGCAGCAGCGACTCTCAGATCCTGGATCTCTCAAATCGCTTTTACACCCTGATC CCCCACGACTTTGGGATGAAGAAGCCTCCGCTCCTGAACAATGCAGACAGTGTGCAGGCC AAGGTGGAAATGCTTGACAACCTGCTGGACATCGAGGTGGCCTACAGTCTGCTCAGGGGA GGGTCTGATGATAGCAGCAAGGATCCCATCGATGTCAACTATGAGAAGCTCAAAACTGAC ATTAAGGTGGTTGACAGAGATTCTGAAGAAGCCGAGATCATCAGGAAGTATGTTAAGAAC ACTCATGCAACCACACACAATGCGTATGACTTGGAAGTCATCGATATCTTTAAGATAGAG CGTGAAGGCGAATGCCAGCGTTACAAGCCCTTTAAGCAGCTTCATAACCGAAGATTGCTG TGGCACGGGTCCAGGACCACCAACTTTGCTGGGATCCTGTCCCAGGGTCTTCGGATAGCC CCGCCTGAAGCGCCCGTGACAGGCTACATGTTTGGTAAAGGGATCTATTTCGCTGACATG GTCTCCAAGAGTGCCAACTACTGCCATACGTCTCAGGGAGACCCAATAGGCTTAATCCTG TTGGGAGAAGTTGCCCTTGGAAACATGTATGAACTGAAGCACGCTTCACATATCAGCAAG TTACCCAAGGGCAAGCACAGTGTCAAAGGTTTGGGCAAAACTACCCCTGATCCTTCAGCT AACATTAGTCTGGATGGTGTAGACGTTCCTCTTGGGACCGGGATTTCATCTGGTGTGAAT GACACCTCTCTACTATATAACGAGTACATTGTCTATGATATTGCTCAGGTAAATCTGAAG TATCTGCTGAAACTGAAATTCAATTTTAAGACCTCCCTGTGGTAA PF00645 zf-PARP PF00644 PARP PF00533 BRCT PF08063 PADR1 PF02877 PARP_reg PF05406 WGR component nucleus component cell component intracellular component organelle component membrane-bound organelle component intracellular membrane-bound organelle function transferase activity, transferring pentosyl groups function DNA binding function transferase activity function transferase activity, transferring glycosyl groups function binding function NAD+ ADP-ribosyltransferase activity function catalytic activity function nucleic acid binding process biopolymer modification process protein modification process DNA metabolism process protein amino acid ADP-ribosylation process physiological process process metabolism process cellular metabolism process macromolecule metabolism process biopolymer metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism "
drug:trans-4-(7-carbamoyl-1H-benzimidazol-2-yl)-1-propylpiperidiniumrdfs:label"trans-4-(7-carbamoyl-1H-benzimidazol-2-yl)-1-propylpiperidinium"
drug:trans-4-(7-carbamoyl-1H-benzimidazol-2-yl)-1-propylpiperidiniumrdf:typedrugbank:drugs
drug:trans-urocanic aciddrugbank:description" 104-98-3 experimental This compound belongs to the imidazolyl carboxylic acids and derivatives. These are organic compounds containing a carboxylic acid chain (of at least 2 carbon atoms) linked to an imidazole ring. Imidazolyl Carboxylic Acids and Derivatives Organic Compounds Heterocyclic Compounds Azoles Imidazoles Enones Polyamines Enolates Carboxylic Acids enone enolate carboxylic acid carboxylic acid derivative polyamine organonitrogen compound (2E)-3-(1H-imidazol-4-yl)acrylic acid (E)-3-(1H-imidazol-4-yl)-2-propenoic acid Urocanic acid logP 0.22 ALOGPS logS -0.51 ALOGPS Water Solubility 4.25e+01 g/l ALOGPS logP -1 ChemAxon IUPAC Name (2E)-3-(1H-imidazol-4-yl)prop-2-enoic acid ChemAxon Traditional IUPAC Name trans-urocanic acid ChemAxon Molecular Weight 138.124 ChemAxon Monoisotopic Weight 138.042927446 ChemAxon SMILES OC(=O)\C=C\C1=CNC=N1 ChemAxon Molecular Formula C6H6N2O2 ChemAxon InChI InChI=1S/C6H6N2O2/c9-6(10)2-1-5-3-7-4-8-5/h1-4H,(H,7,8)(H,9,10)/b2-1+ ChemAxon InChIKey InChIKey=LOIYMIARKYCTBW-OWOJBTEDSA-N ChemAxon Polar Surface Area (PSA) 65.98 ChemAxon Refractivity 35.57 ChemAxon Polarizability 13.1 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 3.85 ChemAxon pKa (strongest basic) 6.13 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Water Solubility 1500 mg/L (at 17 °C) YALKOWSKY,SH & DANNENFELSER,RM (1992) Melting Point 225 °C PhysProp ChEBI 30817 KEGG Compound C00785 PDB URO SMP00009 Ammonia Recycling DB00116 Tetrahydrofolic acid DB00117 L-Histidine DB00119 Pyruvic acid DB00121 Biotin DB00128 L-Aspartic Acid DB00130 L-Glutamine DB00133 L-Serine DB00142 L-Glutamic Acid DB00145 Glycine DB01971 trans-urocanic acid P20132 Q7L266 P08243 P42357 P31327 A8YXX4 P00367 Q9UI32 P48728 P09622 P23378 P23434 SMP00044 Histidine Metabolism DB00116 Tetrahydrofolic acid DB00117 L-Histidine DB00118 S-Adenosylmethionine DB00142 L-Glutamic Acid DB01373 Calcium DB01593 Zinc DB01971 trans-urocanic acid DB03107 Beta-Alanine Q96KN2 A5YM72 O60678 P19113 P50135 P21397 P30838 P05091 P42357 Q96N76 Q96NU7 O95954 P49590 P12081 P19801 SMP00191 Histidinemia DB00116 Tetrahydrofolic acid DB00117 L-Histidine DB00118 S-Adenosylmethionine DB00142 L-Glutamic Acid DB01373 Calcium DB01593 Zinc DB01971 trans-urocanic acid DB03107 Beta-Alanine Q96KN2 A5YM72 O60678 P19113 P50135 P21397 P30838 P05091 P42357 Q96N76 Q96NU7 O95954 P49590 P12081 P19801 BE0001420 Urocanate hydratase Pseudomonas putida (strain KT2440) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Urocanate hydratase Amino acid transport and metabolism 3-(5-oxo-4,5-dihydro-3H-imidazol-4- yl)propanoate = urocanate + H(2)O hutU Cytoplasm None 5.76 60718.0 Pseudomonas putida (strain KT2440) GenBank Gene Database AE015451 GenBank Protein Database 24986811 UniProtKB Q88CZ6 UniProt Accession HUTU_PSEPK EC 4.2.1.49 Imidazolonepropionate hydrolase Urocanase >Urocanate hydratase MTDNNKYRDVEIRAPRGNKLTAKSWLTEAPLRMLMNNLDPQVAENPKELVVYGGIGRAAR NWACYDKIVETLTRLEDDETLLVQSGKPVGVFKTHSNAPRVLIANSNLVPHWANWEHFNE LDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHYGGSLKGKWVLTAGLGGMGG AQPLAATLAGACSLNIECQQSRIDFRLETRYVDEQATDLDDALARIAKYTAEGKAISIAL HGNAAEILPELVKRGVRPDMVTDQTSAHDPLNGYLPAGWTWEQYRDRAQTEPAAVVKAAK QSMAVHVQAMLDFQKQGIPTFDYGNNIRQMAKEEGVANAFDFPGFVPAYIRPLFCRGVGP FRWAALSGEAEDIYKTDAKVKELIPDDAHLHRWLDMARERISFQGLPARICWVGLGLRAK LGLAFNEMVRSGELSAPVVIGRDHLDSGSVSSPNRETEAMRDGSDAVSDWPLLNALLNTA GGATWVSLHHGGGVGMGFSQHSGMVIVCDGTDEAAERIARVLTNDPGTGVMRHADAGYDI AIDCAKEQGLDLPMITG >1674 bp TCAGCCGGTGATCATCGGCAGGTCCAGGCCCTGCTCCTTGGCGCAGTCGATGGCGATGTC ATAACCGGCATCGGCGTGACGCATGACGCCAGTCCCTGGGTCGTTGGTCAGTACCCGGGC GATGCGCTCGGCGGCCTCATCGGTACCGTCGCAGACGATGACCATGCCCGAGTGCTGCGA GAAGCCCATGCCCACGCCACCGCCATGGTGCAGCGATACCCAGGTGGCGCCGCCTGCGGT GTTCAGCAGGGCGTTGAGCAGCGGCCAGTCGGAAACAGCGTCCGAACCATCACGCATGGC CTCGGTTTCGCGGTTCGGGCTGGATACCGAGCCGGAGTCGAGGTGGTCACGGCCGATCAC CACCGGTGCCGACAGCTCGCCGCTGCGGACCATTTCGTTGAAAGCCAGGCCCAGCTTGGC GCGAAGGCCCAGCCCCACCCAGCAGATACGTGCCGGCAGGCCCTGGAAGCTGATGCGCTC GCGGGCCATGTCCAGCCAGCGGTGCAGGTGGGCGTCGTCGGGGATCAGTTCCTTGACCTT GGCGTCGGTCTTGTAGATGTCCTCGGCTTCACCGGACAGCGCCGCCCAGCGGAACGGGCC GACGCCGCGGCAGAACAGTGGGCGGATGTAGGCCGGGACGAAGCCTGGGAAGTCGAAGGC ATTGGCCACGCCCTCCTCCTTGGCCATCTGGCGGATGTTGTTGCCGTAATCGAAGGTCGG GATGCCCTGCTTCTGGAAGTCCAGCATGGCCTGCACGTGCACGGCCATCGACTGCTTGGC GGCCTTGACCACTGCAGCCGGTTCGGTCTGCGCACGATCGCGGTACTGTTCCCAGGTCCA GCCGGCTGGCAGGTAGCCGTTCAGTGGGTCGTGGGCGCTGGTCTGGTCGGTGACCATGTC CGGGCGGACGCCACGTTTGACCAGCTCTGGGAGGATTTCGGCGGCGTTGCCGTGCAGGGC GATGGAGATGGCCTTGCCTTCGGCGGTGTACTTGGCGATGCGTGCGAGGGCGTCGTCGAG GTCAGTGGCCTGCTCGTCGACGTAGCGGGTTTCCAGGCGGAAGTCGATACGGCTCTGCTG GCATTCGATGTTCAGCGAGCAAGCCCCAGCCAGGGTCGCGGCCAGTGGCTGGGCGCCGCC CATGCCGCCCAGGCCAGCGGTGAGTACCCACTTGCCTTTCAGGCTGCCGCCGTAGTGCTG GCGACCGGCTTCGACGAAGGTTTCATAGGTGCCCTGGACGATGCCCTGGCTGCCGATGTA GATCCAGCTGCCGGCGGTCATCTGGCCATACATCGCCAGGCCCTTGGCGTCCAGTTCGTT GAAGTGTTCCCAGTTGGCCCAGTGTGGCACCAGGTTGGAGTTGGCAATCAGCACGCGCGG TGCGTTGCTGTGGGTCTTGAACACACCGACCGGCTTGCCCGACTGCACCAGCAGGGTTTC GTCGTCTTCCAGGCGGGTCAGGGTTTCGACGATCTTGTCGTAGCAGGCCCAGTTGCGCGC GGCGCGGCCGATACCGCCGTATACCACCAGCTCTTTCGGGTTTTCCGCGACCTGTGGATC GAGGTTGTTCATCAGCATGCGCAGTGGCGCTTCGGTCAGCCAGCTTTTGGCGGTCAGCTT GTTGCCACGTGGGGCACGGATTTCAACGTCACGGTATTTGTTGTTGTCGGTCAC PF01175 Urocanase function carbon-oxygen lyase activity function hydro-lyase activity function catalytic activity function urocanate hydratase activity function lyase activity process amino acid and derivative metabolism process histidine family amino acid metabolism process histidine metabolism process physiological process process histidine catabolism process metabolism process cellular metabolism process amino acid metabolism "
drug:trans-urocanic acidrdfs:label"trans-urocanic acid"
drug:trans-urocanic acidowl:sameAsdrug:Beta-Alanine
drug:trans-urocanic acidowl:sameAsdrug:Biotin
drug:trans-urocanic acidowl:sameAsdrug:Calcium
drug:trans-urocanic acidowl:sameAsdrug:EXPT03207
drug:trans-urocanic acidowl:sameAsdrug:Glycine
drug:trans-urocanic acidowl:sameAsdrug:L-Aspartic Acid
drug:trans-urocanic acidowl:sameAsdrug:L-Glutamic Acid
drug:trans-urocanic acidowl:sameAsdrug:L-Glutamine
drug:trans-urocanic acidowl:sameAsdrug:L-Histidine
drug:trans-urocanic acidowl:sameAsdrug:L-Serine
drug:trans-urocanic acidowl:sameAsdrug:Pyruvic acid
drug:trans-urocanic acidowl:sameAsdrug:S-Adenosylmethionine
drug:trans-urocanic acidowl:sameAsdrug:Tetrahydrofolic acid
drug:trans-urocanic acidowl:sameAsdrug:Zinc
drug:trans-urocanic acidowl:sameAsdrug:trans-urocanic acid
drug:trans-urocanic acidrdf:typedrugbank:drugs
drug:transdermal testosterone geldrugbank:description"Transdermal Testosterone Gel Improves Sexual Function, Mood, Muscle Strength, and Body Composition Parameters in Hypogonadal Men."
drug:transdermal testosterone geldrugbank:interactsWithdrug:Acenocoumarol
drug:transdermal testosterone geldrugbank:interactsWithdrug:Cyclosporine
drug:transdermal testosterone geldrugbank:interactsWithdrug:Warfarin
drug:transdermal testosterone gelrdfs:label"transdermal testosterone gel"
drug:transdermal testosterone gelowl:sameAsdrug:Acenocoumarol
drug:transdermal testosterone gelowl:sameAsdrug:Cyclosporine
drug:transdermal testosterone gelowl:sameAsdrug:Warfarin
drug:transdermal testosterone gelrdf:typedrugbank:drugs
drug:triacetyl uridinedrugbank:description"Triacetyl uridine is a novel approach for treating neurodegenerative diseases associated with impaired mitochondrial function. Triacetyluridine delivers exogenous pyrimidines to the brain, which may help to compensate for bioenergetic defects. "
drug:triacetyl uridinerdfs:label"triacetyl uridine"
drug:triacetyl uridinerdf:typedrugbank:drugs
drug:tributylstannanyldrugbank:description" experimental This compound belongs to the polyamines. These are compounds containing more than one amine group. Polyamines Organic Compounds Organonitrogen Compounds Amines Polyamines Organotin Compounds organotin organometallic compound organic post-transition metal moeity logP 6.17 ALOGPS logS -3.5 ALOGPS Water Solubility 8.82e-02 g/l ALOGPS logP 3.53 ChemAxon IUPAC Name tributyl-$l^{3}-stannyl ChemAxon Traditional IUPAC Name tributyltin ChemAxon Molecular Weight 290.05 ChemAxon Monoisotopic Weight 291.113472435 ChemAxon SMILES CCCC[Sn](CCCC)CCCC ChemAxon Molecular Formula C12H27Sn ChemAxon InChI InChI=1S/3C4H9.Sn/c3*1-3-4-2;/h3*1,3-4H2,2H3; ChemAxon InChIKey InChIKey=PIILXFBHQILWPS-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 0 ChemAxon Refractivity 58.42 ChemAxon Polarizability 27.18 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 0 ChemAxon H Bond Donor Count 0 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 3032732 PubChem Substance 99445072 ChemSpider 5734 PDB TBY BE0003740 Nuclear receptor coactivator 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Nuclear receptor coactivator 2 Involved in nuclear hormone receptor binding Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF- 2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues NCOA2 8q13.3 Nucleus None 6.62 159155.6 Human HUGO Gene Nomenclature Committee (HGNC) GNC:7669 GeneCards NCOA2 GenBank Gene Database X97674 GenBank Protein Database 1877215 UniProtKB Q15596 UniProt Accession NCOA2_HUMAN hTIF2 NCoA-2 Transcriptional intermediary factor 2 >Nuclear receptor coactivator 2 MSGMGENTSDPSRAETRKRKECPDQLGPSPKRNTEKRNREQENKYIEELAELIFANFNDI DNFNFKPDKCAILKETVKQIRQIKEQEKAAAANIDEVQKSDVSSTGQGVIDKDALGPMML EALDGFFFVVNLEGNVVFVSENVTQYLRYNQEELMNKSVYSILHVGDHTEFVKNLLPKSI VNGGSWSGEPPRRNSHTFNCRMLVKPLPDSEEEGHDNQEAHQKYETMQCFAVSQPKSIKE EGEDLQSCLICVARRVPMKERPVLPSSESFTTRQDLQGKITSLDTSTMRAAMKPGWEDLV RRCIQKFHAQHEGESVSYAKRHHHEVLRQGLAFSQIYRFSLSDGTLVAAQTKSKLIRSQT TNEPQLVISLHMLHREQNVCVMNPDLTGQTMGKPLNPISSNSPAHQALCSGNPGQDMTLS SNINFPINGPKEQMGMPMGRFGGSGGMNHVSGMQATTPQGSNYALKMNSPSQSSPGMNPG QPTSMLSPRHRMSPGVAGSPRIPPSQFSPAGSLHSPVGVCSSTGNSHSYTNSSLNALQAL SEGHGVSLGSSLASPDLKMGNLQNSPVNMNPPPLSKMGSLDSKDCFGLYGEPSEGTTGQA ESSCHPGEQKETNDPNLPPAVSSERADGQSRLHDSKGQTKLLQLLTTKSDQMEPSPLASS LSDTNKDSTGSLPGSGSTHGTSLKEKHKILHRLLQDSSSPVDLAKLTAEATGKDLSQESS STAPGSEVTIKQEPVSPKKKENALLRYLLDKDDTKDIGLPEITPKLERLDSKTDPASNTK LIAMKTEKEEMSFEPGDQPGSELDNLEEILDDLQNSQLPQLFPDTRPGAPAGSVDKQAII NDLMQLTAENSPVTPVGAQKTALRISQSTFNNPRPGQLGRLLPNQNLPLDITLQSPTGAG PFPPIRNSSPYSVIPQPGMMGNQGMIGNQGNLGNSSTGMIGNSASRPTMPSGEWAPQSSA VRVTCAATTSAMNRPVQGGMIRNPAASIPMRPSSQPGQRQTLQSQVMNIGPSELEMNMGG PQYSQQQAPPNQTAPWPESILPIDQASFASQNRQPFGSSPDDLLCPHPAAESPSDEGALL DQLYLALRNFDGLEEIDRALGIPELVSQSQAVDPEQFSSQDSNIMLEQKAPVFPQQYASQ AQMAQGSYSPMQDPNFHTMGQRPSYATLRMQPRPGLRPTGLVQNQPNQLRLQLQHRLQAQ QNRQPLMNQISNVSNVNLTLRPGVPTQAPINAQMLAQRQREILNQHLRQRQMHQQQQVQQ RTLMMRGQGLNMTPSMVAPSGMPATMSNPRIPQANAQQFPFPPNYGISQQPDPGFTGATT PQSPLMSPRMAHTQSPMMQQSQANPAYQAPSDINGWAQGNMGGNSMFSQQSPPHFGQQAN TSMYSNNMNINVSMATNTGGMSSMNQMTGQISMTSVTSVPTSGLSSMGPEQVNDPALRGG NLFPNQLPGMDMIKQEGDTTRKYC >4395 bp ATGAGTGGGATGGGAGAAAATACCTCTGACCCCTCCAGGGCAGAGACAAGAAAGCGCAAG GAATGTCCTGACCAACTTGGACCCAGCCCCAAAAGGAACACTGAAAAACGTAATCGTGAA CAGGAAAATAAATATATAGAAGAACTTGCAGAGTTGATTTTTGCAAATTTTAATGATATA GACAACTTTAACTTCAAACCTGACAAATGTGCAATCTTAAAAGAAACTGTGAAGCAAATT CGTCAGATCAAAGAACAAGAGAAAGCAGCAGCTGCCAACATAGATGAAGTGCAGAAGTCA GATGTATCCTCTACAGGGCAGGGTGTCATCGACAAGGATGCGCTGGGGCCTATGATGCTT GAGGCCCTTGATGGGTTCTTCTTTGTAGTGAACCTGGAAGGCAACGTTGTGTTTGTGTCA GAGAATGTGACACAGTATCTAAGGTATAACCAAGAAGAGCTGATGAACAAAAGTGTATAT AGCATCTTGCATGTTGGGGACCACACGGAATTTGTCAAAAACCTGCTGCCAAAGTCTATA GTAAATGGGGGATCTTGGTCTGGCGAACCTCCGAGGCGGAACAGCCATACCTTCAATTGT CGGATGCTGGTAAAACCTTTACCTGATTCAGAAGAGGAGGGTCATGATAACCAGGAAGCT CATCAGAAATATGAAACTATGCAGTGCTTCGCTGTCTCTCAACCAAAGTCCATCAAAGAA GAAGGAGAAGATTTGCAGTCCTGCTTGATTTGCGTGGCAAGAAGAGTTCCCATGAAGGAA AGACCAGTTCTTCCCTCATCAGAAAGTTTTACTACTCGCCAGGATCTCCAAGGCAAGATC ACGTCTCTGGATACCAGCACCATGAGAGCAGCCATGAAACCAGGCTGGGAGGACCTGGTA AGAAGGTGTATTCAGAAGTTCCATGCGCAGCATGAAGGAGAATCTGTGTCCTATGCTAAG AGGCATCATCATGAAGTACTGAGACAAGGATTGGCATTCAGTCAAATCTATCGTTTTTCC TTGTCTGATGGCACTCTTGTTGCTGCACAAACGAAGAGCAAACTCATCCGTTCTCAGACT ACTAATGAACCTCAACTTGTAATATCTTTACATATGCTTCACAGAGAGCAGAATGTGTGT GTGATGAATCCGGATCTGACTGGACAAACGATGGGGAAGCCACTGAATCCAATTAGCTCT AACAGCCCTGCCCATCAGGCCCTGTGCAGTGGGAACCCAGGTCAGGACATGACCCTCAGT AGCAATATAAATTTTCCCATAAATGGCCCAAAGGAACAAATGGGCATGCCCATGGGCAGG TTTGGTGGTTCTGGGGGAATGAACCATGTGTCAGGCATGCAAGCAACCACTCCTCAGGGT AGTAACTATGCACTCAAAATGAACAGCCCCTCACAAAGCAGCCCTGGCATGAATCCAGGA CAGCCCACCTCCATGCTTTCACCAAGGCATCGCATGAGCCCTGGAGTGGCTGGCAGCCCT CGAATCCCACCCAGTCAGTTTTCCCCTGCAGGAAGCTTGCATTCCCCTGTGGGAGTTTGC AGCAGCACAGGAAATAGCCATAGTTATACCAACAGCTCCCTCAATGCACTTCAGGCCCTC AGCGAGGGGCACGGGGTCTCATTAGGGTCATCGTTGGCTTCACCAGACCTAAAAATGGGC AATTTGCAAAACTCCCCAGTTAATATGAATCCTCCCCCACTCAGCAAGATGGGAAGCTTG GACTCAAAAGACTGTTTTGGACTATATGGGGAGCCCTCTGAAGGTACAACTGGACAAGCA GAGAGCAGCTGCCATCCTGGAGAGCAAAAGGAAACAAATGACCCCAACCTGCCCCCGGCC GTGAGCAGTGAGAGAGCTGACGGGCAGAGCAGACTGCATGACAGCAAAGGGCAGACCAAA CTCCTGCAGCTGCTGACCACCAAATCTGATCAGATGGAGCCCTCGCCCTTAGCCAGCTCT TTGTCGGATACAAACAAAGACTCCACAGGTAGCTTGCCTGGTTCTGGGTCTACACATGGA ACCTCGCTCAAGGAGAAGCATAAAATTTTGCACAGACTCTTGCAGGACAGCAGTTCCCCT GTGGACTTGGCCAAGTTAACAGCAGAAGCCACAGGCAAAGACCTGAGCCAGGAGTCCAGC AGCACAGCTCCTGGATCAGAAGTGACTATTAAACAAGAGCCGGTGAGCCCCAAGAAGAAA GAGAATGCACTACTTCGCTATTTGCTAGATAAAGATGATACTAAAGATATTGGTTTACCA GAAATAACCCCCAAACTTGAGAGACTGGACAGTAAGACAGATCCTGCCAGTAACACAAAA TTAATAGCAATGAAAACTGAGAAGGAGGAGATGAGCTTTGAGCCTGGTGACCAGCCTGGC AGTGAGCTGGACAACTTGGAGGAGATTTTGGATGATTTGCAGAATAGTCAATTACCACAG CTTTTCCCAGACACGAGGCCAGGCGCCCCTGCTGGATCAGTTGACAAGCAAGCCATCATC AATGACCTCATGCAACTCACAGCTGAAAACAGCCCTGTCACACCTGTTGGAGCCCAGAAA ACAGCACTGCGAATTTCACAGAGCACTTTTAATAACCCACGACCAGGGCAACTGGGCAGG TTATTGCCAAACCAGAATTTACCACTTGACATCACATTGCAAAGCCCAACTGGTGCTGGA CCTTTCCCACCAATCAGAAACAGTAGTCCCTACTCAGTGATACCTCAGCCAGGAATGATG GGTAATCAAGGGATGATAGGAAACCAAGGAAATTTAGGGAACAGTAGCACAGGAATGATT GGTAACAGTGCTTCTCGGCCTACTATGCCATCTGGAGAATGGGCACCGCAGAGTTCGGCT GTGAGAGTCACCTGTGCTGCTACCACCAGTGCCATGAACCGGCCAGTCCAAGGAGGTATG ATTCGGAACCCAGCAGCCAGCATCCCCATGAGGCCCAGCAGCCAGCCTGGCCAAAGACAG ACGCTTCAGTCTCAGGTCATGAATATAGGGCCATCTGAATTAGAGATGAACATGGGGGGA CCTCAGTATAGCCAACAACAAGCTCCTCCAAATCAGACTGCCCCATGGCCTGAAAGCATC CTGCCTATAGACCAGGCGTCTTTTGCCAGCCAAAACAGGCAGCCATTTGGCAGTTCTCCA GATGACTTGCTATGTCCACATCCTGCAGCTGAGTCTCCGAGTGATGAGGGAGCTCTCCTG GACCAGCTGTATCTGGCCTTGCGGAATTTTGATGGCCTGGAGGAGATTGATAGAGCCTTA GGAATACCCGAACTGGTCAGCCAGAGCCAAGCAGTAGATCCAGAACAGTTCTCAAGTCAG GATTCCAACATCATGCTGGAGCAGAAGGCGCCCGTTTTCCCACAGCAGTATGCATCTCAG GCACAAATGGCCCAGGGTAGCTATTCTCCCATGCAAGATCCAAACTTTCACACCATGGGA CAGCGGCCTAGTTATGCCACACTCCGTATGCAGCCCAGACCGGGCCTCAGGCCCACGGGC CTAGTGCAGAACCAGCCAAATCAACTAAGACTTCAACTTCAGCATCGCCTCCAAGCACAG CAGAATCGCCAGCCACTTATGAATCAAATCAGCAATGTTTCCAATGTGAACTTGACTCTG AGGCCTGGAGTACCAACACAGGCACCTATTAATGCACAGATGCTGGCCCAGAGACAGAGG GAAATCCTGAACCAGCATCTTCGACAGAGACAAATGCATCAGCAACAGCAAGTTCAGCAA CGAACTTTGATGATGAGAGGACAAGGGTTGAATATGACACCAAGCATGGTGGCTCCTAGT GGTATGCCAGCAACTATGAGCAACCCTCGGATTCCCCAGGCAAATGCACAGCAGTTTCCA TTTCCTCCAAACTACGGAATAAGTCAGCAACCTGATCCAGGCTTTACTGGGGCTACGACT CCCCAGAGCCCACTTATGTCACCCCGAATGGCACATACACAGAGTCCCATGATGCAACAG TCTCAGGCCAACCCAGCCTATCAGGCCCCCTCCGACATAAATGGATGGGCGCAGGGGAAC ATGGGCGGAAACAGCATGTTTTCCCAGCAGTCCCCACCACACTTTGGGCAGCAAGCAAAC ACCAGCATGTACAGTAACAACATGAACATCAATGTGTCCATGGCGACCAACACAGGTGGC ATGAGCAGCATGAACCAGATGACAGGACAGATCAGCATGACCTCAGTGACCTCCGTGCCT ACGTCAGGGCTGTCCTCCATGGGTCCCGAGCAGGTTAATGATCCTGCTCTGAGGGGAGGC AACCTGTTCCCAAACCAGCTGCCTGGAATGGATATGATTAAGCAGGAGGGAGACACAACA CGGAAATATTGCTGA PF00989 PAS PF07469 DUF1518 PF08815 Nuc_rec_co-act PF08832 SRC-1 component organelle component membrane-bound organelle component intracellular membrane-bound organelle component nucleus function protein binding function signal transducer activity function transcription factor binding function transcription regulator activity function transcription cofactor activity function transcription coactivator activity function binding process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent process cellular process process cell communication process signal transduction process regulation of biological process process regulation of physiological process process regulation of metabolism BE0000412 Retinoic acid receptor RXR-alpha Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Retinoic acid receptor RXR-alpha Involved in transcription factor activity Nuclear hormone receptor. Involved in the retinoic acid response pathway. Binds 9-cis retinoic acid (9C-RA). ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer RXRA 9q34.3 Nucleus None 7.86 50812.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:10477 GenAtlas RXRA GeneCards RXRA GenBank Gene Database X52773 GenBank Protein Database 35885 IUPHAR 610 Guide to Pharmacology 108 UniProtKB P19793 UniProt Accession RXRA_HUMAN Retinoid X receptor alpha >Retinoic acid receptor RXR-alpha MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPING MGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVP AHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLID KRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAEL AVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVIL LRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDM QMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLL RLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT >1389 bp ATGGACACCAAACATTTCCTGCCGCTCGATTTCTCCACCCAGGTGAACTCCTCCCTCACC TCCCCGACGGGGCGAGGCTCCATGGCTGCCCCCTCGCTGCACCCGTCCCTGGGGCCTGGC ATCGGCTCCCCGGGACAGCTGCATTCTCCCATCAGCACCCTGAGCTCCCCCATCAACGGC ATGGGCCCGCCTTTCTCGGTCATCAGCTCCCCCATGGGCCCCCACTCCATGTCGGTGCCC ACCACACCCACCCTGGGCTTCAGCACTGGCAGCCCCCAGCTCAGCTCACCTATGAACCCC GTCAGCAGCAGCGAGGACATCAAGCCCCCCCTGGGCCTCAATGGCGTCCTCAAGGTCCCC GCCCACCCCTCAGGAAACATGGCTTCCTTCACCAAGCACATCTGCGCCATCTGCGGGGAC CGCTCCTCAGGCAAGCACTATGGAGTGTACAGCTGCGAGGGGTGCAAGGGCTTCTTCAAG CGGACGGTGCGCAAGGACCTGACCTACACCTGCCGCGACAACAAGGACTGCCTGATTGAC AAGCGGCAGCGGAACCGGTGCCAGTACTGCCGCTACCAGAAGTGCCTGGCCATGGGCATG AAGCGGGAAGCCGTGCAGGAGGAGCGGCAGCGTGGCAAGGACCGGAACGAGAATGAGGTG GAGTCGACCAGCAGCGCCAACGAGGACATGCCGGTGGAGAGGATCCTGGAGGCTGAGCTG GCCGTGGAGCCCAAGACCGAGACCTACGTGGAGGCAAACATGGGGCTGAACCCCAGCTCG CCGAACGACCCTGTCACCAACATTTGCCAAGCAGCCGACAAACAGCTTTTCACCCTGGTG GAGTGGGCCAAGCGGATCCCACACTTCTCAGAGCTGCCCCTGGACGACCAGGTCATCCTG CTGCGGGCAGGCTGGAATGAGCTGCTCATCGCCTCCTTCTCCCACCGCTCCATCGCCGTG AAGGACGGGATCCTCCTGGCCACCGGGCTGCACGTCCACCGGAACAGCGCCCACAGCGCA GGGGTGGGCGCCATCTTTGACAGGGTGCTGACGGAGCTTGTGTCCAAGATGCGGGACATG CAGATGGACAAGACGGAGCTGGGCTGCCTGCGCGCCATCGTCCTCTTTAACCCTGACTCC AAGGGGCTCTCGAACCCGGCCGAGGTGGAGGCGCTGAGGGAGAAGGTCTATGCGTCCTTG GAGGCCTACTGCAAGCACAAGTACCCAGAGCAGCCGGGAAGGTTCGCTAAGCTCTTGCTC CGCCTGCCGGCTCTGCGCTCCATCGGGCTCAAATGCCTGGAACATCTCTTCTTCTTCAAG CTCATCGGGGACACACCCATTGACACCTTCCTTATGGAGATGCTGGAGGCGCCGCACCAA ATGACTTAG PF00104 Hormone_recep PF00105 zf-C4 component membrane-bound organelle component intracellular membrane-bound organelle component nucleus component organelle function signal transducer activity function receptor activity function nucleic acid binding function steroid hormone receptor activity function transcription factor activity function steroid binding function ligand-dependent nuclear receptor activity function DNA binding function binding process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent process regulation of biological process process regulation of physiological process "
drug:tributylstannanylrdfs:label"tributylstannanyl"
drug:tributylstannanylrdf:typedrugbank:drugs
drug:tripotassium (1R)-4-biphenyl-4-yl-1-phosphonatobutane-1-sulfonatedrugbank:description" experimental This compound belongs to the biphenyls and derivatives. These are organic compounds containing to benzene rings linked together by a C-C bond. Biphenyls and Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Biphenyls and Derivatives Sulfonyls Sulfonic Acids and Derivatives Organic Sulfites Organic Phosphonic Acids and Derivatives Polyamines sulfonyl sulfonic acid derivative organic sulfite phosphonic acid derivative polyamine logP 2.89 ALOGPS logS -2.5 ALOGPS Water Solubility 1.42e+00 g/l ALOGPS logP 5.07 ChemAxon IUPAC Name potassium (1R)-1-[bis(potassiooxy)phosphoryl]-4-(4-phenylphenyl)butane-1-sulfonate ChemAxon Traditional IUPAC Name potassium (1R)-1-(dipotassiooxyphosphoryl)-4-(4-phenylphenyl)butane-1-sulfonate ChemAxon Molecular Weight 484.628 ChemAxon Monoisotopic Weight 483.931641029 ChemAxon SMILES [H][C@@](CCCC1=CC=C(C=C1)C1=CC=CC=C1)(P(=O)(O[K])O[K])S(=O)(=O)O[K] ChemAxon Molecular Formula C16H16K3O6PS ChemAxon InChI InChI=1S/C16H19O6PS.3K/c17-23(18,19)16(24(20,21)22)8-4-5-13-9-11-15(12-10-13)14-6-2-1-3-7-14;;;/h1-3,6-7,9-12,16H,4-5,8H2,(H2,17,18,19)(H,20,21,22);;;/q;3*+1/p-3/t16-;;;/m1.../s1 ChemAxon InChIKey InChIKey=LBNUOQAEVSXSSE-UFRNLTNDSA-K ChemAxon Polar Surface Area (PSA) 78.9 ChemAxon Refractivity 87.36 ChemAxon Polarizability 41.18 ChemAxon Rotatable Bond Count 10 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest basic) -7.5 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon PubChem Compound 46937072 PubChem Substance 99443895 PDB B70 BE0003866 Dehydrosqualene synthase Staphylococcus aureus # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dehydrosqualene synthase Lipid transport and metabolism Catalyzes the head-to-head condensation of two molecules of farnesyl diphosphate (FPP) into the colorless C(30) carotenoid dehydrosqualene (4,4'-diapophytoene). This is the initial step in the biosynthesis of staphyloxanthin, an orange carotenoid present in most staphylococci strains crtM None 6.05 34312.8 Staphylococcus aureus GeneCards crtM GenBank Gene Database AM920687 GenBank Protein Database 161788394 UniProtKB A9JQL9 UniProt Accession CRTM_STAAU 4,4'-diapophytoene synthase DAP synthase Diapophytoene synthase >Dehydrosqualene synthase MTMMDMNFKYCHKIMKKHSKSFSYAFDLLPEDQRKAVWAIYAVCRKIDDSIDVYGDIQFL NQIKEDIQSIEKYPYEYHHFQSDRRIMMALQHVAQHKNIAFQSFYNLIDTVYKDQHFTMF ETDAELFGYCYGVAGTVGEVLTPILSDHETHQTYDVARRLGESLQLINILRDVGEDFENE RIYFSKQRLKQYEVDIAEVYQNGVNNHYIDLWEYYAAIAEKDFRDVMDQIKVFSIEAQPI IELAARIYIEILDEVRQANYTLHERVFVEKRKKAKLFHEINSKYHRI PF00494 SQS_PSY function transferase activity function catalytic activity process metabolism process biosynthesis process physiological process "
drug:tripotassium (1R)-4-biphenyl-4-yl-1-phosphonatobutane-1-sulfonaterdfs:label"tripotassium (1R)-4-biphenyl-4-yl-1-phosphonatobutane-1-sulfonate"
drug:tripotassium (1R)-4-biphenyl-4-yl-1-phosphonatobutane-1-sulfonaterdf:typedrugbank:drugs
drug:undecan-2-onedrugbank:description" experimental This compound belongs to the ketones. These are organic compounds in which a carbonyl group is bonded to two carbon atoms R2C=O (neither R may be H). Ketones Organic Compounds Organooxygen Compounds Carbonyl Compounds Ketones Polyamines Enolates enolate polyamine logP 4.25 ALOGPS logS -4.2 ALOGPS Water Solubility 1.18e-02 g/l ALOGPS logP 3.92 ChemAxon IUPAC Name undecan-2-one ChemAxon Traditional IUPAC Name undecanone ChemAxon Molecular Weight 170.2918 ChemAxon Monoisotopic Weight 170.167065326 ChemAxon SMILES CCCCCCCCCC(C)=O ChemAxon Molecular Formula C11H22O ChemAxon InChI InChI=1S/C11H22O/c1-3-4-5-6-7-8-9-10-11(2)12/h3-10H2,1-2H3 ChemAxon InChIKey InChIKey=KYWIYKKSMDLRDC-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 17.07 ChemAxon Refractivity 53.03 ChemAxon Polarizability 22.66 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest acidic) 19.64 ChemAxon pKa (strongest basic) -7.3 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon ChEBI 17700 ChemSpider 7871 PDB UOC BE0004376 Acyl-coenzyme A thioesterase 13 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Acyl-coenzyme A thioesterase 13 Secondary metabolites biosynthesis, transport and catabolism Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3- hydroxyphenylacetyl-CoA and 3,4-dihydrohyphenylacetyl-CoA (in vitro) ACOT13 6p22.3 Cytoplasm (By similarity). Mitochondrion (By similarity) None 9.74 14960.4 Human HUGO Gene Nomenclature Committee (HGNC) GNC:20999 GeneCards ACOT13 GenBank Gene Database AF155649 GenBank Protein Database 7677052 UniProtKB Q9NPJ3 UniProt Accession ACO13_HUMAN Acyl-CoA thioesterase 13 Thioesterase superfamily member 2 >Acyl-coenzyme A thioesterase 13 MTSMTQSLREVIKAMTKARNFERVLGKITLVSAAPGKVICEMKVEEEHTNAIGTLHGGLT ATLVDNISTMALLCTERGAPGVSVDMNITYMSPAKLGEDIVITAHVLKQGKTLAFTSVDL TNKATGKLIAQGRHTKHLGN >423 bp ATGACCAGCATGACTCAGTCTCTGCGGGAGGTGATAAAGGCCATGACCAAGGCTCGCAAT TTTGAGAGAGTTTTGGGAAAGATTACTCTTGTCTCTGCTGCTCCTGGGAAAGTGATTTGT GAAATGAAAGTAGAAGAAGAGCATACCAATGCAATAGGCACTCTCCACGGCGGTTTGACA GCCACGTTAGTAGATAACATATCAACAATGGCTCTGCTATGCACGGAAAGGGGAGCACCC GGAGTCAGTGTCGATATGAACATAACGTACATGTCACCTGCAAAATTAGGAGAAGATATA GTGATTACAGCACATGTTCTGAAGCAAGGAAAAACACTTGCATTTACCTCTGTGGATCTG ACCAACAAGGCCACAGGAAAATTAATAGCACAAGGAAGACACACAAAACACCTGGGAAAC TGA PF03061 4HBT function catalytic activity "
drug:undecan-2-onerdfs:label"undecan-2-one"
drug:undecan-2-onerdf:typedrugbank:drugs
drug:vapitadine dihydrochloridedrugbank:description"Vapitadine dihydrochloride is an antihistamine that Barrier Therapeutics is developing as a treatment for allergic reactions of the skin, such as those associated with hives and for the itch associated with atopic dermatitis. An advantage of vapitadine dihydrochloride over other antihistamines may be the absence of the sedation, even at high doses."
drug:vapitadine dihydrochloriderdfs:label"vapitadine dihydrochloride"
drug:vapitadine dihydrochloriderdf:typedrugbank:drugs
drug:{(1s)-1-Benzyl-4-[3-Carbamoyl-1-(1-Carbamoyl-2-Phenyl-Ethylcarbamoyl)-(S)-Propylcarbamoyl]-2-Oxo-5-Phenyl-Pentyl}-Carbamic Acid Tert-Butyl Esterdrugbank:description" experimental This compound belongs to the peptides. These are compounds containing an amide derived from two or more amino carboxylic acid molecules (the same or different) by formation of a covalent bond from the carbonyl carbon of one to the nitrogen atom of another. Peptides Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues N-acyl-alpha Amino Acids and Derivatives Alpha Amino Acid Amides Amphetamines and Derivatives Phenylpropylamines Ketones Secondary Carboxylic Acid Amides Primary Carboxylic Acid Amides Carbamic Acids and Derivatives Carboxylic Acids Enolates Ethers Polyamines n-acyl-alpha amino acid or derivative alpha-amino acid amide alpha-amino acid or derivative amphetamine or derivative phenylpropylamine benzene secondary carboxylic acid amide primary carboxylic acid amide ketone carbamic acid derivative carboxamide group polyamine ether carboxylic acid enolate carbonyl group amine organonitrogen compound logP 2.76 ALOGPS logS -5.7 ALOGPS Water Solubility 1.38e-03 g/l ALOGPS logP 3.46 ChemAxon IUPAC Name tert-butyl N-[(2S,5R)-5-benzyl-5-{[(1S)-3-carbamoyl-1-{[(1R)-1-carbamoyl-2-phenylethyl]carbamoyl}propyl]carbamoyl}-3-oxo-1-phenylpentan-2-yl]carbamate ChemAxon Traditional IUPAC Name tert-butyl N-[(2S,5R)-5-benzyl-5-{[(1S)-3-carbamoyl-1-{[(1R)-1-carbamoyl-2-phenylethyl]carbamoyl}propyl]carbamoyl}-3-oxo-1-phenylpentan-2-yl]carbamate ChemAxon Molecular Weight 685.8091 ChemAxon Monoisotopic Weight 685.347548883 ChemAxon SMILES CC(C)(C)OC(=O)N[C@@H](CC1=CC=CC=C1)C(=O)C[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](CC1=CC=CC=C1)C(N)=O ChemAxon Molecular Formula C38H47N5O7 ChemAxon InChI InChI=1S/C38H47N5O7/c1-38(2,3)50-37(49)43-30(22-26-15-9-5-10-16-26)32(44)24-28(21-25-13-7-4-8-14-25)35(47)41-29(19-20-33(39)45)36(48)42-31(34(40)46)23-27-17-11-6-12-18-27/h4-18,28-31H,19-24H2,1-3H3,(H2,39,45)(H2,40,46)(H,41,47)(H,42,48)(H,43,49)/t28-,29+,30+,31-/m1/s1 ChemAxon InChIKey InChIKey=DDOOHEYBNHOFCV-QNRWOPMTSA-N ChemAxon Polar Surface Area (PSA) 199.78 ChemAxon Refractivity 187.35 ChemAxon Polarizability 72.24 ChemAxon Rotatable Bond Count 20 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 5 ChemAxon pKa (strongest acidic) 12.13 ChemAxon pKa (strongest basic) -0.63 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 46936955 PubChem Substance 46507702 PDB Q50 BE0001342 Gag-Pol polyprotein HIV-1 # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Gag-Pol polyprotein Involved in RNA binding Integrase performs the integration of the newly synthesized dsDNA copy of the viral genome into the host chromosome. The integrated DNA is called provirus gag-pol Nucleus. Cytoplasm (By similarity). Note=Following virus entry, the nuclear localization signal (NLS None 9.03 161901.0 HIV-1 GenBank Gene Database M22639 GenBank Protein Database 329380 UniProtKB P12499 UniProt Accession POL_HV1Z2 Pr160Gag-Pol >Gag-Pol polyprotein MGARASVLSGGKLDAWEKIRLRPGGKKKYRLKHLVWASRELERFALNPGLLETSDGCKQI IGQLQPAIRTGSEELRSLFNTVATLYCVHERIEVKDTKEALEKMEEEQNKSKNKKAQQAA ADAGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVIEEKAFSPEVIPMFSALSEGA TPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGT TSTLQEQIAWMTSNPPIPVGEIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDR FYKTLRAEQASQEVKGWMTETLLVQNANPDCKTILKALGPQATLEEMMTACQGVGGPSHK ARVLAEAMSQATNSAAAVMMQRGNFKGPRKTIKCFNCGKEGHIAKNCRAPRRKGCWKCGK EGHQLKDCTERQANFLREDLAFPQGKAGELSSEQTRANSPTSRELRVWGRDNPLSETGAE RQGTVSFNCPQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMNLPGKWKPKMIGGIG GFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKL KPGMDGPKVKQWPLTEEKIKALTEICTEMEKEGKISRVGPENPYNTPIFAIKKKDSTKWR KLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDKDFRKYTAFTI PSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPEIVIYQYMDDLYVGSD LEIGQHRTKIEELREHLLRWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQSIKLPEKESW TVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKE PVHGVYYDPSKDLIAEIQKQGHGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLAEVV QKISTESIVIWGKTPKFRLPIQKETWETWWVEYWQATWIPEWEFVNTPPLVKLWYQLEKE PIIGAETFYVDGAANRETKLGKAGYVTDRGRQKVVPFTDTTNQKTELQAINLALQDSGLE VNIVTDSQYALGIIQAQPDKSESELVSQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLV SQGIRKVLFLDGIDKAQEEHEKYHNNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHG QVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFILKLAGRWPVKI VHTDNGSNFTSAAVKAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKIIGQVRDQAEHL KTAVQMAVFIHNFKRKGGIGGYSAGERIIDIIATDIQTKELQKQITKIQNFRVYYRDSRD PIWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKVKIIRDYGKQMAGDDCVASRQDED >3009 bp TTTTTTAGGGAAGATTTGGCCTTCCCACAAGGGAAGGCCGGGGAACTTTCTTCAGAGCAG ACCAGAGCCAACAGCCCCACCAGCAGAGAGCTTCGGGTTTGGGGAAGAGATAACCCCCTC TCAGAAACAGGAGCAGAAAGACAAGGAACTGTATCCTTCAACTGCCCTCAAATCACTCTT TGGCAACGACCCCTTGTTACAATAAAAATAGGGGGACAGCTAAAGGAAGCTCTATTAGAT ACAGGAGCAGATGATACAGTATTAGAAGAAATGAATTTGCCAGGAAAATGGAAACCAAAA ATGATAGGGGGAATTGGAGGTTTTATCAAAGTAAGACAGTATGATCAAATACTCATAGAA ATCTGTGGGCATAAAGCTATAGGTACAGTATTAGTAGGACCTACACCTGTCAACATAATT GGAAGAAATTTGTTGACCCAGATTGGCTGCACTTTAAATTTTCCAATTAGTCCTATTGAA ACTGTACCAGTAAAATTAAAGCCAGGAATGGATGGCCCAAAAGTTAAACAATGGCCATTG ACAGAAGAAAAAATAAAAGCATTAACAGAAATTTGTACAGAAATGGAAAAGGAAGGAAAA ATTTCAAGAGTTGGGCCTGAAAATCCATACAATACTCCCATATTTGCCATAAAGAAAAAA GACAGTACCAAGTGGAGAAAATTAGTAGATTTCAGGGAACTTAATAAGAGAACTCAAGAT TTCTGGGAAGTTCAATTAGGAATACCGCATCCGGCAGGGCTAAAAAAGAAAAAATCAGTA ACAGTACTGGATGTGGGTGATGCATATTTTTCAGTTCCCTTAGATAAAGACTTTAGGAAA TATACTGCATTTACCATACCTAGTATAAATAATGAGACACCAGGGATTAGATATCAGTAC AATGTGCTTCCACAGGGATGGAAAGGATCACCGGCAATATTCCAAAGTAGCATGACAAAA ATCTTAGAGCCCTTTAGAAAACAAAATCCAGAAATAGTTATCTATCAATACATGGATGAT TTGTATGTAGGATCTGACTTAGAAATAGGGCAGCATAGAACAAAAATAGAGGAATTAAGA GAACATCTATTAAGGTGGGGATTTACCACACCAGATAAAAAACATCAGAAAGAACCCCCA TTTCTTTGGATGGGGTATGAACTCCATCCTGATAAATGGACAGTACAGTCTATAAAATTG CCAGAAAAGGAGAGCTGGACTGTCAATGATATACAGAAGTTAGTGGGGAAATTAAACTGG GCAAGCCAGATTTATCCAGGAATTAAAGTAAGGCAATTGTGTAAACTCCTTAGGGGAACC AAAGCACTAACAGAAGTAATACCACTAACAGAAGAAGCAGAATTAGAACTGGCAGAAAAC AGGGAAATTCTAAAAGAACCAGTACATGGAGTGTATTATGACCCATCAAAAGACTTAATA GCAGAAATACAGAAACAAGGGCACGGCCAATGGACATACCAAATTTATCAAGAACCATTT AAAAATCTGAAAACAGGAAAGTATGCAAGAATGAGGGGTGCCCACACTAATGATGTAAAA CAATTAGCAGAGGTAGTGCAAAAAATATCCACAGAAAGCATAGTGATATGGGGAAAGACT CCTAAATTTAGATTACCCATACAAAAGGAAACATGGGAAACATGGTGGGTAGAGTATTGG CAAGCCACTTGGATTCCTGAGTGGGAATTTGTCAATACCCCTCCTTTAGTAAAATTATGG TACCAGTTAGAGAAGGAACCCATAATAGGAGCAGAAACTTTCTATGTAGATGGGGCAGCT AATAGAGAGACTAAATTAGGAAAGGCAGGATATGTTACTGACAGAGGAAGACAGAAAGTT GTCCCTTTTACTGATACAACAAATCAGAAGACTGAGTTACAAGCAATTAATTTAGCTTTG CAGGATTCGGGATTAGAAGTAAACATAGTAACAGATTCACAATATGCATTAGGAATCATT CAAGCACAACCAGATAAGAGTGAATCAGAGTTAGTCAGTCAAATAATAGAGCAGTTAATA AAAAAGGAAAAGGTTTACCTGGCATGGGTACCAGCACATAAAGGAATTGGAGGAAATGAA CAAGTAGATAAATTAGTCAGTCAGGGAATCAGGAAAGTACTATTTTTGGATGGAATAGAT AAAGCTCAAGAAGAACATGAGAAATATCACAACAATTGGAGAGCAATGGCTAGTGATTTT AACCTACCACCTGTGGTAGCAAAAGAAATAGTAGCTAGCTGTGATAAATGTCAGCTAAAA GGAGAAGCCATGCATGGACAAGTAGACTGTAGTCCAGGAATATGGCAATTAGATTGTACA CATTTAGAAGGAAAAGTTATCCTGGTAGCAGTTCATGTAGCCAGTGGCTATATAGAAGCA GAAGTTATTCCAGCAGAAACAGGGCAGGAAACAGCATATTTTATTTTAAAATTAGCAGGA AGATGGCCAGTAAAAATAGTACATACAGACAATGGCAGCAATTTCACCAGTGCTGCAGTT AAGGCTGCCTGTTGGTGGGCAGGTATTAAACAGGAATTTGGAATTCCCTACAATCCCCAA AGTCAAGGAGTAGTAGAATCTATGAATAAAGAATTGAAGAAAATTATAGGACAGGTAAGA GATCAAGCTGAGCATCTTAAGACAGCTGTACAAATGGCAGTATTCATCCACAATTTTAAA AGAAAAGGGGGGATTGGGGGATACAGTGCAGGGGAGAGAATAATAGACATAATAGCAACA GACATACAAACTAAAGAATTACAAAAACAAATCACAAAAATTCAAAATTTTCGGGTTTAT TACAGGGACAGCAGAGATCCAATTTGGAAAGGACCAGCAAAGCTCCTCTGGAAAGGTGAA GGGGCAGTAGTAATACAAGACAATAGTGACATAAAGGTAGTACCAAGAAGAAAAGTAAAG ATTATCAGGGATTATGGAAAACAGATGGCAGGTGATGATTGTGTGGCAAGTAGACAGGAT GAGGATTAG PF00078 RVT_1 PF00540 Gag_p17 PF00607 Gag_p24 PF00552 Integrase PF02022 Integrase_Zn PF00075 RnaseH PF00665 rve PF00077 RVP PF06815 RVT_connect PF06817 RVT_thumb PF00098 zf-CCHC function endoribonuclease activity, producing 5'-phosphomonoesters function catalytic activity function nucleic acid binding function ribonuclease H activity function RNA binding function structural molecule activity function nucleotidyltransferase activity function integrase activity function hydrolase activity function aspartic-type endopeptidase activity function ion binding function cation binding function peptidase activity function nuclease activity function transition metal ion binding function endopeptidase activity function RNA-directed DNA polymerase activity function transferase activity function binding function endonuclease activity function zinc ion binding function hydrolase activity, acting on ester bonds function endoribonuclease activity function transferase activity, transferring phosphorus-containing groups function DNA binding process DNA replication process metabolism process DNA metabolism process RNA-dependent DNA replication process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA recombination process macromolecule metabolism process DNA integration process protein metabolism process cellular protein metabolism process viral life cycle process proteolysis process physiological process "
drug:{(1s)-1-Benzyl-4-[3-Carbamoyl-1-(1-Carbamoyl-2-Phenyl-Ethylcarbamoyl)-(S)-Propylcarbamoyl]-2-Oxo-5-Phenyl-Pentyl}-Carbamic Acid Tert-Butyl Esterrdfs:label"{(1s)-1-Benzyl-4-[3-Carbamoyl-1-(1-Carbamoyl-2-Phenyl-Ethylcarbamoyl)-(S)-Propylcarbamoyl]-2-Oxo-5-Phenyl-Pentyl}-Carbamic Acid Tert-Butyl Ester"
drug:{(1s)-1-Benzyl-4-[3-Carbamoyl-1-(1-Carbamoyl-2-Phenyl-Ethylcarbamoyl)-(S)-Propylcarbamoyl]-2-Oxo-5-Phenyl-Pentyl}-Carbamic Acid Tert-Butyl Esterowl:sameAsdrug:EXPT02729
drug:{(1s)-1-Benzyl-4-[3-Carbamoyl-1-(1-Carbamoyl-2-Phenyl-Ethylcarbamoyl)-(S)-Propylcarbamoyl]-2-Oxo-5-Phenyl-Pentyl}-Carbamic Acid Tert-Butyl Esterrdf:typedrugbank:drugs
drug:{(2S)-1-[N-(tert-butoxycarbonyl)glycyl]pyrrolidin-2-yl}methyl (3-chlorophenyl)acetatedrugbank:description" experimental This compound belongs to the n-acyl-alpha amino acids and derivatives. These are compounds containing an alpha amino acid (or a derivative thereof) which bears an acyl group at his terminal nitrogen atom. N-acyl-alpha Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Alpha Amino Acid Amides Phenylacetic Acid Derivatives Chlorobenzenes Dicarboxylic Acids and Derivatives Aryl Chlorides Tertiary Carboxylic Acid Amides Pyrrolidines Carbamic Acids and Derivatives Carboxylic Acid Esters Tertiary Amines Carboxylic Acids Polyamines Ethers Enolates Organochlorides phenylacetate chlorobenzene aryl chloride aryl halide benzene dicarboxylic acid derivative tertiary carboxylic acid amide pyrrolidine tertiary amine carboxamide group carbamic acid derivative carboxylic acid ester ether polyamine enolate carboxylic acid organohalogen organochloride amine organonitrogen compound logP 2.74 ALOGPS logS -4.2 ALOGPS Water Solubility 2.90e-02 g/l ALOGPS logP 2.64 ChemAxon IUPAC Name [(2S)-1-(2-{[(tert-butoxy)carbonyl]amino}acetyl)pyrrolidin-2-yl]methyl 2-(3-chlorophenyl)acetate ChemAxon Traditional IUPAC Name [(2S)-1-{2-[(tert-butoxycarbonyl)amino]acetyl}pyrrolidin-2-yl]methyl 2-(3-chlorophenyl)acetate ChemAxon Molecular Weight 410.892 ChemAxon Monoisotopic Weight 410.160849691 ChemAxon SMILES [H][C@@]1(COC(=O)CC2=CC(Cl)=CC=C2)CCCN1C(=O)CNC(=O)OC(C)(C)C ChemAxon Molecular Formula C20H27ClN2O5 ChemAxon InChI InChI=1S/C20H27ClN2O5/c1-20(2,3)28-19(26)22-12-17(24)23-9-5-8-16(23)13-27-18(25)11-14-6-4-7-15(21)10-14/h4,6-7,10,16H,5,8-9,11-13H2,1-3H3,(H,22,26)/t16-/m0/s1 ChemAxon InChIKey InChIKey=ONXGIEJBNQLITK-INIZCTEOSA-N ChemAxon Polar Surface Area (PSA) 84.94 ChemAxon Refractivity 104.67 ChemAxon Polarizability 42.9 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 13.46 ChemAxon pKa (strongest basic) -4.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 24754814 PubChem Substance 99444623 PDB M18 BE0000048 Prothrombin Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Prothrombin Involved in blood clotting cascade Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C F2 11p11-q12 Secreted protein; extracellular space None 5.7 70037.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3535 GenAtlas F2 GeneCards F2 GenBank Gene Database M17262 GenBank Protein Database 339641 UniProtKB P00734 UniProt Accession THRB_HUMAN Activated Factor II [IIa] Coagulation factor II EC 3.4.21.5 Prothrombin precursor Thrombin >Prothrombin precursor MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY GFYTHVFRLKKWIQKVIDQFGE >1869 bp ATGGCGCACGTCCGAGGCTTGCAGCTGCCTGGCTGCCTGGCCCTGGCTGCCCTGTGTAGC CTTGTGCACAGCCAGCATGTGTTCCTGGCTCCTCAGCAAGCACGGTCGCTGCTCCAGCGG GTCCGGCGAGCCAACACCTTCTTGGAGGAGGTGCGCAAGGGCAACCTAGAGCGAGAGTGC GTGGAGGAGACGTGCAGCTACGAGGAGGCCTTCGAGGCTCTGGAGTCCTCCACGGCTACG GATGTGTTCTGGGCCAAGTACACAGCTTGTGAGACAGCGAGGACGCCTCGAGATAAGCTT GCTGCATGTCTGGAAGGTAACTGTGCTGAGGGTCTGGGTACGAACTACCGAGGGCATGTG AACATCACCCGGTCAGGCATTGAGTGCCAGCTATGGAGGAGTCGCTACCCACATAAGCCT GAAATCAACTCCACTACCCATCCTGGGGCCGACCTACAGGAGAATTTCTGCCGCAACCCC GACAGCAGCACCACGGGACCCTGGTGCTACACTACAGACCCCACCGTGAGGAGGCAGGAA TGCAGCATCCCTGTCTGTGGCCAGGATCAAGTCACTGTAGCGATGACTCCACGCTCCGAA GGCTCCAGTGTGAATCTGTCACCTCCATTGGAGCAGTGTGTCCCTGATCGGGGGCAGCAG TACCAGGGGCGCCTGGCGGTGACCACACATGGGCTCCCCTGCCTGGCCTGGGCCAGCGCA CAGGCCAAGGCCCTGAGCAAGCACCAGGACTTCAACTCAGCTGTGCAGCTGGTGGAGAAC TTCTGCCGCAACCCAGACGGGGATGAGGAGGGCGTGTGGTGCTATGTGGCCGGGAAGCCT GGCGACTTTGGGTACTGCGACCTCAACTATTGTGAGGAGGCCGTGGAGGAGGAGACAGGA GATGGGCTGGATGAGGACTCAGACAGGGCCATCGAAGGGCGTACCGCCACCAGTGAGTAC CAGACTTTCTTCAATCCGAGGACCTTTGGCTCGGGAGAGGCAGACTGTGGGCTGCGACCT CTGTTCGAGAAGAAGTCGCTGGAGGACAAAACCGAAAGAGAGCTCCTGGAATCCTACATC GACGGGCGCATTGTGGAGGGCTCGGATGCAGAGATCGGCATGTCACCTTGGCAGGTGATG CTTTTCCGGAAGAGTCCCCAGGAGCTGCTGTGTGGGGCCAGCCTCATCAGTGACCGCTGG GTCCTCACCGCCGCCCACTGCCTCCTGTACCCGCCCTGGGACAAGAACTTCACCGAGAAT GACCTTCTGGTGCGCATTGGCAAGCACTCCCGCACAAGGTACGAGCGAAACATTGAAAAG ATATCCATGTTGGAAAAGATCTACATCCACCCCAGGTACAACTGGCGGGAGAACCTGGAC CGGGACATTGCCCTGATGAAGCTGAAGAAGCCTGTTGCCTTCAGTGACTACATTCACCCT GTGTGTCTGCCCGACAGGGAGACGGCAGCCAGCTTGCTCCAGGCTGGATACAAGGGGCGG GTGACAGGCTGGGGCAACCTGAAGGAGACGTGGACAGCCAACGTTGGTAAGGGGCAGCCC AGTGTCCTGCAGGTGGTGAACCTGCCCATTGTGGAGCGGCCGGTCTGCAAGGACTCCACC CGGATCCGCATCACTGACAACATGTTCTGTGCTGGTTACAAGCCTGATGAAGGGAAACGA GGGGATGCCTGTGAAGGTGACAGTGGGGGACCCTTTGTCATGAAGAGCCCCTTTAACAAC CGCTGGTATCAAATGGGCATCGTCTCATGGGGTGAAGGCTGTGACCGGGATGGGAAATAT GGCTTCTACACACATGTGTTCCGCCTGAAGAAGTGGATACAGAAGGTCATTGATCAGTTT GGAGAGTAG PF00594 Gla PF00051 Kringle PF00089 Trypsin component extracellular region function catalytic activity function thrombin activity function hydrolase activity function calcium ion binding function peptidase activity function ion binding function endopeptidase activity function cation binding function serine-type endopeptidase activity function binding process blood coagulation process metabolism process macromolecule metabolism process protein metabolism process proteolysis process cellular protein metabolism process organismal physiological process process regulation of body fluids process physiological process process hemostasis "
drug:{(2S)-1-[N-(tert-butoxycarbonyl)glycyl]pyrrolidin-2-yl}methyl (3-chlorophenyl)acetaterdfs:label"{(2S)-1-[N-(tert-butoxycarbonyl)glycyl]pyrrolidin-2-yl}methyl (3-chlorophenyl)acetate"
drug:{(2S)-1-[N-(tert-butoxycarbonyl)glycyl]pyrrolidin-2-yl}methyl (3-chlorophenyl)acetaterdf:typedrugbank:drugs
drug:{(2Z)-3-[(6-chloropyridin-3-yl)methyl]-1,3-thiazolidin-2-ylidene}cyanamidedrugbank:description" experimental This compound belongs to the pyridines and derivatives. These are compounds containing a pyridine ring, which is a six-member aromatic heterocycle which consists of one nitrogen atom and five carbon atoms. Pyridines and Derivatives Organic Compounds Heterocyclic Compounds Pyridines and Derivatives Aryl Chlorides Thiazolidines Tertiary Amines Nitriles Polyamines Organochlorides thiazolidine tertiary amine nitrile polyamine organochloride amine organohalogen organonitrogen compound logP 1.91 ALOGPS logS -2.7 ALOGPS Water Solubility 4.58e-01 g/l ALOGPS logP 2.06 ChemAxon IUPAC Name {[(2Z)-3-[(6-chloropyridin-3-yl)methyl]-1,3-thiazolidin-2-ylidene]amino}carbonitrile ChemAxon Traditional IUPAC Name [(2Z)-3-[(6-chloropyridin-3-yl)methyl]-1,3-thiazolidin-2-ylidene]aminocarbonitrile ChemAxon Molecular Weight 252.723 ChemAxon Monoisotopic Weight 252.023644705 ChemAxon SMILES ClC1=NC=C(CN2CCS\C2=N/C#N)C=C1 ChemAxon Molecular Formula C10H9ClN4S ChemAxon InChI InChI=1S/C10H9ClN4S/c11-9-2-1-8(5-13-9)6-15-3-4-16-10(15)14-7-12/h1-2,5H,3-4,6H2/b14-10- ChemAxon InChIKey InChIKey=HOKKPVIRMVDYPB-UVTDQMKNSA-N ChemAxon Polar Surface Area (PSA) 52.28 ChemAxon Refractivity 67.05 ChemAxon Polarizability 24.48 ChemAxon Rotatable Bond Count 2 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 0 ChemAxon pKa (strongest basic) 1.62 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 115224 PubChem Substance 99445091 ChemSpider 103099 PDB TH4 BE0003963 CHRNA7-FAM7A fusion protein Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown CHRNA7-FAM7A fusion protein Involved in extracellular ligand-gated ion channel acti CHRFAM7A 15q13.1 Membrane 144-164 172-192 205-225 240-254 380-400 6.55 46217.3 Human HUGO Gene Nomenclature Committee (HGNC) GNC:15781 GeneCards CHRFAM7A GenBank Gene Database AK292984 GenBank Protein Database 158259429 UniProtKB Q494W8 UniProt Accession CRFM7_HUMAN CHRNA7-DR1 D-10 >CHRNA7-FAM7A fusion protein MQKYCIYQHFQFQLLIQHLWIAANCDIADERFDATFHTNVLVNSSGHCQYLPPGIFKSSC YIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPGKRSERFY ECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLL SLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPDGGKMPKW TRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLASVEMSAVAPPPASNGNLLYIGFR GLDGVHCVPTPDSGVVCGRMACSPTHDEHLLHGGQPPEGDPDLAKILEEVRYIANRFRCQ DESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDFA >1239 bp ATGCAAAAATATTGCATCTACCAGCATTTTCAGTTCCAATTGCTAATCCAGCATTTGTGG ATAGCTGCAAACTGTGATATTGCTGATGAGCGCTTTGACGCCACATTCCACACTAACGTG TTGGTGAATTCTTCTGGGCATTGCCAGTACCTGCCTCCAGGCATATTCAAGAGTTCCTGC TACATCGATGTACGCTGGTTTCCCTTTGATGTGCAGCACTGCAAACTGAAGTTTGGGTCC TGGTCTTACGGAGGCTGGTCCTTGGATCTGCAGATGCAGGAGGCAGATATCAGTGGCTAT ATCCCCAATGGAGAATGGGACCTAGTGGGAATCCCCGGCAAGAGGAGTGAAAGGTTCTAT GAGTGCTGCAAAGAGCCCTACCCTGATGTCACCTTCACAGTGACCATGCGCCGCAGGACA CTCTACTATGGCCTCAACCTGCTGATCCCCTGTGTGCTCATCTCCGCCCTCGCCCTGCTG GTGTTCCTGCTTCCTGCAGATTCCGGGGAGAAGATTTCCCTGGGGATAACAGTCTTACTC TCTCTTACCGTCTTCATGCTGCTCGTGGCTGAGATCATGCCCGCAACATCCGATTCGGTA CCATTGATAGCCCAGTACTTCGCCAGCACCATGATCATCGTGGGCCTCTCGGTGGTGGTG ACGGTGATCGTGCTGCAGTACCACCACCACGACCCCGACGGGGGCAAGATGCCCAAGTGG ACCAGAGTCATCCTTCTGAACTGGTGCGCGTGGTTCCTGCGAATGAAGAGGCCCGGGGAG GACAAGGTGCGCCCGGCCTGCCAGCACAAGCAGCGGCGCTGCAGCCTGGCCAGTGTGGAG ATGAGCGCCGTGGCGCCGCCGCCCGCCAGCAACGGGAACCTGCTGTACATCGGCTTCCGC GGCCTGGACGGCGTGCACTGTGTCCCGACCCCCGACTCTGGGGTAGTGTGTGGCCGCATG GCCTGCTCCCCCACGCACGATGAGCACCTCCTGCACGGTGGGCAACCCCCCGAGGGGGAC CCGGACTTGGCCAAGATCCTGGAGGAGGTCCGCTACATTGCCAACCGCTTCCGCTGCCAG GACGAAAGCGAGGCGGTCTGCAGCGAGTGGAAGTTCGCCGCCTGTGTGGTGGACCGCCTG TGCCTCATGGCCTTCTCGGTCTTCACCATCATCTGCACCATCGGCATCCTGATGTCGGCT CCCAACTTCGTGGAGGCCGTGTCCAAAGACTTTGCGTAA PF02931 Neur_chan_LBD PF02932 Neur_chan_memb component postsynaptic membrane component intrinsic to membrane component integral to membrane component membrane component cell function ion transporter activity function ion channel activity function signal transducer activity function receptor activity function transporter activity function ligand-gated ion channel activity function extracellular ligand-gated ion channel activity function neurotransmitter receptor activity process ion transport process physiological process process cellular physiological process process transport "
drug:{(2Z)-3-[(6-chloropyridin-3-yl)methyl]-1,3-thiazolidin-2-ylidene}cyanamiderdfs:label"{(2Z)-3-[(6-chloropyridin-3-yl)methyl]-1,3-thiazolidin-2-ylidene}cyanamide"
drug:{(2Z)-3-[(6-chloropyridin-3-yl)methyl]-1,3-thiazolidin-2-ylidene}cyanamiderdf:typedrugbank:drugs
drug:{(2Z)-4-AMINO-2-[(4-METHOXYPHENYL)IMINO]-2,3-DIHYDRO-1,3-THIAZOL-5-YL}(4-METHOXYPHENYL)METHANONEdrugbank:description" experimental This compound belongs to the acetophenones. These are organic compounds containing the acetophenone structure. Acetophenones Organic Compounds Benzenoids Benzene and Substituted Derivatives Acetophenones Thiazolecarboxylic Acids and Derivatives Anisoles Benzoyl Derivatives Alkyl Aryl Ethers Primary Aromatic Amines Aminothiazoles Ketones Polyamines Enolates phenol ether anisole thiazolecarboxylic acid or derivative benzoyl alkyl aryl ether 1,3-thiazolamine primary aromatic amine thiazole azole ketone ether enolate polyamine carbonyl group primary amine amine organonitrogen compound logP 2.5 ALOGPS logS -3.9 ALOGPS Water Solubility 4.85e-02 g/l ALOGPS logP 3.18 ChemAxon IUPAC Name (2Z)-5-[(4-methoxyphenyl)carbonyl]-2-[(4-methoxyphenyl)imino]-2,3-dihydro-1,3-thiazol-4-amine ChemAxon Traditional IUPAC Name (2Z)-5-[(4-methoxyphenyl)carbonyl]-2-[(4-methoxyphenyl)imino]-3H-1,3-thiazol-4-amine ChemAxon Molecular Weight 355.411 ChemAxon Monoisotopic Weight 355.099062115 ChemAxon SMILES COC1=CC=C(C=C1)\N=C1\NC(N)=C(S1)C(=O)C1=CC=C(OC)C=C1 ChemAxon Molecular Formula C18H17N3O3S ChemAxon InChI InChI=1S/C18H17N3O3S/c1-23-13-7-3-11(4-8-13)15(22)16-17(19)21-18(25-16)20-12-5-9-14(24-2)10-6-12/h3-10H,19H2,1-2H3,(H,20,21) ChemAxon InChIKey InChIKey=XQKUGFIWKSKCDL-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 85.94 ChemAxon Refractivity 110.57 ChemAxon Polarizability 38.31 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 10.84 ChemAxon pKa (strongest basic) 3.78 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 399618 PubChem Substance 99443959 ChemSpider 354219 PDB BRK BE0003958 Casein kinase I isoform gamma-3 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Casein kinase I isoform gamma-3 Involved in ATP binding Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling (By similarity) CSNK1G3 5q23 Cytoplasm None 9.63 51388.1 Human HUGO Gene Nomenclature Committee (HGNC) GNC:2456 GeneCards CSNK1G3 GenBank Gene Database AF049089 GenBank Protein Database 4590040 UniProtKB Q9Y6M4 UniProt Accession KC1G3_HUMAN CKI-gamma 3 >Casein kinase I isoform gamma-3 MENKKKDKDKSDDRMARPSGRSGHNTRGTGSSSSGVLMVGPNFRVGKKIGCGNFGELRLG KNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLG PSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQV IHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFM YFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEKPD YDYLRKLFTDLFDRKGYMFDYEYDWIGKQLPTPVGAVQQDPALSSNREAHQHRDKMQQSK NQSADHRAAWDSQQANPHHLRAHLAADRHGGSVQVVSSTNGELNTDDPTAGRSNAPITAP TEVEVMDETKCCCFFKRRKRKTIQRHK >1344 bp ATGGAAAATAAAAAGAAAGACAAGGACAAATCAGATGATAGAATGGCACGACCTAGTGGT CGATCGGGACACAACACTCGAGGAACTGGGTCTTCATCGTCTGGAGTTTTAATGGTTGGA CCTAACTTTAGAGTTGGAAAAAAAATTGGATGTGGCAATTTTGGAGAATTACGATTAGGG AAAAATTTATACACAAATGAATATGTGGCAATTAAGTTGGAGCCCATGAAATCAAGAGCA CCACAGCTACATTTGGAATACAGATTCTATAAGCAGTTAGGATCTGGAGATGGTATACCT CAAGTTTACTATTTCGGCCCTTGTGGTAAATACAATGCTATGGTGCTGGAACTGCTGGGA CCTAGTTTGGAAGACTTGTTTGACTTGTGTGACAGAACATTTTCTCTTAAAACAGTTCTC ATGATAGCTATACAACTGATTTCTCGCATGGAATATGTCCATTCAAAGAACTTGATATAC AGAGATGTAAAACCTGAGAACTTCTTAATAGGACGACCAAGAAACAAAACCCAGCAAGTT ATTCACATTATAGATTTTGGTTTGGCAAAGGAATATATTGATCCGGAGACAAAGAAACAC ATACCATACAGAGAACACAAGAGCCTTACAGGAACAGCTAGATATATGAGCATAAACACA CATTTAGGAAAAGAACAAAGTAGAAGAGACGATTTAGAAGCTTTAGGTCATATGTTCATG TATTTTCTGAGAGGCAGTCTTCCTTGGCAAGGCTTAAAGGCTGACACATTAAAGGAGAGG TATCAGAAAATTGGAGATACAAAACGGGCTACACCAATAGAAGTGTTATGTGAAAATTTT CCAGAAATGGCAACATATCTTCGTTATGTAAGAAGGCTAGATTTTTTTGAAAAACCAGAC TATGAATACTTAAGAAAGCTTTTTACTGACTTGTTTGATCGAAAAGGATATATGTTTGAT TATGAATATGACTGGATTGGTAAACAGTTGCCTACTCCAGTGGGTGCAGTTCAGCAAGAT CCTGCTCTGTCATCAAACAGAGAAGCACATCAACACAGAGATAAGATGCAACAATCCAAA AACCAGTCGGCAGACCACAGGGCAGCTTGGGACTCCCAGCAGGCAAATCCCCACCATTTG AGAGCTCACCTTGCAGCAGACAGACATGGTGGCTCGGTACAGGTTGTAAGTTCTACAAAT GGAGAGTTAAACACAGATGACCCCACCGCAGGACGTTCAAATGCACCCATCACAGCCCCT ACTGAAGTAGAAGTGATGGATGAAACCAAGTGCTGCTGCTTTTTCAAACGAAGGAAAAGG AAAACCATACAGCGCCACAAATGA PF00069 Pkinase function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity process physiological process process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification "
drug:{(2Z)-4-AMINO-2-[(4-METHOXYPHENYL)IMINO]-2,3-DIHYDRO-1,3-THIAZOL-5-YL}(4-METHOXYPHENYL)METHANONErdfs:label"{(2Z)-4-AMINO-2-[(4-METHOXYPHENYL)IMINO]-2,3-DIHYDRO-1,3-THIAZOL-5-YL}(4-METHOXYPHENYL)METHANONE"
drug:{(2Z)-4-AMINO-2-[(4-METHOXYPHENYL)IMINO]-2,3-DIHYDRO-1,3-THIAZOL-5-YL}(4-METHOXYPHENYL)METHANONErdf:typedrugbank:drugs
drug:{1-[(3-Hydroxy-Methyl-5-Phosphonooxy-Methyl-Pyridin-4-Ylmethyl)-Amino]-Ethyl}-Phosphonic Aciddrugbank:description" experimental This compound belongs to the pyridines and derivatives. These are compounds containing a pyridine ring, which is a six-member aromatic heterocycle which consists of one nitrogen atom and five carbon atoms. Pyridines and Derivatives Organic Compounds Heterocyclic Compounds Pyridines and Derivatives Organic Phosphoric Acids Organophosphate Esters Organic Phosphonic Acids Polyamines Dialkylamines phosphonic acid phosphonic acid derivative secondary amine secondary aliphatic amine polyamine amine organonitrogen compound logP -0.7 ALOGPS logS -1.9 ALOGPS Water Solubility 3.98e+00 g/l ALOGPS logP -4.9 ChemAxon IUPAC Name [(1S)-1-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]ethyl]phosphonic acid ChemAxon Traditional IUPAC Name (1S)-1-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]ethylphosphonic acid ChemAxon Molecular Weight 356.206 ChemAxon Monoisotopic Weight 356.053838586 ChemAxon SMILES C[C@@H](NCC1=C(O)C(C)=NC=C1COP(O)(O)=O)P(O)(O)=O ChemAxon Molecular Formula C10H18N2O8P2 ChemAxon InChI InChI=1S/C10H18N2O8P2/c1-6-10(13)9(4-12-7(2)21(14,15)16)8(3-11-6)5-20-22(17,18)19/h3,7,12-13H,4-5H2,1-2H3,(H2,14,15,16)(H2,17,18,19)/t7-/m0/s1 ChemAxon InChIKey InChIKey=WHDCJKAOZPBUAY-ZETCQYMHSA-N ChemAxon Polar Surface Area (PSA) 169.44 ChemAxon Refractivity 76.74 ChemAxon Polarizability 30.62 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 9 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) -0.6 ChemAxon pKa (strongest basic) 8.79 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon PubChem Compound 445719 PubChem Substance 46506756 PDB IN5 BE0001344 Alanine racemase Geobacillus stearothermophilus # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Alanine racemase Cell wall/membrane/envelope biogenesis Provides the D-alanine required for cell wall biosynthesis alr None 7.11 43594.0 Geobacillus stearothermophilus GenBank Gene Database M19142 GenBank Protein Database 142467 UniProtKB P10724 UniProt Accession ALR_GEOSE EC 5.1.1.1 >Alanine racemase MNDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVARTALEAGAS RLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRIALTVFRSDWLEEASALYSG PFPIHFHLKMDTGMGRLGVKDEEETKRIVALIERHPHFVLEGLYTHFATADEVNTDYFSY QYTRFLHMLEWLPSRPPLVHCANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYP LKEAFSLHSRLVHVKKLQPGEKVSYGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVD GQKAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLETINYEVPCTI SYRVPRIFFRHKRIMEVRNAIGRGESSA >1161 bp ATGAACGACTTTCATCGCGATACGTGGGCGGAAGTGGATTTGGACGCCATTTACGACAAT GTGGAGAATTTGCGCCGTTTGCTGCCGGACGACACGCACATTATGGCGGTCGTGAAAGCG AACGCCTATGGACATGGGGATGTGCAGGTGGCAAGGACAGCGCTCGAACGGGGGCCTCCG CCTGCGGTTGCCTTTTTGGATGAGGCGCTCGCTTTAAGGGAAAAAGGAATCGAAGCGCCG ATTCTAGTTCTCGGGGCTTCCCGTCCAGCTGATGCGGCGCTGGCCGCCCAGCAGCGCATT GCCCTGACCGTGTTCCGCTCCGACTGGTTGGAAGAAGCGTCCGCCCTTTACAGCGGCCCT TTTCCTATTCATTTCCATTTGAAAATGGACACCGGCATGGGACGGCTTGGAGTGAAAGAC GAGGAAGAGACGAAACGAATCGTAGCGCTGATTGAGCGCCATCCGCATTTTGTGCTTGAA GGGTTGTACACGCATTTTGCGACTGCGGATGAGGTGAACACCGATTATTTTTCCTATCAG TATACCCGTTTTTTGCACATGCTCGAATGGCTGCCGTCGCGCCCGCCGCTCGTCCATTGC GCCAACAGCGCAGCGTCGCTCCGTTTCCCTGACCGGACGTTCAATATGGTCCGCTTCGGC ATTGCCATGTATGGGCTTGCCCCGTCGCCCGGCATCAAGCCGCTGCTGCCGTATCCATTA AAAGAAGCATTTTCGCTCCATAGCCGCCTCGTACACGTCAAAAAACTGCAACCAGGCGAA AAGGTGAGCTATGGTGCGACGTACACTGCGCAGACGGAGGAGTGGATCGGGACGATTCCG ATCGGCTATGCGGACGGCGTCCGCCGCCTGCAGCACTTTCATGTCCTTGTTGACGGACAA AAGGCGCCGATTGTCGGCCGCATTTGCATGGACCAGTGCATGATCCGCCTGCCTGGTCCG CTGCCGGTCGGCACGAAGGTGACACTGATTGGTCGCCAAGGGGACGAGGTAATTTCCATT GATGATGTCGCTCGCCATTTGGAAACGATCAACTACGAAGTGCCTTGCACGATCAGTTAT CGAGTGCCCCGTATTTTTTTCCGCCATAAGCGTATAATGGAAGTGAGAAACGCCATTGGC CGCGGGGAAAGCAGTGCATAA PF00842 Ala_racemase_C PF01168 Ala_racemase_N function vitamin binding function pyridoxal phosphate binding function isomerase activity function racemase and epimerase activity function binding function racemase and epimerase activity, acting on amino acids and derivatives function alanine racemase activity function catalytic activity process amino acid and derivative metabolism process physiological process process pyruvate family amino acid metabolism process metabolism process alanine metabolism process cellular metabolism process amino acid metabolism "
drug:{1-[(3-Hydroxy-Methyl-5-Phosphonooxy-Methyl-Pyridin-4-Ylmethyl)-Amino]-Ethyl}-Phosphonic Acidrdfs:label"{1-[(3-Hydroxy-Methyl-5-Phosphonooxy-Methyl-Pyridin-4-Ylmethyl)-Amino]-Ethyl}-Phosphonic Acid"
drug:{1-[(3-Hydroxy-Methyl-5-Phosphonooxy-Methyl-Pyridin-4-Ylmethyl)-Amino]-Ethyl}-Phosphonic Acidowl:sameAsdrug:EXPT01879
drug:{1-[(3-Hydroxy-Methyl-5-Phosphonooxy-Methyl-Pyridin-4-Ylmethyl)-Amino]-Ethyl}-Phosphonic Acidrdf:typedrugbank:drugs
drug:{1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTERdrugbank:description" experimental This compound belongs to the n-acyl-alpha amino acids and derivatives. These are compounds containing an alpha amino acid (or a derivative thereof) which bears an acyl group at his terminal nitrogen atom. N-acyl-alpha Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Alpha Amino Acid Amides Tertiary Carboxylic Acid Amides Sulfonyls Pyrrolidines Sulfonamides Tertiary Amines Carbamic Acids and Derivatives Polyamines Carboxylic Acids Ethers Enolates Aldehydes sulfonic acid derivative pyrrolidine sulfonamide sulfonyl tertiary carboxylic acid amide carboxamide group carbamic acid derivative tertiary amine carboxylic acid enolate polyamine ether organonitrogen compound amine aldehyde logP 1.11 ALOGPS logS -2.7 ALOGPS Water Solubility 8.26e-01 g/l ALOGPS logP 0.51 ChemAxon IUPAC Name tert-butyl N-[(2S)-1-[(2R,3S)-3-methanesulfonamido-2-[(2S)-1-oxobutan-2-yl]pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]carbamate ChemAxon Traditional IUPAC Name tert-butyl N-[(2S)-1-[(2R,3S)-3-methanesulfonamido-2-[(2S)-1-oxobutan-2-yl]pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]carbamate ChemAxon Molecular Weight 433.563 ChemAxon Monoisotopic Weight 433.224656557 ChemAxon SMILES [H][C@@](CC)(C=O)[C@@]1([H])N(CC[C@]1([H])NS(C)(=O)=O)C(=O)[C@@]([H])(NC(=O)OC(C)(C)C)C(C)C ChemAxon Molecular Formula C19H35N3O6S ChemAxon InChI InChI=1S/C19H35N3O6S/c1-8-13(11-23)16-14(21-29(7,26)27)9-10-22(16)17(24)15(12(2)3)20-18(25)28-19(4,5)6/h11-16,21H,8-10H2,1-7H3,(H,20,25)/t13-,14+,15+,16-/m1/s1 ChemAxon InChIKey InChIKey=NOWIRVOXJOWTSQ-FXUDXRNXSA-N ChemAxon Polar Surface Area (PSA) 121.88 ChemAxon Refractivity 108.25 ChemAxon Polarizability 46.01 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 10.36 ChemAxon pKa (strongest basic) -3.1 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 6323528 PubChem Substance 99445115 ChemSpider 4883464 PDB TRL BE0003935 Genome polyprotein HCV # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Genome polyprotein Involved in ATP binding NS5B is a RNA-dependent RNA polymerase that plays an essential role in the virus replication RNA-directed RNA polymerase:Host endoplasmic reticulum membrane 169-189 359-379 726-746 758-778 783-803 814-834 882-902 929-949 1658-1678 1806-1826 1829-1849 1851-1871 1882-1902 2991-3011 8.37 327142.8 HCV GenBank Gene Database M67463 GenBank Protein Database 329738 UniProtKB P27958 UniProt Accession POLG_HCVH Capsid protein C Core protein p19 Core protein p21 Envelope glycoprotein E1 Envelope glycoprotein E2 gp32 gp35 gp68 gp70 Hepacivirin Non-structural protein 4A Non-structural protein 4B Non-structural protein 5A NS1 NS3P NS4A NS4B NS5A NS5B p21 p23 p27 p56 p68 p7 p70 p8 Protease NS2-3 RNA-directed RNA polymerase Serine protease/NTPase/helicase NS3 >Genome polyprotein MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRG RRQPIPKARRPEGRTWAQPGYPWPLYGNEGCGWAGWLLSPRGSRPSWGPTDPRRRSRNLG KVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLA LLSCLTVPASAYQVRNSSGLYHVTNDCPNSSVVYEAADAILHTPGCVPCVREGNASRCWV AVTPTVATRDGKLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRHHWT TQDCNCSIYPGHITGHRMAWNMMMNWSPTAALVVAQLLRIPQAIMDMIAGAHWGVLAGIK YFSMVGNWAKVLVVLLLFAGVDAETHVTGGNAGRTTAGLVGLLTPGAKQNIQLINTNGSW HINSTALNCNESLNTGWLAGLFYQHKFNSSGCPERLASCRRLTDFAQGWGPISYANGSGL DERPYCWHYPPRPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGANDTDVFVLN NTRPPLGNWFGCTWMNSTGFTKVCGAPPCVIGGVGNNTLLCPTDCFRKYPEATYSRCGSG PRITPRCMVDYPYRLWHYPCTINYTIFKVRMYVGGVEHRLEAACNWTRGERCDLEDRDRS ELSPLLLSTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVV LLFLLLADARVCSCLWMMLLISQAEAALENLVILNAASLAGTHGLVSFLVFFCFAWYLKG RWVPGAVYALYGMWPLLLLLLALPQRAYALDTEVAASCGGVVLVGLMALTLSPYYKRYIS WCMWWLQYFLTRVEAQLHVWVPPLNVRGGRDAVILLTCVVHPALVFDITKLLLAIFGPLW ILQASLLKVPYFVRVQGLLRICALARKIAGGHYVQMAIIKLGALTGTCVYNHLAPLRDWA HNGLRDLAVAVEPVVFSRMETKLITWGADTAACGDIINGLPVSARRGQEILLGPADGMVS KGWRLLAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCINGVCWT VYHGAGTRTIASPKGPVIQTYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVI PVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTRGVAKAVDFIPVEN LETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAKGYKVLVLNPSVAA TLGFGAYMSKAHGVDPNIRTGVRTITTGSPITYSTYGKFLADAGCSGGAYDIIICDECHS TDATSISGIGTVLDQAETAGARLVVLATATPPGSVTVSHPNIEEVALSTTGEIPFYGKAI PLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVSTDAL MTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYR FVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLGFWEG VFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARAQAPPPSWDQMRKCLIRLKPTLHG PTPLLYRLGAVQNEVTLTHPITKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCV VIVGRIVLSGKPAIIPDREVLYQEFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTAS RHAEVITPAVQTNWQKLEVFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSP LTTGQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAALDSVGLGKVLVDILAGYGAGVA GALVAFKIMSGEVPSTEDLVNLLPAILSPGALAVGVVFASILRRRVGPGEGAVQWMNRLI AFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPCSGSWLRDI WDWICEVLSDFKTWLKAKLMPQLPGIPFVSCQRGYRGVWRGDGIMHTRCHCGAEITGHVK NGTMRIVGPRTCKNMWSGTFFINAYTTGPCTPLPAPNYKFALWRVSAEEYVEIRRVGDFH YVSGMTTDNLKCPCQIPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQL PCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSMASSSASQLSAPSLKATCTANHD SPDAELIEANLLWRQEMGGNITRVESENKVVILDSFDPLVAEEDEREVSVPAEILRKSRR FAPALPVWARPDYNPLLVETWKKPDYEPPVVHGCPLPPPRSPPVPPPRKKRTVVLTESTL PTALAELATKSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDVESYSSMPPLEGEPGDPDL SDGSWSTVSSGADTEDVVCCSMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYST TSRSACQRKKKVTFDRLQVLDSHYQDVLKEVKAAASKVKANLLSVEEACSLAPPHSAKSK FGYGAKDVRCHARKAVAHINSVWKDLLEDSVTPIDTTIMAKNEVFCVQPEKGGRKPARLI VFPDLGVRVCEKMALYDVVSKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGLSYD TRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCR ASRVLTTSCGNTLTRYIKARAACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFT EAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKRVYYLTRDPTTPLARAAWETA RHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALNCEIYGACYSIEPLDLP PIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRAWSVRARLLARGGKAAI CGKYLFNWAVRTKLKLTPITAAGRLDLSGWFTAGYSGGDIYHSVSHARPRWFWFCLLLLA AGVGIYLLPNR >9036 bp ATGAGCACGAATCCTAAACCTCAAAGAAAAACCAAACGTAACACCAACCGTCGCCCACAG GACGTCAAGTTCCCGGGTGGCGGTCAGATCGTTGGTGGAGTTTACTTGTTGCCGCGCAGG GGCCCTAGATTGGGTGTGCGCGCGACGAGGAAGACTTCCGAGCGGTCGCAACCTCGAGGT AGACGTCAGCCTATCCCCAAGGCACGTCGGCCCGAGGGCAGGACCTGGGCTCAGCCCGGG TACCCTTGGCCCCTCTATGGCAATGAGGGTTGCGGGTGGGCGGGATGGCTCCTGTCTCCC CGTGGCTCTCGGCCTAGCTGGGGCCCCACAGACCCCCGGCGTAGGTCGCGCAATTTGGGT AAGGTCATCGATACCCTTACGTGCGGCTTCGCCGACCTCATGGGGTACATACCGCTCGTC GGCGCCCCTCTTGGAGGCGCTGCCAGGGCCCTGGCGCATGGCGTCCGGGTTCTGGAAGAC GGCGTGAACTATGCAACAGGGAACCTTCCTGGTTGCTCTTTCTCTATCTTCCTTCTGGCC CTGCTCTCTTGCCTGACTGTGCCCGCTTCAGCCTACCAAGTGCGCAATTCCTCGGGGCTT TACCATGTCACCAATGATTGCCCTAACTCGAGTGTTGTGTACGAGGCGGCCGATGCCATC CTGCACACTCCGGGGTGTGTCCCTTGCGTTCGCGAGGGTAACGCCTCGAGGTGTTGGGTG GCGGTGACCCCCACGGTGGCCACCAGGGACGGCAAACTCCCCACAACGCAGCTTCGACGT CATATCGATCTGCTTGTCGGGAGCGCCACCCTCTGCTCGGCCCTCTACGTGGGGGACCTG TGCGGGTCTGTCTTTCTTGTTGGTCAACTGTTTACCTTCTCTCCCAGGCACCACTGGACG ACGCAAGACTGCAATTGTTCTATCTATCCCGGCCATATAACGGGTCATCGCATGGCATGG AATATGATGATGAACTGGTCCCCTACGGCAGCGTTGGTGGTAGCTCAGCTGCTCCGAATC CCACAAGCCATCATGGACATGATCGCTGGCGCCCACTGGGGAGTCCTGGCGGGCATAAAG TATTTCTCCATGGTGGGGAACTGGGCGAAGGTCCTGGTAGTGCTGCTGCTATTTGCCGGC GTCGACGCGGAAACCCACGTCACCGGGGGAAATGCCGGCCGCACCACGGCTGGGCTTGTT GGTCTCCTTACACCAGGCGCCAAGCAGAACATCCAACTGATCAACACCAACGGCAGTTGG CACATCAATAGCACGGCCTTGAACTGCAATGAAAGCCTTAACACCGGCTGGTTAGCAGGG CTCTTCTATCAGCACAAATTCAACTCTTCAGGCTGTCCTGAGAGGTTGGCCAGCTGCCGA CGCCTTACCGATTTTGCCCAGGGCTGGGGTCCTATCAGTTATGCCAACGGAAGCGGCCTC GACGAACGCCCCTACTGCTGGCACTACCCTCCAAGACCTTGTGGCATTGTGCCCGCAAAG AGCGTGTGTGGCCCGGTATATTGCTTCACTCCCAGCCCCGTGGTGGTGGGAACGACCGAC AGGTCGGGCGCGCCTACCTACAGCTGGGGTGCAAATGATACGGATGTCTTCGTCCTTAAC AACACCAGGCCACCGCTGGGCAATTGGTTCGGTTGTACCTGGATGAACTCAACTGGATTC ACCAAAGTGTGCGGAGCGCCCCCTTGTGTCATCGGAGGGGTGGGCAACAACACCTTGCTC TGCCCCACTGATTGCTTCCGCAAATATCCGGAAGCCACATACTCTCGGTGCGGCTCCGGT CCCAGGATTACACCCAGGTGCATGGTCGACTACCCGTATAGGCTTTGGCACTATCCTTGT ACCATCAATTACACCATATTCAAAGTCAGGATGTACGTGGGAGGGGTCGAGCACAGGCTG GAAGCGGCCTGCAACTGGACGCGGGGCGAACGCTGTGATCTGGAAGACAGGGACAGGTCC GAGCTCAGCCCGTTGCTGCTGTCCACCACACAGTGGCAGGTCCTTCCGTGTTCTTTCACG ACCCTGCCAGCCTTGTCCACCGGCCTCATCCACCTCCACCAGAACATTGTGGACGTGCAG TACTTGTACGGGGTAGGGTCAAGCATCGCGTCCTGGGCCATTAAGTGGGAGTACGTCGTT CTCCTGTTCCTTCTGCTTGCAGACGCGCGCGTCTGTTCCTGCTTGTGGATGATGTTACTC ATATCCCAAGCGGAGGCGGCTTTGGAGAACCTCGTAATACTCAATGCAGCATCCCTGGCC GGGACGCATGGTCTTGTGTCCTTCCTCGTGTTCTTCTGCTTTGCGTGGTATCTGAAGGGT AGGTGGGTGCCCGGAGCGGTCTACGCCCTCTACGGGATGTGGCCTCTCCTCCTGCTCCTG CTGGCGTTGCCTCAGCGGGCATACGCACTGGACACGGAGGTGGCCGCGTCGTGTGGCGGC GTTGTTCTTGTCGGGTTAATGGCGCTGACTCTGTCGCCATATTACAAGCGCTATATCAGC TGGTGCATGTGGTGGCTTCAGTATTTTCTGACCAGAGTAGAAGCGCAACTGCACGTGTGG GTTCCCCCCCTCAACGTCCGGGGGGGGCGCGATGCCGTCATCTTACTCACGTGTGTAGTA CACCCGGCCCTGGTATTTGACATCACCAAACTACTCCTGGCCATCTTCGGACCCCTTTGG ATTCTTCAAGCCAGTTTGCTTAAAGTCCCCTACTTCGTGCGCGTTCAAGGCCTTCTCCGG ATCTGCGCGCTAGCGCGGAAGATAGCCGGAGGTCATTACGTGCAAATGGCCATCATCAAG TTAGGGGCGCTTACTGGCACCTGTGTGTATAACCATCTCGCTCCTCTTCGAGACTGGGCG CACAACGGCCTGCGAGATCTGGCCGTGGCTGTGGAACCAGTCGTCTTCTCCCGAATGGAG ACCAAGCTCATCACGTGGGGGGCAGATACCGCCGCGTGCGGTGACATCATCAACGGCTTG CCCGTCTCTGCCCGTAGGGGCCAGGAGATACTGCTTGGGCCAGCCGACGGAATGGTCTCC AAGGGGTGGAGGTTGCTGGCGCCCATCACGGCGTACGCCCAGCAGACGAGAGGCCTCCTA GGGTGTATAATCACCAGCCTGACTGGCCGGGACAAAAACCAAGTGGAGGGTGAGGTCCAG ATCGTGTCAACTGCTACCCAGACCTTCCTGGCAACGTGCATCAATGGGGTATGCTGGACT GTCTACCACGGGGCCGGAACGAGGACCATCGCATCACCCAAGGGTCCTGTCATCCAGACG TATACCAATGTGGATCAAGACCTCGTGGGCTGGCCCGCTCCTCAAGGTTCCCGCTCATTG ACACCCTGCACCTGCGGCTCCTCGGACCTTTACCTGGTCACGAGGCACGCCGATGTCATT CCCGTGCGCCGGCGAGGTGATAGCAGGGGTAGCCTGCTTTCGCCCCGGCCCATTTCCTAC TTGAAAGGCTCCTCGGGGGGTCCGCTGTTGTGCCCCACGGGACACGCCGTGGGCCTATTC AGGGCCGCGGTGTGCACCCGTGGAGTGGCTAAGGCGGTGGACTTTATCCCTGTGGAGAAC CTAGAGACAACCATGAGATCCCCGGTGTTCACGGACAACTCCTCTCCACCAGCAGTGCCC CAGAGCTTCCAGGTGGCCCACCTGCATGCTCCCACCGGCAGCGGTAAGAGCACCAAGGTC CCGGCTGCGTACGCAGCCAAGGGCTACAAGGTGTTGGTGCTCAACCCCTCTGTTGCTGCA ACACTGGGCTTTGGTGCTTACATGTCCAAGGCCCATGGGGTTGATCCTAATATCAGGACC GGGGTGAGAACAATTACCACTGGCAGCCCCATCACGTACTCCACCTACGGCAAGTTCCTT GCCGACGCCGGGTGCTCAGGAGGTGCTTATGACATAATAATTTGTGACGAGTGCCACTCC ACGGATGCCACATCCATCTCGGGCATCGGCACTGTCCTTGACCAAGCAGAGACTGCGGGG GCGAGACTGGTTGTGCTCGCCACTGCTACCCCTCCGGGCTCCGTCACTGTGTCCCATCCT AACATCGAGGAGGTTGCTCTGTCCACCACCGGAGAGATCCCCTTTTACGGCAAGGCTATC CCCCTCGAGGTGATCAAGGGGGGAAGACATCTCATCTTCTGCCACTCAAAGAAGAAGTGC GACGAGCTCGCCGCGAAGCTGGTCGCATTGGGCATCAATGCCGTGGCCTACTACCGCGGT CTTGACGTGTCTGTCATCCCGACCAGCGGCGATGTTGTCGTCGTGTCGACCGATGCTCTC ATGACTGGCTTTACCGGCGACTTCGACTCTGTGATAGACTGCAACACGTGTGTCACTCAG ACAGTCGATTTTAGCCTTGACCCTACCTTTACCATTGAGACAACCACGCTCCCCCAGGAT GCTGTCTCCAGGACTCAACGCCGGGGCAGGACTGGCAGGGGGAAGCCAGGCATCTATAGA TTTGTGGCACCGGGGGAGCGCCCCTCCGGCATGTTCGACTCGTCCGTCCTCTGTGAGTGC TATGACGCGGGCTGTGCTTGGTATGAGCTCACGCCCGCCGAGACTACAGTTAGGCTACGA GCGTACATGAACACCCCGGGGCTTCCCGTGTGCCAGGACCATCTTGGATTTTGGGAGGGC GTCTTTACGGGCCTCACTCATATAGATGCCCACTTTCTATCCCAGACAAAGCAGAGTGGG GAGAACTTTCCTTACCTGGTAGCGTACCAAGCCACCGTGTGCGCTAGGGCTCAAGCCCCT CCCCCATCGTGGGACCAGATGCGGAAGTGTTTGATCCGCCTTAAACCCACCCTCCATGGG CCAACACCCCTGCTATACAGACTGGGCGCTGTTCAGAATGAAGTCACCCTGACGCACCCA ATCACCAAATACATCATGACATGCATGTCGGCCGACCTGGAGGTCGTCACGAGCACCTGG GTGCTCGTTGGCGGCGTCCTGGCTGCTCTGGCCGCGTATTGCCTGTCAACAGGCTGCGTG GTCATAGTGGGCAGGATCGTCTTGTCCGGGAAGCCGGCAATTATACCTGACAGGGAGGTT CTCTACCAGGAGTTCGATGAGATGGAAGAGTGCTCTCAGCACTTACCGTACATCGAGCAA GGGATGATGCTCGCTGAGCAGTTCAAGCAGAAGGCCCTCGGCCTCCTGCAGACCGCGTCC CGCCATGCAGAGGTTATCACCCCTGCTGTCCAGACCAACTGGCAGAAACTCGAGGTCTTT TGGGCGAAGCACATGTGGAATTTCATCAGTGGGATACAATACTTGGCGGGCCTGTCAACG CTGCCTGGTAACCCCGCCATTGCTTCATTGATGGCTTTTACAGCTGCCGTCACCAGCCCA CTAACCACTGGCCAAACCCTCCTCTTCAACATATTGGGGGGGTGGGTGGCTGCCCAGCTC GCCGCCCCCGGTGCCGCTACCGCCTTTGTGGGCGCTGGCTTAGCTGGCGCCGCACTCGAC AGCGTTGGACTGGGGAAGGTCCTCGTGGACATTCTTGCAGGCTATGGCGCGGGCGTGGCG GGAGCTCTTGTGGCATTCAAGATCATGAGCGGTGAGGTCCCCTCCACGGAGGACCTGGTC AATCTGCTGCCCGCCATCCTCTCACCTGGAGCCCTTGCAGTCGGTGTGGTCTTTGCATCA ATACTGCGCCGGCGTGTTGGCCCGGGCGAGGGGGCAGTGCAATGGATGAACCGGCTAATA GCCTTCGCCTCCCGGGGGAACCATGTTTCCCCCACACACTACGTGCCGGAGAGCGATGCA GCCGCCCGCGTCACTGCCATACTCAGCAGCCTCACTGTAACCCAGCTCCTGAGGCGACTG CATCAGTGGATAAGCTCGGAGTGTACCACTCCATGCTCCGGTTCCTGGCTAAGGGACATC TGGGACTGGATATGCGAGGTGCTGAGCGACTTTAAGACCTGGCTGAAAGCCAAGCTCATG CCACAACTGCCTGGGATTCCCTTTGTGTCCTGCCAGCGCGGGTATAGGGGGGTCTGGCGA GGAGACGGCATTATGCACACTCGCTGCCACTGTGGAGCTGAGATCACTGGACATGTCAAA AACGGGACGATGAGGATCGTCGGTCCTAGGACCTGCAAGAACATGTGGAGTGGGACGTTC TTCATTAATGCCTACACCACGGGCCCCTGTACTCCCCTTCCTGCGCCGAACTATAAGTTC GCGCTGTGGAGGGTGTCTGCAGAGGAATACGTGGAGATAAGGCGGGTGGGGGACTTCCAC TACGTATCGGGCATGACTACTGACAATCTCAAATGCCCGTGCCAGATCCCATCGCCCGAA TTTTTCACAGAATTGGACGGGGTGCGCCTACATAGGTTTGCGCCCCCTTGCAAGCCCTTG CTGCGGGAGGAGGTATCATTCAGAGTAGGACTCCACGAGTACCCGGTGGGGTCGCAATTA CCTTGCGAGCCCGAACCGGACGTAGCCGTGTTGACGTCCATGCTCACTGATCCCTCCCAT ATAACAGCAGAGGCGGCCGGGAGAAGGTTGGCGAGAGGGTCACCCCCTTCTATGGCCAGC TCCTCGGCTAGCCAGCTGTCCGCTCCATCTCTCAAGGCAACTTGCACCGCCAACCATGAC TCCCCTGACGCCGAGCTCATAGAGGCTAACCTCCTGTGGAGGCAGGAGATGGGCGGCAAC ATCACCAGGGTTGAGTCAGAGAACAAAGTGGTGATTCTGGACTCCTTCGATCCGCTTGTG GCAGAGGAGGATGAGCGGGAGGTCTCCGTACCCGCAGAAATTCTGCGGAAGTCTCGGAGA TTCGCCCCAGCCCTGCCCGTCTGGGCGCGGCCGGACTACAACCCCCTGCTAGTAGAGACG TGGAAAAAGCCTGACTACGAACCACCTGTGGTCCATGGCTGCCCGCTACCACCTCCACGG TCCCCTCCTGTGCCTCCGCCTCGGAAAAAGCGTACGGTGGTCCTCACCGAATCAACCCTA CCTACTGCCTTGGCCGAGCTTGCCACCAAAAGTTTTGGCAGCTCCTCAACTTCCGGCATT ACGGGCGACAATACGACAACATCCTCTGAGCCCGCCCCTTCTGGCTGCCCCCCCGACTCC GACGTTGAGTCCTATTCTTCCATGCCCCCCCTGGAGGGGGAGCCTGGGGATCCGGATCTC AGCGACGGGTCATGGTCGACGGTCAGTAGTGGGGCCGACACGGAAGATGTCGTGTGCTGC TCAATGTCTTATTCCTGGACAGGCGCACTCGTCACCCCGTGCGCTGCGGAGGAACAAAAA CTGCCCATCAACGCACTGAGCAACTCGTTGCTACGCCATCACAATCTGGTGTATTCCACC ACTTCACGCAGTGCTTGCCAAAGGAAGAAGAAAGTCACATTTGACAGACTGCAAGTTCTG GACAGCCATTACCAGGACGTGCTCAAGGAGGTCAAAGCAGCGGCGTCAAAAGTGAAGGCT AACTTGCTATCCGTAGAGGAAGCTTGCAGCCTGGCGCCCCCACATTCAGCCAAATCCAAG TTTGGCTATGGGGCAAAAGACGTCCGTTGCCATGCCAGAAAGGCCGTAGCCCACATCAAC TCCGTGTGGAAAGACCTTCTGGAAGACAGTGTAACACCAATAGACACTACCATCATGGCC AAGAACGAGGTTTTCTGCGTTCAGCCTGAGAAGGGGGGTCGTAAGCCAGCTCGTCTCATC GTGTTCCCCGACCTGGGCGTGCGCGTGTGCGAGAAGATGGCCCTGTACGACGTGGTTAGC AAGCTCCCCTTGGCCGTGATGGGAAGCTCCTACGGATTCCAATACTCACCAGGACAGCGG GTTGAATTCCTCGTGCAAGCGTGGAAGTCCAAGAAGACCCCGATGGGGCTCTCGTATGAT ACCCGCTGTTTTGACTCCACAGTCACTGAGAGCGACATCCGTACGGAGGAGGCAATTTAC CAATGTTGTGACCTGGACCCCCAAGCCCGCGTGGCCATCAAGTCCCTCACTGAGAGGCTT TATGTTGGGGGCCCTCTTACTAATTCAAGGGGGGAAAACTGCGGCTACCGCAGGTGCCGC GCGAGCAGAGTACTGACAACTAGCTGTGGTAACACCCTCACTCGCTACATCAAGGCCCGG GCAGCCTGTCGAGCCGCAGGGCTCCAGGACTGCACCATGCTCGTGTGTGGCGACGACTTA GTCGTTATCTGTGAAAGTGCGGGGGTCCAGGAGGACGCGGCGAGCCTGAGAGCCTTCACG GAGGCTATGACCAGGTACTCCGCCCCCCCCGGGGACCCCCCACAACCAGAATACGACTTG GAGCTTATAACATCATGCTCCTCCAACGTGTCAGTCGCCCACGACGGCGCTGGAAAGAGG GTCTACTACCTTACCCGTGACCCTACAACCCCCCTCGCGAGAGCCGCGTGGGAGACAGCA AGACACACTCCAGTCAATTCCTGGCTAGGCAACATAATCATGTTTGCCCCCACACTGTGG GCGAGGATGATACTGATGACCCACTTCTTTAGCGTCCTCATAGCCAGGGATCAGCTTGAA CAGGCTCTCAACTGCGAGATCTACGGAGCCTGCTACTCCATAGAACCACTGGATCTACCT CCAATCATTCAAAGACTCCATGGCCTCAGCGCATTTTCACTCCACAGTTACTCTCCAGGT GAAATTAATAGGGTGGCCGCATGCCTCAGAAAACTTGGGGTCCCGCCCTTGCGAGCTTGG AGACACCGGGCCTGGAGCGTCCGCGCTAGGCTTCTGGCCAGAGGAGGCAAGGCTGCCATA TGTGGCAAGTACCTCTTCAACTGGGCAGTAAGAACAAAGCTCAAACTCACTCCGATAACG GCCGCTGGCCGGCTGGACTTGTCCGGCTGGTTCACGGCTGGCTACAGCGGGGGAGACATT TATCACAGCGTGTCTCATGCCCGGCCCCGCTGGTTCTGGTTTTGCCTACTCCTGCTTGCT GCAGGGGTAGGCATCTACCTCCTCCCCAACCGATGA PF01543 HCV_capsid PF01542 HCV_core PF01539 HCV_env PF01560 HCV_NS1 PF01538 HCV_NS2 PF01006 HCV_NS4a PF01001 HCV_NS4b PF01506 HCV_NS5a PF08300 HCV_NS5a_1a PF08301 HCV_NS5a_1b PF02907 Peptidase_S29 PF00998 RdRP_3 component virion component viral envelope component viral capsid function nucleotide binding function purine nucleotide binding function peptidase activity function helicase activity function adenyl nucleotide binding function transferase activity function nucleotidyltransferase activity function binding function ATP binding function transferase activity, transferring phosphorus-containing groups function serine-type peptidase activity function catalytic activity function nucleic acid binding function RNA-directed RNA polymerase activity function RNA binding function structural molecule activity function hydrolase activity process macromolecule metabolism process protein metabolism process cellular protein metabolism process proteolysis process interaction between organisms process interspecies interaction between organisms process transcription process physiological process process symbiosis, encompassing mutualism through parasitism process interaction with host process metabolism process virus-host interaction process viral life cycle process cellular metabolism process transformation of host cell by virus process viral infectious cycle process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process viral genome replication "
drug:{1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTERrdfs:label"{1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTER"
drug:{1-[2-(1-FORMYL-PROPYL)-3-METHANESULFONYLAMINO-PYRROLIDINE-1-CARBONYL]-2-METHYL-PROPYL}-CARBAMIC ACID TERT-BUTYL ESTERrdf:typedrugbank:drugs
drug:{3-[(3-Hydroxy-2-Methyl-5-Phosphonooxymethyl-Pyridin-4-Ylmethyl)-Amino]-2-Methyl-Propyl}-Phosphonic Aciddrugbank:description" experimental This compound belongs to the phosphoethanolamines. These are compounds containing a phosphate linked to the second carbon of an ethanolamine. Phosphoethanolamines Organic Compounds Organophosphorus Compounds Organic Phosphoric Acids and Derivatives Organophosphate Esters Pyridines and Derivatives Organic Phosphoric Acids Polyamines Dialkylamines organic phosphate pyridine secondary aliphatic amine polyamine secondary amine amine organonitrogen compound logP -0.58 ALOGPS logS -2.2 ALOGPS Water Solubility 2.62e+00 g/l ALOGPS logP -4.1 ChemAxon IUPAC Name {[(2R)-1-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]propan-2-yl]oxy}phosphonic acid ChemAxon Traditional IUPAC Name [(2R)-1-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]propan-2-yl]oxyphosphonic acid ChemAxon Molecular Weight 386.232 ChemAxon Monoisotopic Weight 386.064403272 ChemAxon SMILES C[C@H](CNCC1=C(O)C(C)=NC=C1COP(O)(O)=O)OP(O)(O)=O ChemAxon Molecular Formula C11H20N2O9P2 ChemAxon InChI InChI=1S/C11H20N2O9P2/c1-7(22-24(18,19)20)3-12-5-10-9(6-21-23(15,16)17)4-13-8(2)11(10)14/h4,7,12,14H,3,5-6H2,1-2H3,(H2,15,16,17)(H2,18,19,20)/t7-/m1/s1 ChemAxon InChIKey InChIKey=JMZWWHLIKAYMPJ-SSDOTTSWSA-N ChemAxon Polar Surface Area (PSA) 178.67 ChemAxon Refractivity 82.99 ChemAxon Polarizability 33.56 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 9 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) 1.3 ChemAxon pKa (strongest basic) 9.81 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon PubChem Compound 5496700 PubChem Substance 46508946 PDB 33P BE0001652 Threonine-phosphate decarboxylase Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Threonine-phosphate decarboxylase Amino acid transport and metabolism Decarboxylates L-threonine-O-3-phosphate to yield (R)-1- amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin cobD None 6.92 40766.0 Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GenBank Gene Database U90625 GenBank Protein Database 1895094 UniProtKB P97084 UniProt Accession COBD_SALTY EC 4.1.1.81 L-threonine-O-3- phosphate decarboxylase >Threonine-phosphate decarboxylase MALFNSAHGGNIREAATVLGISPDQLLDFSANINPLGMPVSVKRALIDNLDCIERYPDAD YFHLHQALARHHQVPASWILAGNGETESIFTVASGLKPRRAMIVTPGFAEYGRALAQSGC EIRRWSLREADGWQLTDAILEALTPDLDCLFLCTPNNPTGLLPERPLLQAIADRCKSLNI NLILDEAFIDFIPHETGFIPALKDNPHIWVLRSLTKFYAIPGLRLGYLVNSDDAAMARMR RQQMPWSVNALAALAGEVALQDSAWQQATWHWLREEGARFYQALCQLPLLTVYPGRANYL LLRCEREDIDLQRRLLTQRILIRSCANYPGLDSRYYRVAIRSAAQNERLLAALRNVLTGI APAD >1095 bp ATGGCTTTATTCAACACCGCGCATGGCGGTAATATTCGGGAACCCGCAACGGTGTTGGGC ATCTCCCCTGACCATTTACTGGATTTTACCGCAAACATTAATCCGCTGGGTATGCCTGTC AGCTTGAAACCCCCCCTTATCGACAATCTGGACTGCATTGAGCGCTACCCGGACGCCGAT TATTTTCATTTGCACCAGGCGCTGGCGCGTCATCATCAGGTGCCGGCATCGTGGATACTG GCGGGAAATGGCGAGACGGAGTCAATCTTTACCGTGGCGAGCGGTCTTAAACCGCGTCGT GCAATGATTGTCACGCCAGGTTTCGCGGAGTATGGCCGGGCGCTGGCGCAAAGTGGCTGT GAAATTCGTCGCTGGTCTCTACGCGAAGCGGATGGCTGGCAGCTTACCGATGCCATTCTT GAGGCGTTGACGCCCGATCTGGACTGCCTGTTTCTGTGTACGCCTAATAATCCTACCGGC CTGCTGCCGGAGCGGCCGTTATTACAGGCCATTGCCGATCGCTGCAAATCGCTGAACATT AACCTGATCCTGGATGAAGCGTTTATCGATTTTATTCCGCATGAGACGGGCTTTATTCCT GCTCTTAAAGATAATCCGCATATCTGGGTGCTGCGTTCGCTGACCAAATTTTATGCCATT CCCGGCCTGCGGTTGGGATATCTCGTCAATAGCGATGACGCGGCGATGGCGCGGATGCGT CGCCAACAAATGCCGTGGTCGGTTAACGCGCTGGCGGCGCTTGCCGGTGAGGTAGCGTTA CAGGATAGCGCCTGGCAACAGGCGACCTGGCATTGGTTACGGGAGGAGGGCGCCCGGTTT TATCAGGCGCTTTGTCAGCTCCCCCTGCTGACGGTTTATCCCGGGCGGGCAAACTATCTG TTGTTACGCTGTGAGCGAGAGGATATTGATCTGCAGCGACGGTTGCTGACGCAGCGGATT TTAATCCGTAGCTGCGCTAACTACCCGGGGCTGGACAGCCGCTATTATCGTGTGGCGATA CGCAGCGCTGCGCAAAACGAGCGTCTGCTGGCGGCGCTGCGCAATGTGCTTACCGGTATA GCCCCTGCTGATTGA PF00155 Aminotran_1_2 function transferase activity function transferase activity, transferring nitrogenous groups function catalytic activity process metabolism process cellular metabolism process biosynthesis process heterocycle metabolism process porphyrin metabolism process porphyrin biosynthesis process cobalamin biosynthesis process physiological process "
drug:{3-[(3-Hydroxy-2-Methyl-5-Phosphonooxymethyl-Pyridin-4-Ylmethyl)-Amino]-2-Methyl-Propyl}-Phosphonic Acidrdfs:label"{3-[(3-Hydroxy-2-Methyl-5-Phosphonooxymethyl-Pyridin-4-Ylmethyl)-Amino]-2-Methyl-Propyl}-Phosphonic Acid"
drug:{3-[(3-Hydroxy-2-Methyl-5-Phosphonooxymethyl-Pyridin-4-Ylmethyl)-Amino]-2-Methyl-Propyl}-Phosphonic Acidowl:sameAsdrug:EXPT00153
drug:{3-[(3-Hydroxy-2-Methyl-5-Phosphonooxymethyl-Pyridin-4-Ylmethyl)-Amino]-2-Methyl-Propyl}-Phosphonic Acidrdf:typedrugbank:drugs
drug:{3-[(4,5,7-TRIFLUORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-1H-INDOL-1-YL}ACETIC ACIDdrugbank:description" experimental This compound belongs to the indolyl carboxylic acids and derivatives. These are compounds containing a carboxylic acid chain (of at least 2 carbon atoms) linked to an indole ring. Indolyl Carboxylic Acids and Derivatives Organic Compounds Heterocyclic Compounds Indoles and Derivatives Indolyl Carboxylic Acids and Derivatives Indoles Benzothiazoles Fluorobenzenes Aryl Fluorides N-substituted Pyrroles Thiazoles Enolates Polyamines Carboxylic Acids Organofluorides indole 1,3-benzothiazole fluorobenzene substituted pyrrole benzene aryl halide n-substituted pyrrole aryl fluoride pyrrole azole thiazole polyamine carboxylic acid derivative enolate carboxylic acid organofluoride amine organohalogen organonitrogen compound logP 3.94 ALOGPS logS -4.5 ALOGPS Water Solubility 1.10e-02 g/l ALOGPS logP 4.3 ChemAxon IUPAC Name 2-{3-[(4,5,7-trifluoro-1,3-benzothiazol-2-yl)methyl]-1H-indol-1-yl}acetic acid ChemAxon Traditional IUPAC Name {3-[(4,5,7-trifluoro-1,3-benzothiazol-2-yl)methyl]indol-1-yl}acetic acid ChemAxon Molecular Weight 376.352 ChemAxon Monoisotopic Weight 376.049332911 ChemAxon SMILES OC(=O)CN1C=C(CC2=NC3=C(S2)C(F)=CC(F)=C3F)C2=C1C=CC=C2 ChemAxon Molecular Formula C18H11F3N2O2S ChemAxon InChI InChI=1S/C18H11F3N2O2S/c19-11-6-12(20)18-17(16(11)21)22-14(26-18)5-9-7-23(8-15(24)25)13-4-2-1-3-10(9)13/h1-4,6-7H,5,8H2,(H,24,25) ChemAxon InChIKey InChIKey=KYHVTMFADJNSGS-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 55.12 ChemAxon Refractivity 89.01 ChemAxon Polarizability 33.81 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 4.22 ChemAxon pKa (strongest basic) 1.45 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 157839 PubChem Substance 99443534 ChemSpider 138877 PDB 3NA BE0000747 Aldose reductase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aldose reductase Involved in oxidoreductase activity Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies AKR1B1 7q35 Cytoplasm None 6.99 35723.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:381 GenAtlas AKR1B1 GeneCards AKR1B1 GenBank Gene Database J04795 GenBank Protein Database 178487 UniProtKB P15121 UniProt Accession ALDR_HUMAN Aldehyde reductase AR EC 1.1.1.21 >Aldose reductase ASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQE KLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKE FFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPA VNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKH NKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCAL LSCTSHKDYPFHEEF >951 bp ATGGCAAGCCGTCTCCTGCTCAACAACGGCGCCAAGATGCCCATCCTGGGGTTGGGTACC TGGAAGTCCCCTCCAGGGCAGGTGACTGAGGCCGTGAAGGTGGCCATTGACGTCGGGTAC CGCCACATCGACTGTGCCCATGTGTACCAGAATGAGAATGAGGTGGGGGTGGCCATTCAG GAGAAGCTCAGGGAGCAGGTGGTGAAGCGTGAGGAGCTCTTCATCGTCAGCAAGCTGTGG TGCACGTACCATGAGAAGGGCCTGGTGAAAGGAGCCTGCCAGAAGACACTCAGCGACCTG AAGCTGGACTACCTGGACCTCTACCTTATTCACTGGCCGACTGGCTTTAAGCCTGGGAAG GAATTTTTCCCATTGGATGAGTCGGGCAATGTGGTTCCCAGTGACACCAACATTCTGGAC ACGTGGGCGGCCATGGAAGAGCTGGTGGATGAAGGGCTGGTGAAAGCTATTGGCATCTCC AACTTCAACCATCTCCAGGTGGAGATGATCTTAAACAAACCTGGCTTGAAGTATAAGCCT GCAGTTAACCAGATTGAGTGCCACCCATATCTCACTCAGGAGAAGTTAATCCAGTACTGC CAGTCCAAAGGCATCGTGGTGACCGCCTACAGCCCCCTCGGCTCTCCTGACAGGCCCTGG GCCAAGCCCGAGGACCCTTCTCTCCTGGAGGATCCCAGGATCAAGGCGATCGCAGCCAAG CACAATAAAACTACAGCCCAGGTCCTGATCCGGTTCCCCATGCAGAGGAACTTGGTGGTG ATCCCCAAGTCTGTGACACCAGAACGCATTGCTGAGAACTTTAAGGTCTTTGACTTTGAA CTGAGCAGCCAGGATATGACCACCTTACTCAGCTACAACAGGAACTGGAGGGTCTGTGCC TTGTTGAGCTGTACCTCCCACAAGGATTACCCCTTCCATGAAGAGTTTTGA PF00248 Aldo_ket_red function oxidoreductase activity function catalytic activity "
drug:{3-[(4,5,7-TRIFLUORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-1H-INDOL-1-YL}ACETIC ACIDrdfs:label"{3-[(4,5,7-TRIFLUORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-1H-INDOL-1-YL}ACETIC ACID"
drug:{3-[(4,5,7-TRIFLUORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-1H-INDOL-1-YL}ACETIC ACIDrdf:typedrugbank:drugs
drug:{3-[(5-CHLORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL}ACETIC ACIDdrugbank:description" experimental This compound belongs to the benzothiazoles. These are organic compounds containing a benzene fused to a thiazole ring (a five-member ring with four carbon atoms, one nitrogen atom and one sulfur atom). Benzothiazoles Organic Compounds Heterocyclic Compounds Benzothiazoles Chlorobenzenes Pyrimidones Aryl Chlorides Hydropyrimidines Thiazoles Polyamines Enolates Carboxylic Acids Organochlorides chlorobenzene pyrimidone aryl chloride aryl halide benzene hydropyrimidine pyrimidine thiazole azole polyamine enolate carboxylic acid derivative carboxylic acid organohalogen amine organochloride organonitrogen compound logP 1.98 ALOGPS logS -4.5 ALOGPS Water Solubility 1.18e-02 g/l ALOGPS logP 1.43 ChemAxon IUPAC Name 2-{3-[(5-chloro-1,3-benzothiazol-2-yl)methyl]-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-1-yl}acetic acid ChemAxon Traditional IUPAC Name {3-[(5-chloro-1,3-benzothiazol-2-yl)methyl]-2,4-dioxopyrimidin-1-yl}acetic acid ChemAxon Molecular Weight 351.765 ChemAxon Monoisotopic Weight 351.00805422 ChemAxon SMILES OC(=O)CN1C=CC(=O)N(CC2=NC3=CC(Cl)=CC=C3S2)C1=O ChemAxon Molecular Formula C14H10ClN3O4S ChemAxon InChI InChI=1S/C14H10ClN3O4S/c15-8-1-2-10-9(5-8)16-11(23-10)6-18-12(19)3-4-17(14(18)22)7-13(20)21/h1-5H,6-7H2,(H,20,21) ChemAxon InChIKey InChIKey=RQWICELTTDJODO-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 90.81 ChemAxon Refractivity 81.66 ChemAxon Polarizability 32.58 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 3.74 ChemAxon pKa (strongest basic) 2.3 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 10450624 PubChem Substance 99443564 ChemSpider 8626041 PDB 47D BE0000747 Aldose reductase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aldose reductase Involved in oxidoreductase activity Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies AKR1B1 7q35 Cytoplasm None 6.99 35723.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:381 GenAtlas AKR1B1 GeneCards AKR1B1 GenBank Gene Database J04795 GenBank Protein Database 178487 UniProtKB P15121 UniProt Accession ALDR_HUMAN Aldehyde reductase AR EC 1.1.1.21 >Aldose reductase ASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQE KLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKE FFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPA VNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKH NKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCAL LSCTSHKDYPFHEEF >951 bp ATGGCAAGCCGTCTCCTGCTCAACAACGGCGCCAAGATGCCCATCCTGGGGTTGGGTACC TGGAAGTCCCCTCCAGGGCAGGTGACTGAGGCCGTGAAGGTGGCCATTGACGTCGGGTAC CGCCACATCGACTGTGCCCATGTGTACCAGAATGAGAATGAGGTGGGGGTGGCCATTCAG GAGAAGCTCAGGGAGCAGGTGGTGAAGCGTGAGGAGCTCTTCATCGTCAGCAAGCTGTGG TGCACGTACCATGAGAAGGGCCTGGTGAAAGGAGCCTGCCAGAAGACACTCAGCGACCTG AAGCTGGACTACCTGGACCTCTACCTTATTCACTGGCCGACTGGCTTTAAGCCTGGGAAG GAATTTTTCCCATTGGATGAGTCGGGCAATGTGGTTCCCAGTGACACCAACATTCTGGAC ACGTGGGCGGCCATGGAAGAGCTGGTGGATGAAGGGCTGGTGAAAGCTATTGGCATCTCC AACTTCAACCATCTCCAGGTGGAGATGATCTTAAACAAACCTGGCTTGAAGTATAAGCCT GCAGTTAACCAGATTGAGTGCCACCCATATCTCACTCAGGAGAAGTTAATCCAGTACTGC CAGTCCAAAGGCATCGTGGTGACCGCCTACAGCCCCCTCGGCTCTCCTGACAGGCCCTGG GCCAAGCCCGAGGACCCTTCTCTCCTGGAGGATCCCAGGATCAAGGCGATCGCAGCCAAG CACAATAAAACTACAGCCCAGGTCCTGATCCGGTTCCCCATGCAGAGGAACTTGGTGGTG ATCCCCAAGTCTGTGACACCAGAACGCATTGCTGAGAACTTTAAGGTCTTTGACTTTGAA CTGAGCAGCCAGGATATGACCACCTTACTCAGCTACAACAGGAACTGGAGGGTCTGTGCC TTGTTGAGCTGTACCTCCCACAAGGATTACCCCTTCCATGAAGAGTTTTGA PF00248 Aldo_ket_red function oxidoreductase activity function catalytic activity "
drug:{3-[(5-CHLORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL}ACETIC ACIDrdfs:label"{3-[(5-CHLORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL}ACETIC ACID"
drug:{3-[(5-CHLORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL}ACETIC ACIDrdf:typedrugbank:drugs
drug:{3-[3-(3,4-Dimethoxy-Phenyl)-1-(1-{1-[2-(3,4,5-Trimethoxy-Phenyl)-Butyryl]-Piperidin-2yl}-Vinyloxy)-Propyl]-Phenoxy}-Acetic Aciddrugbank:description" experimental This compound belongs to the chalcones and dihydrochalcones. These are organic compounds containing 1,3-Diphenylpropenone (benzylideneacetophenone), ArCH=CH(=O)Ar,or its derivatives formed by substitution. Chalcones and Dihydrochalcones Organic Compounds Phenylpropanoids and Polyketides Flavonoids Chalcones and Dihydrochalcones Alpha Amino Acid Esters Phenoxyacetic Acid Derivatives Benzyloxycarbonyls Phenylpropylamines Piperidinecarboxylic Acids Benzylethers N-Acylpiperidines Anisoles Alkyl Aryl Ethers Dicarboxylic Acids and Derivatives Tertiary Carboxylic Acid Amides Carboxylic Acid Esters Tertiary Amines Enolates Polyamines Dialkyl Ethers Carboxylic Acids alpha-amino acid ester phenoxyacetate phenylpropylamine benzyloxycarbonyl n-acyl-piperidine benzylether piperidinecarboxylic acid phenol ether anisole alkyl aryl ether benzene piperidine dicarboxylic acid derivative tertiary carboxylic acid amide tertiary amine carboxylic acid ester carboxamide group enolate ether carboxylic acid polyamine carboxylic acid derivative dialkyl ether organonitrogen compound amine logP 5.32 ALOGPS logS -5.9 ALOGPS Water Solubility 9.40e-04 g/l ALOGPS logP 5.7 ChemAxon IUPAC Name 2-{3-[(1S)-3-(3,4-dimethoxyphenyl)-1-{[(2R)-1-[(2S)-2-(3,4,5-trimethoxyphenyl)butanoyl]piperidin-2-yl]carbonyloxy}propyl]phenoxy}acetic acid ChemAxon Traditional IUPAC Name 3-[(1S)-3-(3,4-dimethoxyphenyl)-1-{[(2R)-1-[(2S)-2-(3,4,5-trimethoxyphenyl)butanoyl]piperidin-2-yl]carbonyloxy}propyl]phenoxyacetic acid ChemAxon Molecular Weight 693.7799 ChemAxon Monoisotopic Weight 693.314911351 ChemAxon SMILES CC[C@H](C(=O)N1CCCC[C@@H]1C(=O)O[C@@H](CCC1=CC=C(OC)C(OC)=C1)C1=CC=CC(OCC(O)=O)=C1)C1=CC(OC)=C(OC)C(OC)=C1 ChemAxon Molecular Formula C38H47NO11 ChemAxon InChI InChI=1S/C38H47NO11/c1-7-28(26-21-33(46-4)36(48-6)34(22-26)47-5)37(42)39-18-9-8-13-29(39)38(43)50-30(25-11-10-12-27(20-25)49-23-35(40)41)16-14-24-15-17-31(44-2)32(19-24)45-3/h10-12,15,17,19-22,28-30H,7-9,13-14,16,18,23H2,1-6H3,(H,40,41)/t28-,29+,30-/m0/s1 ChemAxon InChIKey InChIKey=XCCRAOPQCACRFC-JBOQNHBVSA-N ChemAxon Polar Surface Area (PSA) 139.29 ChemAxon Refractivity 184.01 ChemAxon Polarizability 74.75 ChemAxon Rotatable Bond Count 18 ChemAxon H Bond Acceptor Count 10 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 3.44 ChemAxon pKa (strongest basic) -1.5 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 46936201 PubChem Substance 46506401 ChemSpider 5537 PDB AP1 BE0000695 Peptidyl-prolyl cis-trans isomerase FKBP1A Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Peptidyl-prolyl cis-trans isomerase FKBP1A Posttranslational modification, protein turnover, chaperones May play a role in modulation of ryanodine receptor isoform-1 (RYR-1), a component of the calcium release channel of skeletal muscle sarcoplasmic reticulum. There are four molecules of FKBP12 per skeletal muscle RYR. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides FKBP1A 20p13 Cytoplasm None 8.48 11820.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3711 GenAtlas FKBP1A GeneCards FKBP1A GenBank Gene Database M34539 GenBank Protein Database 182628 UniProtKB P62942 UniProt Accession FKB1A_HUMAN 12 kDa FKBP EC 5.2.1.8 FKBP-12 Immunophilin FKBP12 Peptidyl-prolyl cis-trans isomerase PPIase Rotamase >FK506-binding protein 1A GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWE EGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE >327 bp ATGGGAGTGCAGGTGGAAACCATCTCCCCAGGAGACGGGCGCACCTTCCCCAAGCGCGGC CAGACCTGCGTGGTGCACTACACCGGGATGCTTGAAGATGGAAAGAAATTTGATTCCTCC CGGGACAGAAACAAGCCCTTTAAGTTTATGCTAGGCAAGCAGGAGGTGATCCGAGGCTGG GAAGAAGGGGTTGCCCAGATGAGTGTGGGTCAGAGAGCCAAACTGACTATATCTCCAGAT TATGCCTATGGTGCCACTGGGCACCCAGGCATCATCCCACCACATGCCACTCTCGTCTTC GATGTGGAGCTTCTAAAACTGGAATGA PF00254 FKBP_C process physiological process process metabolism process macromolecule metabolism process protein metabolism process cellular protein metabolism process protein folding "
drug:{3-[3-(3,4-Dimethoxy-Phenyl)-1-(1-{1-[2-(3,4,5-Trimethoxy-Phenyl)-Butyryl]-Piperidin-2yl}-Vinyloxy)-Propyl]-Phenoxy}-Acetic Acidrdfs:label"{3-[3-(3,4-Dimethoxy-Phenyl)-1-(1-{1-[2-(3,4,5-Trimethoxy-Phenyl)-Butyryl]-Piperidin-2yl}-Vinyloxy)-Propyl]-Phenoxy}-Acetic Acid"
drug:{3-[3-(3,4-Dimethoxy-Phenyl)-1-(1-{1-[2-(3,4,5-Trimethoxy-Phenyl)-Butyryl]-Piperidin-2yl}-Vinyloxy)-Propyl]-Phenoxy}-Acetic Acidowl:sameAsdrug:EXPT00532
drug:{3-[3-(3,4-Dimethoxy-Phenyl)-1-(1-{1-[2-(3,4,5-Trimethoxy-Phenyl)-Butyryl]-Piperidin-2yl}-Vinyloxy)-Propyl]-Phenoxy}-Acetic Acidrdf:typedrugbank:drugs
drug:{4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanonedrugbank:description" experimental This compound belongs to the benzophenones. These are organic compounds containing a ketone attached to two phenyl groups. Benzophenones Organic Compounds Benzenoids Benzene and Substituted Derivatives Benzophenones Diphenylmethanes Acetophenones Benzoyl Derivatives Phenol Ethers Alkyl Aryl Ethers Thiophenes Pyrrolidines Ketones Polyamines Dialkylamines Enolates acetophenone benzoyl phenol ether alkyl aryl ether pyrrolidine thiophene ketone secondary amine polyamine enolate ether secondary aliphatic amine carbonyl group amine organonitrogen compound logP 4.78 ALOGPS logS -5.8 ALOGPS Water Solubility 6.40e-04 g/l ALOGPS logP 4.8 ChemAxon IUPAC Name (2R)-2-(4-{[4-(thiophen-3-yl)phenyl]carbonyl}phenoxymethyl)pyrrolidine ChemAxon Traditional IUPAC Name (2R)-2-(4-{[4-(thiophen-3-yl)phenyl]carbonyl}phenoxymethyl)pyrrolidine ChemAxon Molecular Weight 363.473 ChemAxon Monoisotopic Weight 363.129299611 ChemAxon SMILES [H][C@]1(COC2=CC=C(C=C2)C(=O)C2=CC=C(C=C2)C2=CSC=C2)CCCN1 ChemAxon Molecular Formula C22H21NO2S ChemAxon InChI InChI=1S/C22H21NO2S/c24-22(17-5-3-16(4-6-17)19-11-13-26-15-19)18-7-9-21(10-8-18)25-14-20-2-1-12-23-20/h3-11,13,15,20,23H,1-2,12,14H2/t20-/m1/s1 ChemAxon InChIKey InChIKey=VUWFJUJWAWMRQN-HXUWFJFHSA-N ChemAxon Polar Surface Area (PSA) 38.33 ChemAxon Refractivity 105.27 ChemAxon Polarizability 41.29 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest basic) 10.38 ChemAxon Physiological Charge 1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 44129624 PubChem Substance 99443708 ChemSpider 24626134 PDB 798 BE0001680 Leukotriene A-4 hydrolase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Leukotriene A-4 hydrolase Amino acid transport and metabolism Hydrolyzes an epoxide moiety of leukotriene A4 (LTA-4) to form leukotriene B4 (LTB-4). The enzyme also has some peptidase activity LTA4H 12q22 Cytoplasm None 6.1 69286.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6710 GenAtlas LTA4H GeneCards LTA4H GenBank Gene Database U27293 GenBank Protein Database 976396 UniProtKB P09960 UniProt Accession LKHA4_HUMAN EC 3.3.2.6 Leukotriene A(4) hydrolase LTA-4 hydrolase >Leukotriene A-4 hydrolase MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDL TIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLT PEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETP DPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETES MLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISH SWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGET HPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSI TTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAK EDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWL RLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVT AMLVGKDLKVD >1836 bp ATGCCCGAGATAGTGGATACCTGTTCGTTGGCCTCTCCGGCTTCCGTCTGCCGGACCAAG CACCTGCACCTGCGCTGCAGCGTCGACTTTACTCGCCGGACGCTGACCGGGACTGCTGCT CTCACGGTCCAGTCTCAGGAGGACAATCTGCGCAGCCTGGTTTTGGATACAAAGGACCTT ACAATAGAAAAAGTAGTGATCAATGGACAAGAAGTCAAATATGCTCTTGGAGAAAGACAA AGTTACAAGGGATCGCCAATGGAAATCTCTCTTCCTATCGCTTTGAGCAAAAATCAAGAA ATTGTTATAGAAATTTCTTTTGAGACCTCTCCAAAATCTTCTGCTCTCCAGTGGCTCACT CCTGAACAGACTTCTGGGAAGGAACACCCATATCTCTTTAGTCAGTGCCAGGCCATCCAC TGCAGAGCAATCCTTCCTTGTCAGGACACTCCTTCTGTGAAATTAACCTATACTGCAGAG GTGTCTGTCCCTAAAGAACTGGTGGCACTTATGAGTGCTATTCGTGATGGAGAAACACCT GACCCAGAAGACCCAAGCAGGAAAATATACAAATTCATCCAAAAAGTTCCAATACCCTGC TACCTGATTGCTTTAGTTGTTGGAGCTTTAGAAAGCAGGCAAATTGGCCCAAGAACTTTG GTGTGGTCTGAGAAAGAGCAGGTGGAAAAGTCTGCTTATGAGTTTTCTGAGACTGAATCT ATGCTTAAAATAGCAGAAGATCTGGGAGGACCGTATGTATGGGGACAGTATGACCTATTG GTCCTGCCACCATCCTTCCCTTATGGTGGCATGGAGAATCCTTGCCTTACTTTTGTAACT CCTACTCTACTGGCAGGCGACAAGTCACTCTCCAATGTCATTGCACATGAAATATCTCAT AGCTGGACAGGGAATCTAGTGACCAACAAAACTTGGGATCACTTTTGGTTAAATGAGGGA CATACTGTGTACTTGGAACGCCACATTTGCGGACGATTGTTTGGTGAAAAGTTCAGACAT TTTAATGCTCTGGGAGGATGGGGAGAACTACAGAATTCGGTAAAGACATTTGGGGAGACA CATCCTTTCACCAAACTTGTGGTTGATCTGACAGATATAGACCCTGATGTAGCTTATTCT TCAGTTCCCTATGAGAAGGGCTTTGCTTTACTTTTTTACCTTGAACAACTGCTTGGAGGA CCAGAGATTTTCCTAGGATTCTTAAAAGCTTATGTTGAGAAGTTTTCCTATAAGAGCATA ACTACTGATGACTGGAAGGATTTCCTGTATTCCTATTTTAAAGATAAGGTTGATGTTCTC AATCAAGTTGATTGGAATGCCTGGCTCTACTCTCCTGGACTGCCTCCCATAAAGCCCAAT TATGATATGACTCTGACAAATGCTTGTATTGCCTTAAGTCAAAGATGGATTACTGCCAAA GAAGATGATTTAAATTCATTCAATGCCACAGACCTGAAGGATCTCTCTTCTCATCAATTG AATGAGTTTTTAGCACAGACGCTCCAGAGGGCACCTCTTCCATTGGGGCACATAAAGCGA ATGCAAGAGGTGTACAACTTCAATGCCATTAACAATTCTGAAATACGATTCAGATGGCTG CGGCTCTGCATTCAATCCAAGTGGGAGGACGCAATTCCTTTGGCGCTAAAGATGGCAACT GAACAAGGAAGAATGAAGTTTACCCGGCCCTTATTCAAGGATCTTGCTGCCTTTGACAAA TCCCATGATCAAGCTGTCCGAACCTACCAAGAGCACAAAGCAAGCATGCATCCCGTGACT GCAATGCTGGTGGGGAAAGACTTAAAAGTGGATTAA PF01433 Peptidase_M1 PF09127 Leuk-A4-hydro_C function membrane alanyl aminopeptidase activity function ion binding function cation binding function transition metal ion binding function zinc ion binding function binding function peptidase activity function catalytic activity function metallopeptidase activity function hydrolase activity function metalloexopeptidase activity process macromolecule metabolism process protein metabolism process cellular protein metabolism process physiological process process proteolysis process metabolism "
drug:{4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanonerdfs:label"{4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone"
drug:{4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanonerdf:typedrugbank:drugs
drug:{4-[(2s,4e)-2-(1,3-Benzothiazol-2-Yl)-2-(1h-1,2,3-Benzotriazol-1-Yl)-5-Phenylpent-4-Enyl]Phenyl}(Difluoro)Methylphosphonic Aciddrugbank:description" experimental This compound belongs to the lignans and norlignans. These are plant products of low molecular weight formed primarily from oxidative coupling of two p-propylphenol moieties. Lignans and Norlignans Organic Compounds Lignans and Norlignans Amphetamines and Derivatives Benzotriazoles Benzothiazoles Phenylpropenes Styrenes Triazoles Thiazoles Organic Phosphonic Acids Polyamines Organofluorides Alkyl Fluorides amphetamine or derivative benzotriazole 1,3-benzothiazole phenylpropene styrene benzene azole thiazole 1,2,3-triazole phosphonic acid phosphonic acid derivative polyamine organofluoride organohalogen amine alkyl halide alkyl fluoride organonitrogen compound logP 5.46 ALOGPS logS -5.2 ALOGPS Water Solubility 4.10e-03 g/l ALOGPS logP 5.84 ChemAxon IUPAC Name ({4-[(2S,4E)-2-(1,3-benzothiazol-2-yl)-2-(1H-1,2,3-benzotriazol-1-yl)-5-phenylpent-4-en-1-yl]phenyl}difluoromethyl)phosphonic acid ChemAxon Traditional IUPAC Name {4-[(2S,4E)-2-(1,3-benzothiazol-2-yl)-2-(1,2,3-benzotriazol-1-yl)-5-phenylpent-4-en-1-yl]phenyl}difluoromethylphosphonic acid ChemAxon Molecular Weight 602.591 ChemAxon Monoisotopic Weight 602.135304298 ChemAxon SMILES C(=C/C1=CC=CC=C1)\C[C@](CC1=CC=C(C=C1)C(F)(F)P(O)(O)=O)(C1=NC2=C(C=CC=C2)S1)N1N=NC2=C1C=CC=C2 ChemAxon Molecular Formula C31H25F2N4O3PS ChemAxon InChI InChI=1S/C31H25F2N4O3PS/c32-31(33,41(38,39)40)24-18-16-23(17-19-24)21-30(20-8-11-22-9-2-1-3-10-22,29-34-26-13-5-7-15-28(26)42-29)37-27-14-6-4-12-25(27)35-36-37/h1-19H,20-21H2,(H2,38,39,40)/b11-8+/t30-/m0/s1 ChemAxon InChIKey InChIKey=GBLDYRVJENYQNH-GHGCAVAYSA-N ChemAxon Polar Surface Area (PSA) 101.13 ChemAxon Refractivity 169.77 ChemAxon Polarizability 59.59 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 0.72 ChemAxon pKa (strongest basic) 2.02 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 6 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 21145368 PubChem Substance 46508576 PDB P90 BE0000623 Tyrosine-protein phosphatase non-receptor type 1 Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Tyrosine-protein phosphatase non-receptor type 1 Involved in protein tyrosine phosphatase activity May play an important role in CKII- and p60c-src-induced signal transduction cascades PTPN1 20q13.1-q13.2 Endoplasmic reticulum; endoplasmic reticulum membrane; peripheral membrane protein; cytoplasmic side 409-431 6.21 49967.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9642 GenAtlas PTPN1 GeneCards PTPN1 GenBank Gene Database M31724 GenBank Protein Database 190742 UniProtKB P18031 UniProt Accession PTN1_HUMAN EC 3.1.3.48 Protein-tyrosine phosphatase 1B PTP-1B >Tyrosine-protein phosphatase non-receptor type 1 MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLH QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK CAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWP DFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKD PSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLE PPPEHIPPPPRPPKRILEPHNGKCREFFPNHQWVKEETQEDKDCPIKEEKGSPLNAAPYG IESMSQDTEVRSRVVGGSLRGAQAASPAKGEPSLPEKDEDHALSYWKPFLVNMCVATVLT AGAYLCYRFLFNSNT >1308 bp ATGGAGATGGAAAAGGAGTTCGAGCAGATCGACAAGTCCGGGAGCTGGGCGGCCATTTAC CAGGATATCCGACATGAAGCCAGTGACTTCCCATGTAGAGTGGCCAAGCTTCCTAAGAAC AAAAACCGAAATAGGTACAGAGACGTCAGTCCCTTTGACCATAGTCGGATTAAACTACAT CAAGAAGATAATGACTATATCAACGCTAGTTTGATAAAAATGGAAGAAGCCCAAAGGAGT TACATTCTTACCCAGGGCCCTTTGCCTAACACATGCGGTCACTTTTGGGAGATGGTGTGG GAGCAGAAAAGCAGGGGTGTCGTCATGCTCAACAGAGTGATGGAGAAAGGTTCGTTAAAA TGCGCACAATACTGGCCACAAAAAGAAGAAAAAGAGATGATCTTTGAAGACACAAATTTG AAATTAACATTGATCTCTGAAGATATCAAGTCATATTATACAGTGCGACAGCTAGAATTG GAAAACCTTACAACCCAAGAAACTCGAGAGATCTTACATTTCCACTATACCACATGGCCT GACTTTGGAGTCCCTGAATCACCAGCCTCATTCTTGAACTTTCTTTTCAAAGTCCGAGAG TCAGGGTCACTCAGCCCGGAGCACGGGCCCGTTGTGGTGCACTGCAGTGCAGGCATCGGC AGGTCTGGAACCTTCTGTCTGGCTGATACCTGCCTCCTGCTGATGGACAAGAGGAAAGAC CCTTCTTCCGTTGATATCAAGAAAGTGCTGTTAGAAATGAGGAAGTTTCGGATGGGGTTG ATCCAGACAGCCGACCAGCTGCGCTTCTCCTACCTGGCTGTGATCGAAGGTGCCAAATTC ATCATGGGGGACTCTTCCGTGCAGGATCAGTGGAAGGAGCTTTCCCACGAGGACCTGGAG CCCCCACCCGAGCATATCCCCCCACCTCCCCGGCCACCCAAACGAATCCTGGAGCCACAC AATGGGAAATGCAGGGAGTTCTTCCCAAATCACCAGTGGGTGAAGGAAGAGACCCAGGAG GATAAAGACTGCCCCATCAAGGAAGAAAAAGGAAGCCCCTTAAATGCCGCACCCTACGGC ATCGAAAGCATGAGTCAAGACACTGAAGTTAGAAGTCGGGTCGTGGGGGGAAGTCTTCGA GGTGCCCAGGCTGCCTCCCCAGCCAAAGGGGAGCCGTCACTGCCCGAGAAGGACGAGGAC CATGCACTGAGTTACTGGAAGCCCTTCCTGGTCAACATGTGCGTGGCTACGGTCCTCACG GCCGGCGCTTACCTCTGCTACAGGTTCCTGTTCAACAGCAACACATAG PF00102 Y_phosphatase function protein tyrosine phosphatase activity function hydrolase activity function hydrolase activity, acting on ester bonds function phosphoric ester hydrolase activity function phosphoric monoester hydrolase activity function phosphoprotein phosphatase activity function catalytic activity process metabolism process protein amino acid dephosphorylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification process physiological process "
drug:{4-[(2s,4e)-2-(1,3-Benzothiazol-2-Yl)-2-(1h-1,2,3-Benzotriazol-1-Yl)-5-Phenylpent-4-Enyl]Phenyl}(Difluoro)Methylphosphonic Acidrdfs:label"{4-[(2s,4e)-2-(1,3-Benzothiazol-2-Yl)-2-(1h-1,2,3-Benzotriazol-1-Yl)-5-Phenylpent-4-Enyl]Phenyl}(Difluoro)Methylphosphonic Acid"
drug:{4-[(2s,4e)-2-(1,3-Benzothiazol-2-Yl)-2-(1h-1,2,3-Benzotriazol-1-Yl)-5-Phenylpent-4-Enyl]Phenyl}(Difluoro)Methylphosphonic Acidowl:sameAsdrug:EXPT02484
drug:{4-[(2s,4e)-2-(1,3-Benzothiazol-2-Yl)-2-(1h-1,2,3-Benzotriazol-1-Yl)-5-Phenylpent-4-Enyl]Phenyl}(Difluoro)Methylphosphonic Acidrdf:typedrugbank:drugs
drug:{4-[(CARBOXYMETHOXY)CARBONYL]-3,3-DIOXIDO-1-OXONAPHTHO[1,2-D]ISOTHIAZOL-2(1H)-YL}ACETIC ACIDdrugbank:description" experimental This compound belongs to the naphthalenecarboxylic acids. These are compounds containing a napthalene moiety with a ring carbon which bears a carboxylic acid group. Naphthalenecarboxylic Acids Organic Compounds Benzenoids Acenes and Derivatives Naphthalenes Alpha Amino Acids and Derivatives Benzoic Acid Esters Tricarboxylic Acids and Derivatives Benzylethers Benzoyl Derivatives Sulfonamides Carboxylic Acid Esters Carboxylic Acid Amides Polyamines Dialkyl Ethers Enolates Carboxylic Acids alpha-amino acid or derivative benzoate ester benzylether benzoic acid or derivative tricarboxylic acid derivative benzoyl benzene sulfonic acid derivative sulfonamide carboxylic acid ester carboxamide group enolate carboxylic acid dialkyl ether carboxylic acid derivative polyamine ether organonitrogen compound amine logP 0.69 ALOGPS logS -3.6 ALOGPS Water Solubility 9.25e-02 g/l ALOGPS logP 0.62 ChemAxon IUPAC Name 2-{[2-(carboxymethyl)-1,3,3-trioxo-1H,2H-3$l^{6},2-naphtho[1,2-d][1$l^{6},2]thiazol-4-yl]carbonyloxy}acetic acid ChemAxon Traditional IUPAC Name {[2-(carboxymethyl)-1,3,3-trioxo-3$l^{6},2-naphtho[1,2-d][1$l^{6},2]thiazol-4-yl]carbonyloxy}acetic acid ChemAxon Molecular Weight 393.325 ChemAxon Monoisotopic Weight 393.015451645 ChemAxon SMILES OC(=O)COC(=O)C1=C2C(C(=O)N(CC(O)=O)S2(=O)=O)=C2C=CC=CC2=C1 ChemAxon Molecular Formula C16H11NO9S ChemAxon InChI InChI=1S/C16H11NO9S/c18-11(19)6-17-15(22)13-9-4-2-1-3-8(9)5-10(14(13)27(17,24)25)16(23)26-7-12(20)21/h1-5H,6-7H2,(H,18,19)(H,20,21) ChemAxon InChIKey InChIKey=IXLBOIRSEDMRPI-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 155.35 ChemAxon Refractivity 87.94 ChemAxon Polarizability 35.36 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 8 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 2.5 ChemAxon pKa (strongest basic) -7 ChemAxon Physiological Charge -2 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 11494891 PubChem Substance 99444470 ChemSpider 9669697 PDB ITA BE0000747 Aldose reductase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aldose reductase Involved in oxidoreductase activity Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies AKR1B1 7q35 Cytoplasm None 6.99 35723.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:381 GenAtlas AKR1B1 GeneCards AKR1B1 GenBank Gene Database J04795 GenBank Protein Database 178487 UniProtKB P15121 UniProt Accession ALDR_HUMAN Aldehyde reductase AR EC 1.1.1.21 >Aldose reductase ASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQE KLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKE FFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPA VNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKH NKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCAL LSCTSHKDYPFHEEF >951 bp ATGGCAAGCCGTCTCCTGCTCAACAACGGCGCCAAGATGCCCATCCTGGGGTTGGGTACC TGGAAGTCCCCTCCAGGGCAGGTGACTGAGGCCGTGAAGGTGGCCATTGACGTCGGGTAC CGCCACATCGACTGTGCCCATGTGTACCAGAATGAGAATGAGGTGGGGGTGGCCATTCAG GAGAAGCTCAGGGAGCAGGTGGTGAAGCGTGAGGAGCTCTTCATCGTCAGCAAGCTGTGG TGCACGTACCATGAGAAGGGCCTGGTGAAAGGAGCCTGCCAGAAGACACTCAGCGACCTG AAGCTGGACTACCTGGACCTCTACCTTATTCACTGGCCGACTGGCTTTAAGCCTGGGAAG GAATTTTTCCCATTGGATGAGTCGGGCAATGTGGTTCCCAGTGACACCAACATTCTGGAC ACGTGGGCGGCCATGGAAGAGCTGGTGGATGAAGGGCTGGTGAAAGCTATTGGCATCTCC AACTTCAACCATCTCCAGGTGGAGATGATCTTAAACAAACCTGGCTTGAAGTATAAGCCT GCAGTTAACCAGATTGAGTGCCACCCATATCTCACTCAGGAGAAGTTAATCCAGTACTGC CAGTCCAAAGGCATCGTGGTGACCGCCTACAGCCCCCTCGGCTCTCCTGACAGGCCCTGG GCCAAGCCCGAGGACCCTTCTCTCCTGGAGGATCCCAGGATCAAGGCGATCGCAGCCAAG CACAATAAAACTACAGCCCAGGTCCTGATCCGGTTCCCCATGCAGAGGAACTTGGTGGTG ATCCCCAAGTCTGTGACACCAGAACGCATTGCTGAGAACTTTAAGGTCTTTGACTTTGAA CTGAGCAGCCAGGATATGACCACCTTACTCAGCTACAACAGGAACTGGAGGGTCTGTGCC TTGTTGAGCTGTACCTCCCACAAGGATTACCCCTTCCATGAAGAGTTTTGA PF00248 Aldo_ket_red function catalytic activity function oxidoreductase activity "
drug:{4-[(CARBOXYMETHOXY)CARBONYL]-3,3-DIOXIDO-1-OXONAPHTHO[1,2-D]ISOTHIAZOL-2(1H)-YL}ACETIC ACIDrdfs:label"{4-[(CARBOXYMETHOXY)CARBONYL]-3,3-DIOXIDO-1-OXONAPHTHO[1,2-D]ISOTHIAZOL-2(1H)-YL}ACETIC ACID"
drug:{4-[(CARBOXYMETHOXY)CARBONYL]-3,3-DIOXIDO-1-OXONAPHTHO[1,2-D]ISOTHIAZOL-2(1H)-YL}ACETIC ACIDrdf:typedrugbank:drugs
drug:{4-[2,2-BIS(5-METHYL-1,2,4-OXADIAZOL-3-YL)-3-PHENYLPROPYL]PHENYL}SULFAMIC ACIDdrugbank:description" experimental This compound belongs to the sulfanilides. These are organic aromatic compounds containing a sulfanilide moiety, with the general structure RS(=O)(=O)NC1=CC=CC=C1. Sulfanilides Organic Compounds Benzenoids Benzene and Substituted Derivatives Sulfanilides Organic Sulfites Organic Sulfuric Acids and Derivatives Oxadiazoles Polyamines organic sulfite oxadiazole azole sulfuric acid derivative polyamine amine organonitrogen compound logP 2.54 ALOGPS logS -3.9 ALOGPS Water Solubility 5.37e-02 g/l ALOGPS logP 2.2 ChemAxon IUPAC Name N-{4-[2,2-bis(5-methyl-1,2,4-oxadiazol-3-yl)-3-phenylpropyl]phenyl}sulfamic acid ChemAxon Traditional IUPAC Name N-{4-[2,2-bis(5-methyl-1,2,4-oxadiazol-3-yl)-3-phenylpropyl]phenyl}sulfamic acid ChemAxon Molecular Weight 455.487 ChemAxon Monoisotopic Weight 455.126339497 ChemAxon SMILES CC1=NC(=NO1)C(CC1=CC=CC=C1)(CC1=CC=C(NS(O)(=O)=O)C=C1)C1=NOC(C)=N1 ChemAxon Molecular Formula C21H21N5O5S ChemAxon InChI InChI=1S/C21H21N5O5S/c1-14-22-19(24-30-14)21(20-23-15(2)31-25-20,12-16-6-4-3-5-7-16)13-17-8-10-18(11-9-17)26-32(27,28)29/h3-11,26H,12-13H2,1-2H3,(H,27,28,29) ChemAxon InChIKey InChIKey=SXDBFKLPNPUPRI-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 144.24 ChemAxon Refractivity 128.06 ChemAxon Polarizability 45.48 ChemAxon Rotatable Bond Count 7 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) -1.6 ChemAxon pKa (strongest basic) -1 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon ChEBI 40118 PubChem Compound 6914661 PubChem Substance 99443598 ChemSpider 5290539 PDB 4UN BE0003769 Receptor-type tyrosine-protein phosphatase beta Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Receptor-type tyrosine-protein phosphatase beta Involved in protein binding Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate PTPRB 12q15-q21 Membrane 1622-1642 7.72 224266.7 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9665 GeneCards PTPRB GenBank Gene Database X54131 GenBank Protein Database 35788 UniProtKB P23467 UniProt Accession PTPRB_HUMAN Protein-tyrosine phosphatase beta R-PTP-beta >Receptor-type tyrosine-protein phosphatase beta MLSHGAGLALWITLSLLQTGLAEPERCNFTLAESKASSHSVSIQWRILGSPCNFSLIYSS DTLGAALCPTFRIDNTTYGCNLQDLQAGTIYNFKIISLDEERTVVLQTDPLPPARFGVSK EKTTSTGLHVWWTPSSGKVTSYEVQLFDENNQKIQGVQIQESTSWNEYTFFNLTAGSKYN IAITAVSGGKRSFSVYTNGSTVPSPVKDIGISTKANSLLISWSHGSGNVERYRLMLMDKG ILVHGGVVDKHATSYAFHGLSPGYLYNLTVMTEAAGLQNYRWKLVRTAPMEVSNLKVTND GSLTSLKVKWQRPPGNVDSYNITLSHKGTIKESRVLAPWITETHFKELVPGRLYQVTVSC VSGELSAQKMAVGRTFPDKVANLEANNNGRMRSLVVSWSPPAGDWEQYRILLFNDSVVLL NITVGKEETQYVMDDTGLVPGRQYEVEVIVESGNLKNSERCQGRTVPLAVLQLRVKHANE TSLSIMWQTPVAEWEKYIISLADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISG DLKNSSSVKGRTVPAQVTDLHVANQGMTSSLFTNWTQAQGDVEFYQVLLIHENVVIKNES ISSETSRYSFHSLKSGSLYSVVVTTVSGGISSRQVVVEGRTVPSSVSGVTVNNSGRNDYL SVSWLVAPGDVDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGKYE NHSFSQERTVPDKVQGVSVSNSARSDYLRVSWVHATGDFDHYEVTIKNKNNFIQTKSIPK SENECVFVQLVPGRLYSVTVTTKSGQYEANEQGNGRTIPEPVKDLTLRNRSTEDLHVTWS GANGDVDQYEIQLLFNDMKVFPPFHLVNTATEYRFTSLTPGRQYKILVLTISGDVQQSAF IEGFTVPSAVKNIHISPNGATDSLTVNWTPGGGDVDSYTVSAFRHSQKVDSQTIPKHVFE HTFHRLEAGEQYQIMIASVSGSLKNQINVVGRTVPASVQGVIADNAYSSYSLIVSWQKAA GVAERYDILLLTENGILLRNTSEPATTKQHKFEDLTPGKKYKIQILTVSGGLFSKEAQTE GRTVPAAVTDLRITENSTRHLSFRWTASEGELSWYNIFLYNPDGNLQERAQVDPLVQSFS FQNLLQGRMYKMVIVTHSGELSNESFIFGRTVPASVSHLRGSNRNTTDSLWFNWSPASGD FDFYELILYNPNGTKKENWKDKDLTEWRFQGLVPGRKYVLWVVTHSGDLSNKVTAESRTA PSPPSLMSFADIANTSLAITWKGPPDWTDYNDFELQWLPRDALTVFNPYNNRKSEGRIVY GLRPGRSYQFNVKTVSGDSWKTYSKPIFGSVRTKPDKIQNLHCRPQNSTAIACSWIPPDS DFDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGMTSEVVEDS TITMIDRPPPPPPHIRVNEKDVLISKSSINFTVNCSWFSDTNGAVKYFTVVVREADGSDE LKPEQQHPLPSYLEYRHNASIRVYQTNYFASKCAENPNSNSKSFNIKLGAEMESLGGKRD PTQQKFCDGPLKPHTAYRISIRAFTQLFDEDLKEFTKPLYSDTFFSLPITTESEPLFGAI EGVSAGLFLIGMLVAVVALLICRQKVSHGRERPSARLSIRRDRPLSVHLNLGQKGNRKTS CPIKINQFEGHFMKLQADSNYLLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYD ATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVM VTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLI RHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRI LQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLRARKLRSEQENPLFPI YENVNPEYHRDPVYSRH >5994 bp ATGCTGAGCCATGGAGCCGGGTTGGCCTTGTGGATCACACTGAGCCTGCTGCAGACTGGA CTGGCGGAGCCAGAGAGATGTAACTTCACCCTGGCGGAGTCCAAGGCCTCCAGCCATTCT GTGTCTATCCAGTGGAGAATTTTGGGCTCACCCTGTAACTTTAGCCTCATCTATAGCAGT GACACCCTGGGGGCCGCGTTGTGCCCTACCTTTCGGATAGACAACACCACATACGGATGT AACCTTCAAGATTTACAAGCAGGAACCATCTATAACTTCAAGATTATTTCTCTGGATGAA GAGAGAACTGTGGTCTTGCAAACAGATCCTTTACCTCCTGCTAGGTTTGGAGTCAGTAAA GAGAAGACGACTTCAACCGGCTTGCATGTTTGGTGGACTCCTTCTTCCGGAAAAGTCACC TCATATGAGGTGCAATTATTTGATGAAAATAACCAAAAGATACAGGGGGTTCAAATTCAA GAAAGTACTTCATGGAATGAATACACTTTTTTCAATCTCACTGCTGGTAGTAAATACAAT ATTGCCATCACAGCTGTTTCTGGAGGAAAACGTTCTTTTTCAGTTTATACCAATGGATCA ACAGTGCCATCTCCAGTGAAAGATATTGGTATTTCCACAAAAGCCAATTCTCTCCTGATT TCCTGGTCCCATGGTTCTGGGAATGTGGAACGATACCGGCTGATGCTAATGGATAAAGGG ATCCTAGTTCATGGCGGTGTTGTGGACAAACATGCTACTTCCTATGCTTTTCACGGGCTG TCCCCTGGCTACCTCTACAACCTCACTGTTATGACTGAGGCTGCAGGGCTGCAAAACTAC AGGTGGAAACTAGTCAGGACAGCCCCCATGGAAGTCTCAAATCTGAAGGTGACAAATGAT GGCAGTTTGACCTCTCTAAAAGTCAAATGGCAAAGACCTCCTGGAAATGTGGATTCTTAC AATATCACCCTGTCTCACAAAGGGACCATCAAGGAATCCAGAGTATTAGCACCTTGGATT ACTGAAACTCACTTTAAAGAGTTAGTCCCCGGTCGACTTTATCAAGTTACTGTCAGCTGT GTCTCTGGTGAACTGTCTGCTCAGAAGATGGCAGTGGGCAGAACATTTCCAGACAAAGTT GCAAACCTGGAGGCAAACAATAATGGCAGGATGAGGTCTCTTGTAGTGAGCTGGTCGCCC CCTGCTGGAGACTGGGAGCAGTATCGGATCCTACTCTTCAATGATTCTGTGGTGCTGCTC AACATCACTGTGGGAAAGGAAGAAACACAGTATGTCATGGATGACACGGGGCTCGTACCG GGAAGACAGTATGAGGTGGAAGTCATTGTTGAGAGTGGAAATTTGAAGAATTCTGAGCGT TGCCAAGGCAGGACAGTCCCCCTGGCTGTCCTCCAGCTTCGTGTCAAACATGCCAATGAA ACCTCACTGAGTATCATGTGGCAGACCCCTGTAGCAGAATGGGAGAAATACATCATTTCC CTAGCTGACAGAGACCTCTTACTGATCCACAAGTCACTCTCCAAAGATGCCAAAGAATTC ACTTTTACTGACCTGGTGCCTGGACGAAAATACATGGCTACAGTCACCAGTATTAGTGGA GACTTAAAAAATTCCTCTTCAGTAAAAGGAAGAACAGTGCCTGCCCAAGTGACTGACTTG CATGTGGCCAACCAAGGAATGACCAGTAGTCTGTTTACTAACTGGACCCAGGCACAAGGA GACGTAGAATTTTACCAAGTCTTACTGATCCATGAAAATGTGGTCATTAAAAATGAAAGC ATCTCCAGTGAGACCAGCAGATACAGCTTCCACTCTCTCAAGTCCGGCAGCCTGTACTCC GTGGTGGTAACAACAGTGAGTGGAGGGATCTCTTCCCGACAAGTGGTTGTGGAGGGAAGA ACAGTCCCTTCCAGTGTGAGTGGAGTAACGGTGAACAATTCCGGTCGTAATGACTACCTC AGCGTTTCCTGGCTCGTGGCGCCCGGAGATGTGGATAACTATGAGGTAACATTGTCTCAT GACGGCAAGGTGGTTCAGTCCCTTGTCATTGCCAAGTCTGTCAGAGAATGTTCCTTCAGC TCCCTCACCCCAGGCCGCCTCTACACCGTGACCATAACTACAAGGAGTGGCAAGTATGAA AATCACTCCTTCAGCCAAGAGCGGACAGTGCCTGACAAAGTCCAGGGAGTCAGTGTTAGC AACTCAGCCAGGAGTGACTATTTAAGGGTATCCTGGGTGCATGCCACTGGAGACTTTGAT CACTATGAAGTCACCATTAAAAACAAAAACAACTTCATTCAAACTAAAAGCATTCCCAAG TCAGAAAACGAATGTGTATTTGTTCAGCTAGTCCCTGGACGGTTGTACAGTGTCACTGTT ACTACAAAAAGTGGACAATATGAAGCCAATGAACAAGGGAATGGGAGAACAATTCCAGAG CCTGTTAAGGATCTAACATTGCGCAACAGGAGCACTGAGGACTTGCATGTGACTTGGTCA GGAGCTAATGGGGATGTCGACCAATATGAGATCCAGCTGCTCTTCAATGACATGAAAGTA TTTCCTCCTTTTCACCTTGTAAATACCGCAACCGAGTATCGATTTACTTCCCTAACACCA GGCCGCCAATACAAAATTCTTGTCTTGACGATTAGCGGGGATGTACAGCAGTCAGCCTTC ATTGAGGGCTTCACAGTTCCTAGTGCTGTCAAAAATATTCACATTTCTCCCAATGGAGCA ACAGATAGCCTGACGGTGAACTGGACTCCTGGTGGGGGAGACGTTGATTCCTACACGGTG TCGGCATTCAGGCACAGTCAAAAGGTTGACTCTCAGACTATTCCCAAGCACGTCTTTGAG CACACGTTCCACAGACTGGAGGCCGGGGAGCAGTACCAGATCATGATTGCCTCAGTCAGC GGGTCCCTGAAGAATCAGATAAATGTGGTTGGGCGGACAGTTCCAGCATCTGTCCAAGGA GTAATTGCAGACAATGCATACAGCAGTTATTCCTTAATAGTAAGTTGGCAAAAAGCTGCT GGTGTGGCAGAAAGATATGATATCCTGCTTCTAACTGAAAATGGAATCCTTCTGCGCAAC ACATCAGAGCCAGCCACCACTAAGCAACACAAATTTGAAGATCTAACACCAGGCAAGAAA TACAAGATACAGATCCTAACTGTCAGTGGAGGCCTCTTTAGCAAGGAAGCCCAGACTGAA GGCCGAACAGTCCCAGCAGCTGTCACCGACCTGAGGATCACAGAGAACTCCACCAGGCAC CTGTCCTTCCGCTGGACCGCCTCAGAGGGGGAGCTCAGCTGGTACAACATCTTTTTGTAC AACCCAGATGGGAATCTCCAGGAGAGAGCTCAAGTTGACCCACTAGTCCAGAGCTTCTCT TTCCAGAACTTGCTACAAGGCAGAATGTACAAGATGGTGATTGTAACTCACAGTGGGGAG CTGTCTAATGAGTCTTTCATATTTGGTAGAACAGTCCCAGCCTCTGTGAGTCATCTCAGG GGGTCCAATCGGAACACGACAGACAGCCTTTGGTTCAACTGGAGTCCAGCCTCTGGGGAC TTTGACTTTTATGAGCTGATTCTCTATAATCCCAATGGCACAAAGAAGGAAAACTGGAAA GACAAGGACCTGACGGAGTGGCGGTTTCAAGGCCTTGTTCCTGGAAGGAAGTACGTGCTG TGGGTGGTAACTCACAGTGGAGATCTCAGCAATAAAGTCACAGCGGAGAGCAGAACAGCT CCAAGTCCTCCCAGTCTTATGTCATTTGCTGACATTGCAAACACATCCTTGGCCATCACG TGGAAAGGGCCCCCAGACTGGACAGACTACAACGACTTTGAGCTGCAGTGGTTGCCCAGA GATGCACTTACTGTCTTCAACCCCTACAACAACAGAAAATCAGAAGGACGCATTGTGTAT GGTCTTCGTCCAGGGAGATCCTATCAATTCAACGTCAAGACTGTCAGTGGTGATTCCTGG AAAACTTACAGCAAACCAATTTTTGGATCTGTGAGGACAAAGCCTGACAAGATACAAAAC CTGCATTGCCGGCCTCAGAACTCCACGGCCATTGCCTGTTCTTGGATCCCTCCTGATTCT GACTTTGATGGTTATAGTATTGAATGCCGGAAAATGGACACCCAAGAAGTTGAGTTTTCC AGAAAGCTGGAGAAAGAAAAATCTCTGCTCAACATCATGATGCTAGTGCCCCATAAGAGG TACCTGGTGTCCATCAAAGTGCAGTCGGCCGGCATGACCAGCGAGGTGGTTGAAGACAGC ACTATCACAATGATAGACCGCCCCCCTCCTCCACCCCCACACATTCGTGTGAATGAAAAG GATGTGCTAATTAGCAAGTCTTCCATCAACTTTACTGTCAACTGCAGCTGGTTCAGCGAC ACCAATGGAGCTGTGAAATACTTCACAGTGGTGGTGAGAGAGGCTGATGGCAGTGATGAG CTGAAGCCAGAACAGCAGCACCCTCTCCCTTCCTACCTGGAGTACAGGCACAATGCCTCC ATTCGGGTGTATCAGACTAATTATTTTGCCAGCAAATGTGCCGAAAATCCTAACAGCAAC TCCAAGAGTTTTAACATTAAGCTTGGAGCAGAGATGGAGAGCTTAGGTGGAAAACGCGAT CCCACTCAGCAAAAATTCTGTGATGGACCACTGAAGCCACACACTGCCTACAGAATCAGC ATTCGAGCTTTTACACAGCTCTTTGATGAGGACCTGAAGGAATTCACAAAGCCACTCTAT TCAGACACATTTTTTTCTTTACCCATCACTACTGAATCAGAGCCCTTGTTTGGAGCTATT GAAGGTGTGAGTGCTGGTCTGTTTTTAATTGGCATGCTAGTGGCTGTTGTTGCCTTATTG ATCTGCAGACAGAAAGTGAGCCATGGTCGAGAAAGACCCTCTGCCCGTCTGAGCATTCGT AGGGATCGACCATTATCTGTCCACTTAAACCTGGGCCAGAAAGGTAACCGGAAAACTTCT TGTCCAATAAAAATAAATCAGTTTGAAGGGCATTTCATGAAGCTACAGGCTGACTCCAAC TACCTTCTATCCAAGGAATACGAGGAGTTAAAAGACGTGGGCCGAAACCAGTCATGTGAC ATTGCACTCTTGCCGGAGAATAGAGGGAAAAATCGATACAACAATATATTGCCCTATGAT GCCACGCGAGTGAAGCTCTCCAATGTAGATGATGATCCTTGCTCTGACTACATCAATGCC AGCTACATCCCTGGCAACAACTTCAGAAGAGAATACATTGTCACTCAGGGACCGCTTCCT GGCACCAAGGATGACTTCTGGAAAATGGTGTGGGAACAAAACGTTCACAACATCGTCATG GTGACCCAGTGTGTTGAGAAGGGCCGAGTAAAGTGTGACCATTACTGGCCAGCGGACCAG GATTCCCTCTACTATGGGGACCTCATCCTGCAGATGCTCTCAGAGTCCGTCCTGCCTGAG TGGACCATCCGGGAGTTTAAGATATGCGGTGAGGAACAGCTTGATGCACACAGACTCATC CGCCACTTTCACTATACGGTGTGGCCAGACCATGGAGTCCCAGAAACCACCCAGTCTCTG ATCCAGTTTGTGAGAACTGTCAGGGACTACATCAACAGAAGCCCGGGTGCTGGGCCCACT GTGGTGCACTGCAGTGCTGGTGTGGGTAGGACTGGAACCTTTATTGCATTGGACCGAATC CTCCAGCAGTTAGACTCCAAAGACTCTGTGGACATTTATGGAGCAGTGCACGACCTAAGA CTTCACAGGGTTCACATGGTCCAGACTGAGTGTCAGTATGTCTACCTACATCAGTGTGTA AGAGATGTCCTCAGAGCAAGAAAGCTACGGAGTGAACAAGAAAACCCCTTGTTTCCAATC TATGAAAATGTGAATCCAGAGTATCACAGAGATCCAGTCTATTCAAGGCATTGA PF00041 fn3 PF00102 Y_phosphatase function hydrolase activity, acting on ester bonds function phosphoric ester hydrolase activity function phosphoric monoester hydrolase activity function phosphoprotein phosphatase activity function catalytic activity function protein tyrosine phosphatase activity function hydrolase activity process biopolymer metabolism process biopolymer modification process protein modification process physiological process process metabolism process protein amino acid dephosphorylation process macromolecule metabolism "
drug:{4-[2,2-BIS(5-METHYL-1,2,4-OXADIAZOL-3-YL)-3-PHENYLPROPYL]PHENYL}SULFAMIC ACIDrdfs:label"{4-[2,2-BIS(5-METHYL-1,2,4-OXADIAZOL-3-YL)-3-PHENYLPROPYL]PHENYL}SULFAMIC ACID"
drug:{4-[2,2-BIS(5-METHYL-1,2,4-OXADIAZOL-3-YL)-3-PHENYLPROPYL]PHENYL}SULFAMIC ACIDrdf:typedrugbank:drugs
drug:{4-[2-Acetylamino-2-(3-Carbamoyl-2-Cyclohexylmethoxy-6,7,8,9-Tetrahydro-5h-Benzocyclohepten-5ylcarbamoyl)-Ethyl]-2-Phosphono-Phenyl}-Phosphonic Aciddrugbank:description" experimental This compound belongs to the n-acyl-alpha amino acids and derivatives. These are compounds containing an alpha amino acid (or a derivative thereof) which bears an acyl group at his terminal nitrogen atom. N-acyl-alpha Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Alpha Amino Acid Amides Phenylpropylamines Salicylic Acid and Derivatives Amphetamines and Derivatives Benzamides Benzoyl Derivatives Phenol Ethers Alkyl Aryl Ethers Organic Phosphonic Acids Organic Phosphines and Derivatives Secondary Carboxylic Acid Amides Primary Carboxylic Acid Amides Polyamines Carboxylic Acids Enolates salicylic acid or derivative amphetamine or derivative phenylpropylamine benzamide phenol ether benzoyl alkyl aryl ether benzene phosphonic acid derivative phosphonic acid secondary carboxylic acid amide primary carboxylic acid amide carboxamide group phosphine polyamine carboxylic acid ether enolate amine organonitrogen compound logP 1.25 ALOGPS logS -4.8 ALOGPS Water Solubility 1.01e-02 g/l ALOGPS logP 0.54 ChemAxon IUPAC Name {4-[(2S)-2-{[(5R)-3-carbamoyl-2-(cyclohexylmethoxy)-6,7,8,9-tetrahydro-5H-benzo[7]annulen-5-yl]carbamoyl}-2-acetamidoethyl]-2-phosphonophenyl}phosphonic acid ChemAxon Traditional IUPAC Name 4-[(2S)-2-{[(5R)-3-carbamoyl-2-(cyclohexylmethoxy)-6,7,8,9-tetrahydro-5H-benzo[7]annulen-5-yl]carbamoyl}-2-acetamidoethyl]-2-phosphonophenylphosphonic acid ChemAxon Molecular Weight 665.6082 ChemAxon Monoisotopic Weight 665.226717571 ChemAxon SMILES CC(=O)N[C@@H](CC1=CC=C(C(=C1)P(O)(O)=O)P(O)(O)=O)C(=O)N[C@@H]1CCCCC2=CC(OCC3CCCCC3)=C(C=C12)C(N)=O ChemAxon Molecular Formula C30H41N3O10P2 ChemAxon InChI InChI=1S/C30H41N3O10P2/c1-18(34)32-25(13-20-11-12-27(44(37,38)39)28(14-20)45(40,41)42)30(36)33-24-10-6-5-9-21-15-26(23(29(31)35)16-22(21)24)43-17-19-7-3-2-4-8-19/h11-12,14-16,19,24-25H,2-10,13,17H2,1H3,(H2,31,35)(H,32,34)(H,33,36)(H2,37,38,39)(H2,40,41,42)/t24-,25+/m1/s1 ChemAxon InChIKey InChIKey=SPSGYTWOIGAABK-RPBOFIJWSA-N ChemAxon Polar Surface Area (PSA) 225.58 ChemAxon Refractivity 166.34 ChemAxon Polarizability 67.14 ChemAxon Rotatable Bond Count 11 ChemAxon H Bond Acceptor Count 10 ChemAxon H Bond Donor Count 7 ChemAxon pKa (strongest acidic) 1.27 ChemAxon pKa (strongest basic) -1.1 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 4 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 9896036 PubChem Substance 46506466 ChemSpider 2123 PDB CC1 BE0000842 Tyrosine-protein kinase Lck Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Tyrosine-protein kinase Lck Involved in protein kinase activity Tyrosine kinase that plays an essential role for the selection and maturation of developing T-cell in the thymus and in mature T-cell function. Is constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors and plays a key role in T-cell antigen receptor(TCR)-linked signal transduction pathways. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, and thereby recruits the associated LCK to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosines-based activation motifs (ITAMs) in the cytoplasmic tails of the TCRgamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. In addition, contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, and upon engagement of the CD2 molecule, LCK undergoes hyperphosphorylation and activation. Also plays a role in the IL2 receptor-linked signaling pathway that controls T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR LCK 1p34.3 Cytoplasm. Cell membrane; lipid-anchor; cytoplasmic side. Present in lipid rafts in an unactive form None 5.03 57870.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6524 GenAtlas LCK GeneCards LCK GenBank Gene Database X05027 GenBank Protein Database 36808 UniProtKB P06239 UniProt Accession LCK_HUMAN EC 2.7.10.2 LSK Lymphocyte cell-specific protein-tyrosine kinase p56-LCK T cell- specific protein-tyrosine kinase >Proto-oncogene tyrosine-protein kinase LCK GCGCSSHPEDDWMENIDVCENCHYPIVPLDGKGTLLIRNGSEVRDPLVTYEGSNPPASPL QDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANS LEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHY KIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQTQKPQKPWWEDEWEVP RETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHQRLV RLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYI HRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKS DVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEELYQLMRLCWKERP EDRPTFDYLRSVLEDFFTATEGQYQPQP >1524 bp ATGGGCTGTGGCTGCAGCTCACACCCGGAAGATGACTGGATGGAAAACATCGATGTGTGT GAGAACTGCCATTATCCCATAGTCCCACTGGATGGCAAGGGCACGCTGCTCATCCGAAAT GGCTCTGAGGTGCGGGACCCACTGGTTACCTACGAAGGCTCCAATCCGCCGGCTTCCCCA CTGCAAGACAACCTGGTTATCGCTCTGCACAGCTATGAGCCCTCTCACGACGGAGATCTG GGCTTTGAGAAGGGGGAACAGCTCCGCATCCTGGAGCAGAGCGGCGAGTGGTGGAAGGCG CAGTCCCTGACCACGGGCCAGGAAGGCTTCATCCCCTTCAATTTTGTGGCCAAAGCGAAC AGCCTGGAGCCCGAACCCTGGTTCTTCAAGAACCTGAGCCGCAAGGACGCGGAGCGGCAG CTCCTGGCGCCCGGGAACACTCACGGCTCCTTCCTCATCCGGGAGAGCGAGAGCACCGCG GGATCGTTTTCACTGTCGGTCCGGGACTTCGACCAGAACCAGGGAGAGGTGGTGAAACAT TACAAGATCCGTAATCTGGACAACGGTGGCTTCTACATCTCCCCTCGAATCACTTTTCCC GGCCTGCATGAACTGGCCTCCGCCATTACACCAATCGCTTCAGATGGGCTGTGCACACGG TTGAGCCGCCCCTGCCAGACCCAGAAGCCCCAGAAGCCGTGGTGGGAGGACGAGTGGGAG GTTCCCAGGGAGACGCTGAAGCTGGTGGAGCGGCTGGGGGCTGGACAGTTCGGGAGGTGT GGATGGGGTACTACAACGGGCACAACGAAGGTGGCGGTGAAGAGCCTGAAGCAGGGCAGC ATGTCCGCCGGACGCCTTCCTGCCGAGGCCAACCTCATGAAGCAGCTGCAACACCAGCGG CTGGTTCGGCTCTACGCTGTGGTCACCCAGGAGCCCATCTACATCATCACTGAATACATG GAGAATGGGAGTCTAGTGGATTTTCTCAAGACCCCTTCAGGCATCAAGTTGACCATCAAC AAACTCCTGGACATGGCAGCCCAAATTGCAGAAGGCATGGCATTCATTGAAGAGCGGAAT TATATTCATCGTGACCTTCGGGCTGCCAACATTCTGGTGTCTGACACCCTGAGCTGCAAG ATTGCAGACTTTGGCCTAGCACGCCTCATTGAGGACAACGAGTACACAGCCAGGGAGGGG GCCAAGTTTCCCATTAAGTGGACAGCGCCAGAAGCCATTAACTACGGGACATTCACCATC AAGTCAGATGTGTGGTCTTTTGGGATCCTGCTGACGGAAATTGTCACCCACGGCCGCATC CCTTACCCAGGGATGACCAACCCGGAGGTGATTCAGAACCTGGAGCGAGGCTACCGCATG GTGCGCCCTGACAACTGTCCAGAGGAGCTGTACCAACTCATGAGGCTGTGCTGGAAGGAG CGCCCAGAGGACCGGCCCACCTTTGACTACCTGCGCAGTGTGCTGGAGGACTTCTTCACG GCCACAGAGGGCAGTACAGCCTAG PF07714 Pkinase_Tyr PF00017 SH2 PF00018 SH3_1 function transferase activity, transferring phosphorus-containing groups function kinase activity function nucleotide binding function protein kinase activity function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function catalytic activity function protein-tyrosine kinase activity function ATP binding process biopolymer modification process protein modification process intracellular signaling cascade process protein amino acid phosphorylation process physiological process process cellular process process cell communication process metabolism process signal transduction process macromolecule metabolism process biopolymer metabolism "
drug:{4-[2-Acetylamino-2-(3-Carbamoyl-2-Cyclohexylmethoxy-6,7,8,9-Tetrahydro-5h-Benzocyclohepten-5ylcarbamoyl)-Ethyl]-2-Phosphono-Phenyl}-Phosphonic Acidrdfs:label"{4-[2-Acetylamino-2-(3-Carbamoyl-2-Cyclohexylmethoxy-6,7,8,9-Tetrahydro-5h-Benzocyclohepten-5ylcarbamoyl)-Ethyl]-2-Phosphono-Phenyl}-Phosphonic Acid"
drug:{4-[2-Acetylamino-2-(3-Carbamoyl-2-Cyclohexylmethoxy-6,7,8,9-Tetrahydro-5h-Benzocyclohepten-5ylcarbamoyl)-Ethyl]-2-Phosphono-Phenyl}-Phosphonic Acidowl:sameAsdrug:EXPT00856
drug:{4-[2-Acetylamino-2-(3-Carbamoyl-2-Cyclohexylmethoxy-6,7,8,9-Tetrahydro-5h-Benzocyclohepten-5ylcarbamoyl)-Ethyl]-2-Phosphono-Phenyl}-Phosphonic Acidrdf:typedrugbank:drugs
drug:{4-[2-BENZYL-3-METHOXY-2-(METHOXYCARBONYL)-3-OXOPROPYL]PHENYL}SULFAMIC ACIDdrugbank:description" experimental This compound belongs to the sulfanilides. These are organic aromatic compounds containing a sulfanilide moiety, with the general structure RS(=O)(=O)NC1=CC=CC=C1. Sulfanilides Organic Compounds Benzenoids Benzene and Substituted Derivatives Sulfanilides Fatty Acid Esters Dicarboxylic Acids and Derivatives Organic Sulfites Organic Sulfuric Acids and Derivatives Carboxylic Acid Esters Enolates Ethers Polyamines fatty acid ester dicarboxylic acid derivative organic sulfite sulfuric acid derivative carboxylic acid ester carboxylic acid derivative polyamine ether enolate amine organonitrogen compound logP 1.37 ALOGPS logS -4.8 ALOGPS Water Solubility 6.57e-03 g/l ALOGPS logP 2.71 ChemAxon IUPAC Name N-{4-[2-benzyl-3-methoxy-2-(methoxycarbonyl)-3-oxopropyl]phenyl}sulfamic acid ChemAxon Traditional IUPAC Name N-{4-[2-benzyl-3-methoxy-2-(methoxycarbonyl)-3-oxopropyl]phenyl}sulfamic acid ChemAxon Molecular Weight 407.438 ChemAxon Monoisotopic Weight 407.103872721 ChemAxon SMILES COC(=O)C(CC1=CC=CC=C1)(CC1=CC=C(NS(O)(=O)=O)C=C1)C(=O)OC ChemAxon Molecular Formula C19H21NO7S ChemAxon InChI InChI=1S/C19H21NO7S/c1-26-17(21)19(18(22)27-2,12-14-6-4-3-5-7-14)13-15-8-10-16(11-9-15)20-28(23,24)25/h3-11,20H,12-13H2,1-2H3,(H,23,24,25) ChemAxon InChIKey InChIKey=SUACYXRSGYYBGT-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 119 ChemAxon Refractivity 100.92 ChemAxon Polarizability 40.11 ChemAxon Rotatable Bond Count 9 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) -1.4 ChemAxon pKa (strongest basic) -6.9 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 6914659 PubChem Substance 99443460 ChemSpider 5290537 PDB 2UN BE0003769 Receptor-type tyrosine-protein phosphatase beta Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Receptor-type tyrosine-protein phosphatase beta Involved in protein binding Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate PTPRB 12q15-q21 Membrane 1622-1642 7.72 224266.7 Human HUGO Gene Nomenclature Committee (HGNC) GNC:9665 GeneCards PTPRB GenBank Gene Database X54131 GenBank Protein Database 35788 UniProtKB P23467 UniProt Accession PTPRB_HUMAN Protein-tyrosine phosphatase beta R-PTP-beta >Receptor-type tyrosine-protein phosphatase beta MLSHGAGLALWITLSLLQTGLAEPERCNFTLAESKASSHSVSIQWRILGSPCNFSLIYSS DTLGAALCPTFRIDNTTYGCNLQDLQAGTIYNFKIISLDEERTVVLQTDPLPPARFGVSK EKTTSTGLHVWWTPSSGKVTSYEVQLFDENNQKIQGVQIQESTSWNEYTFFNLTAGSKYN IAITAVSGGKRSFSVYTNGSTVPSPVKDIGISTKANSLLISWSHGSGNVERYRLMLMDKG ILVHGGVVDKHATSYAFHGLSPGYLYNLTVMTEAAGLQNYRWKLVRTAPMEVSNLKVTND GSLTSLKVKWQRPPGNVDSYNITLSHKGTIKESRVLAPWITETHFKELVPGRLYQVTVSC VSGELSAQKMAVGRTFPDKVANLEANNNGRMRSLVVSWSPPAGDWEQYRILLFNDSVVLL NITVGKEETQYVMDDTGLVPGRQYEVEVIVESGNLKNSERCQGRTVPLAVLQLRVKHANE TSLSIMWQTPVAEWEKYIISLADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISG DLKNSSSVKGRTVPAQVTDLHVANQGMTSSLFTNWTQAQGDVEFYQVLLIHENVVIKNES ISSETSRYSFHSLKSGSLYSVVVTTVSGGISSRQVVVEGRTVPSSVSGVTVNNSGRNDYL SVSWLVAPGDVDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGKYE NHSFSQERTVPDKVQGVSVSNSARSDYLRVSWVHATGDFDHYEVTIKNKNNFIQTKSIPK SENECVFVQLVPGRLYSVTVTTKSGQYEANEQGNGRTIPEPVKDLTLRNRSTEDLHVTWS GANGDVDQYEIQLLFNDMKVFPPFHLVNTATEYRFTSLTPGRQYKILVLTISGDVQQSAF IEGFTVPSAVKNIHISPNGATDSLTVNWTPGGGDVDSYTVSAFRHSQKVDSQTIPKHVFE HTFHRLEAGEQYQIMIASVSGSLKNQINVVGRTVPASVQGVIADNAYSSYSLIVSWQKAA GVAERYDILLLTENGILLRNTSEPATTKQHKFEDLTPGKKYKIQILTVSGGLFSKEAQTE GRTVPAAVTDLRITENSTRHLSFRWTASEGELSWYNIFLYNPDGNLQERAQVDPLVQSFS FQNLLQGRMYKMVIVTHSGELSNESFIFGRTVPASVSHLRGSNRNTTDSLWFNWSPASGD FDFYELILYNPNGTKKENWKDKDLTEWRFQGLVPGRKYVLWVVTHSGDLSNKVTAESRTA PSPPSLMSFADIANTSLAITWKGPPDWTDYNDFELQWLPRDALTVFNPYNNRKSEGRIVY GLRPGRSYQFNVKTVSGDSWKTYSKPIFGSVRTKPDKIQNLHCRPQNSTAIACSWIPPDS DFDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGMTSEVVEDS TITMIDRPPPPPPHIRVNEKDVLISKSSINFTVNCSWFSDTNGAVKYFTVVVREADGSDE LKPEQQHPLPSYLEYRHNASIRVYQTNYFASKCAENPNSNSKSFNIKLGAEMESLGGKRD PTQQKFCDGPLKPHTAYRISIRAFTQLFDEDLKEFTKPLYSDTFFSLPITTESEPLFGAI EGVSAGLFLIGMLVAVVALLICRQKVSHGRERPSARLSIRRDRPLSVHLNLGQKGNRKTS CPIKINQFEGHFMKLQADSNYLLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYD ATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVM VTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLI RHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRI LQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLRARKLRSEQENPLFPI YENVNPEYHRDPVYSRH >5994 bp ATGCTGAGCCATGGAGCCGGGTTGGCCTTGTGGATCACACTGAGCCTGCTGCAGACTGGA CTGGCGGAGCCAGAGAGATGTAACTTCACCCTGGCGGAGTCCAAGGCCTCCAGCCATTCT GTGTCTATCCAGTGGAGAATTTTGGGCTCACCCTGTAACTTTAGCCTCATCTATAGCAGT GACACCCTGGGGGCCGCGTTGTGCCCTACCTTTCGGATAGACAACACCACATACGGATGT AACCTTCAAGATTTACAAGCAGGAACCATCTATAACTTCAAGATTATTTCTCTGGATGAA GAGAGAACTGTGGTCTTGCAAACAGATCCTTTACCTCCTGCTAGGTTTGGAGTCAGTAAA GAGAAGACGACTTCAACCGGCTTGCATGTTTGGTGGACTCCTTCTTCCGGAAAAGTCACC TCATATGAGGTGCAATTATTTGATGAAAATAACCAAAAGATACAGGGGGTTCAAATTCAA GAAAGTACTTCATGGAATGAATACACTTTTTTCAATCTCACTGCTGGTAGTAAATACAAT ATTGCCATCACAGCTGTTTCTGGAGGAAAACGTTCTTTTTCAGTTTATACCAATGGATCA ACAGTGCCATCTCCAGTGAAAGATATTGGTATTTCCACAAAAGCCAATTCTCTCCTGATT TCCTGGTCCCATGGTTCTGGGAATGTGGAACGATACCGGCTGATGCTAATGGATAAAGGG ATCCTAGTTCATGGCGGTGTTGTGGACAAACATGCTACTTCCTATGCTTTTCACGGGCTG TCCCCTGGCTACCTCTACAACCTCACTGTTATGACTGAGGCTGCAGGGCTGCAAAACTAC AGGTGGAAACTAGTCAGGACAGCCCCCATGGAAGTCTCAAATCTGAAGGTGACAAATGAT GGCAGTTTGACCTCTCTAAAAGTCAAATGGCAAAGACCTCCTGGAAATGTGGATTCTTAC AATATCACCCTGTCTCACAAAGGGACCATCAAGGAATCCAGAGTATTAGCACCTTGGATT ACTGAAACTCACTTTAAAGAGTTAGTCCCCGGTCGACTTTATCAAGTTACTGTCAGCTGT GTCTCTGGTGAACTGTCTGCTCAGAAGATGGCAGTGGGCAGAACATTTCCAGACAAAGTT GCAAACCTGGAGGCAAACAATAATGGCAGGATGAGGTCTCTTGTAGTGAGCTGGTCGCCC CCTGCTGGAGACTGGGAGCAGTATCGGATCCTACTCTTCAATGATTCTGTGGTGCTGCTC AACATCACTGTGGGAAAGGAAGAAACACAGTATGTCATGGATGACACGGGGCTCGTACCG GGAAGACAGTATGAGGTGGAAGTCATTGTTGAGAGTGGAAATTTGAAGAATTCTGAGCGT TGCCAAGGCAGGACAGTCCCCCTGGCTGTCCTCCAGCTTCGTGTCAAACATGCCAATGAA ACCTCACTGAGTATCATGTGGCAGACCCCTGTAGCAGAATGGGAGAAATACATCATTTCC CTAGCTGACAGAGACCTCTTACTGATCCACAAGTCACTCTCCAAAGATGCCAAAGAATTC ACTTTTACTGACCTGGTGCCTGGACGAAAATACATGGCTACAGTCACCAGTATTAGTGGA GACTTAAAAAATTCCTCTTCAGTAAAAGGAAGAACAGTGCCTGCCCAAGTGACTGACTTG CATGTGGCCAACCAAGGAATGACCAGTAGTCTGTTTACTAACTGGACCCAGGCACAAGGA GACGTAGAATTTTACCAAGTCTTACTGATCCATGAAAATGTGGTCATTAAAAATGAAAGC ATCTCCAGTGAGACCAGCAGATACAGCTTCCACTCTCTCAAGTCCGGCAGCCTGTACTCC GTGGTGGTAACAACAGTGAGTGGAGGGATCTCTTCCCGACAAGTGGTTGTGGAGGGAAGA ACAGTCCCTTCCAGTGTGAGTGGAGTAACGGTGAACAATTCCGGTCGTAATGACTACCTC AGCGTTTCCTGGCTCGTGGCGCCCGGAGATGTGGATAACTATGAGGTAACATTGTCTCAT GACGGCAAGGTGGTTCAGTCCCTTGTCATTGCCAAGTCTGTCAGAGAATGTTCCTTCAGC TCCCTCACCCCAGGCCGCCTCTACACCGTGACCATAACTACAAGGAGTGGCAAGTATGAA AATCACTCCTTCAGCCAAGAGCGGACAGTGCCTGACAAAGTCCAGGGAGTCAGTGTTAGC AACTCAGCCAGGAGTGACTATTTAAGGGTATCCTGGGTGCATGCCACTGGAGACTTTGAT CACTATGAAGTCACCATTAAAAACAAAAACAACTTCATTCAAACTAAAAGCATTCCCAAG TCAGAAAACGAATGTGTATTTGTTCAGCTAGTCCCTGGACGGTTGTACAGTGTCACTGTT ACTACAAAAAGTGGACAATATGAAGCCAATGAACAAGGGAATGGGAGAACAATTCCAGAG CCTGTTAAGGATCTAACATTGCGCAACAGGAGCACTGAGGACTTGCATGTGACTTGGTCA GGAGCTAATGGGGATGTCGACCAATATGAGATCCAGCTGCTCTTCAATGACATGAAAGTA TTTCCTCCTTTTCACCTTGTAAATACCGCAACCGAGTATCGATTTACTTCCCTAACACCA GGCCGCCAATACAAAATTCTTGTCTTGACGATTAGCGGGGATGTACAGCAGTCAGCCTTC ATTGAGGGCTTCACAGTTCCTAGTGCTGTCAAAAATATTCACATTTCTCCCAATGGAGCA ACAGATAGCCTGACGGTGAACTGGACTCCTGGTGGGGGAGACGTTGATTCCTACACGGTG TCGGCATTCAGGCACAGTCAAAAGGTTGACTCTCAGACTATTCCCAAGCACGTCTTTGAG CACACGTTCCACAGACTGGAGGCCGGGGAGCAGTACCAGATCATGATTGCCTCAGTCAGC GGGTCCCTGAAGAATCAGATAAATGTGGTTGGGCGGACAGTTCCAGCATCTGTCCAAGGA GTAATTGCAGACAATGCATACAGCAGTTATTCCTTAATAGTAAGTTGGCAAAAAGCTGCT GGTGTGGCAGAAAGATATGATATCCTGCTTCTAACTGAAAATGGAATCCTTCTGCGCAAC ACATCAGAGCCAGCCACCACTAAGCAACACAAATTTGAAGATCTAACACCAGGCAAGAAA TACAAGATACAGATCCTAACTGTCAGTGGAGGCCTCTTTAGCAAGGAAGCCCAGACTGAA GGCCGAACAGTCCCAGCAGCTGTCACCGACCTGAGGATCACAGAGAACTCCACCAGGCAC CTGTCCTTCCGCTGGACCGCCTCAGAGGGGGAGCTCAGCTGGTACAACATCTTTTTGTAC AACCCAGATGGGAATCTCCAGGAGAGAGCTCAAGTTGACCCACTAGTCCAGAGCTTCTCT TTCCAGAACTTGCTACAAGGCAGAATGTACAAGATGGTGATTGTAACTCACAGTGGGGAG CTGTCTAATGAGTCTTTCATATTTGGTAGAACAGTCCCAGCCTCTGTGAGTCATCTCAGG GGGTCCAATCGGAACACGACAGACAGCCTTTGGTTCAACTGGAGTCCAGCCTCTGGGGAC TTTGACTTTTATGAGCTGATTCTCTATAATCCCAATGGCACAAAGAAGGAAAACTGGAAA GACAAGGACCTGACGGAGTGGCGGTTTCAAGGCCTTGTTCCTGGAAGGAAGTACGTGCTG TGGGTGGTAACTCACAGTGGAGATCTCAGCAATAAAGTCACAGCGGAGAGCAGAACAGCT CCAAGTCCTCCCAGTCTTATGTCATTTGCTGACATTGCAAACACATCCTTGGCCATCACG TGGAAAGGGCCCCCAGACTGGACAGACTACAACGACTTTGAGCTGCAGTGGTTGCCCAGA GATGCACTTACTGTCTTCAACCCCTACAACAACAGAAAATCAGAAGGACGCATTGTGTAT GGTCTTCGTCCAGGGAGATCCTATCAATTCAACGTCAAGACTGTCAGTGGTGATTCCTGG AAAACTTACAGCAAACCAATTTTTGGATCTGTGAGGACAAAGCCTGACAAGATACAAAAC CTGCATTGCCGGCCTCAGAACTCCACGGCCATTGCCTGTTCTTGGATCCCTCCTGATTCT GACTTTGATGGTTATAGTATTGAATGCCGGAAAATGGACACCCAAGAAGTTGAGTTTTCC AGAAAGCTGGAGAAAGAAAAATCTCTGCTCAACATCATGATGCTAGTGCCCCATAAGAGG TACCTGGTGTCCATCAAAGTGCAGTCGGCCGGCATGACCAGCGAGGTGGTTGAAGACAGC ACTATCACAATGATAGACCGCCCCCCTCCTCCACCCCCACACATTCGTGTGAATGAAAAG GATGTGCTAATTAGCAAGTCTTCCATCAACTTTACTGTCAACTGCAGCTGGTTCAGCGAC ACCAATGGAGCTGTGAAATACTTCACAGTGGTGGTGAGAGAGGCTGATGGCAGTGATGAG CTGAAGCCAGAACAGCAGCACCCTCTCCCTTCCTACCTGGAGTACAGGCACAATGCCTCC ATTCGGGTGTATCAGACTAATTATTTTGCCAGCAAATGTGCCGAAAATCCTAACAGCAAC TCCAAGAGTTTTAACATTAAGCTTGGAGCAGAGATGGAGAGCTTAGGTGGAAAACGCGAT CCCACTCAGCAAAAATTCTGTGATGGACCACTGAAGCCACACACTGCCTACAGAATCAGC ATTCGAGCTTTTACACAGCTCTTTGATGAGGACCTGAAGGAATTCACAAAGCCACTCTAT TCAGACACATTTTTTTCTTTACCCATCACTACTGAATCAGAGCCCTTGTTTGGAGCTATT GAAGGTGTGAGTGCTGGTCTGTTTTTAATTGGCATGCTAGTGGCTGTTGTTGCCTTATTG ATCTGCAGACAGAAAGTGAGCCATGGTCGAGAAAGACCCTCTGCCCGTCTGAGCATTCGT AGGGATCGACCATTATCTGTCCACTTAAACCTGGGCCAGAAAGGTAACCGGAAAACTTCT TGTCCAATAAAAATAAATCAGTTTGAAGGGCATTTCATGAAGCTACAGGCTGACTCCAAC TACCTTCTATCCAAGGAATACGAGGAGTTAAAAGACGTGGGCCGAAACCAGTCATGTGAC ATTGCACTCTTGCCGGAGAATAGAGGGAAAAATCGATACAACAATATATTGCCCTATGAT GCCACGCGAGTGAAGCTCTCCAATGTAGATGATGATCCTTGCTCTGACTACATCAATGCC AGCTACATCCCTGGCAACAACTTCAGAAGAGAATACATTGTCACTCAGGGACCGCTTCCT GGCACCAAGGATGACTTCTGGAAAATGGTGTGGGAACAAAACGTTCACAACATCGTCATG GTGACCCAGTGTGTTGAGAAGGGCCGAGTAAAGTGTGACCATTACTGGCCAGCGGACCAG GATTCCCTCTACTATGGGGACCTCATCCTGCAGATGCTCTCAGAGTCCGTCCTGCCTGAG TGGACCATCCGGGAGTTTAAGATATGCGGTGAGGAACAGCTTGATGCACACAGACTCATC CGCCACTTTCACTATACGGTGTGGCCAGACCATGGAGTCCCAGAAACCACCCAGTCTCTG ATCCAGTTTGTGAGAACTGTCAGGGACTACATCAACAGAAGCCCGGGTGCTGGGCCCACT GTGGTGCACTGCAGTGCTGGTGTGGGTAGGACTGGAACCTTTATTGCATTGGACCGAATC CTCCAGCAGTTAGACTCCAAAGACTCTGTGGACATTTATGGAGCAGTGCACGACCTAAGA CTTCACAGGGTTCACATGGTCCAGACTGAGTGTCAGTATGTCTACCTACATCAGTGTGTA AGAGATGTCCTCAGAGCAAGAAAGCTACGGAGTGAACAAGAAAACCCCTTGTTTCCAATC TATGAAAATGTGAATCCAGAGTATCACAGAGATCCAGTCTATTCAAGGCATTGA PF00041 fn3 PF00102 Y_phosphatase function hydrolase activity, acting on ester bonds function phosphoric ester hydrolase activity function phosphoric monoester hydrolase activity function phosphoprotein phosphatase activity function catalytic activity function protein tyrosine phosphatase activity function hydrolase activity process biopolymer metabolism process biopolymer modification process protein modification process physiological process process metabolism process protein amino acid dephosphorylation process macromolecule metabolism "
drug:{4-[2-BENZYL-3-METHOXY-2-(METHOXYCARBONYL)-3-OXOPROPYL]PHENYL}SULFAMIC ACIDrdfs:label"{4-[2-BENZYL-3-METHOXY-2-(METHOXYCARBONYL)-3-OXOPROPYL]PHENYL}SULFAMIC ACID"
drug:{4-[2-BENZYL-3-METHOXY-2-(METHOXYCARBONYL)-3-OXOPROPYL]PHENYL}SULFAMIC ACIDrdf:typedrugbank:drugs
drug:{4-[3-(4-acetyl-3-hydroxy-2-propylphenoxy)propoxy]phenoxy}acetic aciddrugbank:description" experimental This compound belongs to the phenoxyacetic acid derivatives. These are compounds containing an anisole where the methane group is linked to an acetic acid or a derivative. Phenoxyacetic Acid Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Phenoxyacetic Acid Derivatives Acetophenones Phenol Ethers Benzoyl Derivatives Alkyl Aryl Ethers Phenols and Derivatives Polyols Ketones Enolates Carboxylic Acids Polyamines Enols acetophenone phenol ether benzoyl alkyl aryl ether phenol derivative ketone polyol ether carboxylic acid carboxylic acid derivative polyamine enol enolate carbonyl group logP 3.88 ALOGPS logS -4.7 ALOGPS Water Solubility 7.86e-03 g/l ALOGPS logP 4.15 ChemAxon IUPAC Name 2-{4-[3-(4-acetyl-3-hydroxy-2-propylphenoxy)propoxy]phenoxy}acetic acid ChemAxon Traditional IUPAC Name 4-[3-(4-acetyl-3-hydroxy-2-propylphenoxy)propoxy]phenoxyacetic acid ChemAxon Molecular Weight 402.4376 ChemAxon Monoisotopic Weight 402.167853186 ChemAxon SMILES CCCC1=C(OCCCOC2=CC=C(OCC(O)=O)C=C2)C=CC(C(C)=O)=C1O ChemAxon Molecular Formula C22H26O7 ChemAxon InChI InChI=1S/C22H26O7/c1-3-5-19-20(11-10-18(15(2)23)22(19)26)28-13-4-12-27-16-6-8-17(9-7-16)29-14-21(24)25/h6-11,26H,3-5,12-14H2,1-2H3,(H,24,25) ChemAxon InChIKey InChIKey=HBBVCKCCQCQCTJ-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 102.29 ChemAxon Refractivity 107.11 ChemAxon Polarizability 42.84 ChemAxon Rotatable Bond Count 12 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 3.28 ChemAxon pKa (strongest basic) -3.9 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 6603901 PubChem Substance 99444549 ChemSpider 5036209 PDB L41 IUPHAR 2691 Guide to Pharmacology 2691 BE0001007 Peroxisome proliferator-activated receptor delta Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Peroxisome proliferator-activated receptor delta Involved in DNA binding Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Decreases expression of NPC1L1 once activated by a ligand PPARD 6p21.2-p21.1 Nucleus None 7.65 49904.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9235 GenAtlas PPARD GeneCards PPARD GenBank Gene Database L07592 GenBank Protein Database 190230 IUPHAR 594 Guide to Pharmacology 86 UniProtKB Q03181 UniProt Accession PPARD_HUMAN NUC1 NUCI Nuclear hormone receptor 1 PPAR- beta PPAR-delta >Peroxisome proliferator-activated receptor delta MEQPQEEAPEVREEEEKEEVAEAEGAPELNGGPQHALPSSSYTDLSRSSSPPSLLDQLQM GCDGASCGSLNMECRVCGDKASGFHYGVHACEGCKGFFRRTIRMKLEYEKCERSCKIQKK NRNKCQYCRFQKCLALGMSHNAIRFGRMPEAEKRKLVAGLTANEGSQYNPQVADLKAFSK HIYNAYLKNFNMTKKKARSILTGKASHTAPFVIHDIETLWQAEKGLVWKQLVNGLPPYKE ISVHVFYRCQCTTVETVRELTEFAKSIPSFSSLFLNDQVTLLKYGVHEAIFAMLASIVNK DGLLVANGSGFVTREFLRSLRKPFSDIIEPKFEFAVKFNALELDDSDLALFIAAIILCGD RPGLMNVPRVEAIQDTILRALEFHLQANHPDAQYLFPKLLQKMADLRQLVTEHAQMMQRI KKTETETSLHPLLQEIYKDMY >1326 bp ATGGAGCAGCCACAGGAGGAAGCCCCTGAGGTCCGGGAAGAGGAGGAGAAAGAGGAAGTG GCAGAGGCAGAAGGAGCCCCAGAGCTCAATGGGGGACCACAGCATGCACTTCCTTCCAGC AGCTACACAGACCTCTCCCGGAGCTCCTCGCCACCCTCACTGCTGGACCAACTGCAGATG GGCTGTGACGGGGCCTCATGCGGCAGCCTCAACATGGAGTGCCGGGTGTGCGGGGACAAG GCATCGGGCTTCCACTACGGTGTTCATGCATGTGAGGGGTGCAAGGGCTTCTTCCGTCGT ACGATCCGCATGAAGCTGGAGTACGAGAAGTGTGAGCGCAGCTGCAAGATTCAGAAGAAG AACCGCAACAAGTGCCAGTACTGCCGCTTCCAGAAGTGCCTGGCACTGGGCATGTCACAC AACGCTATCCGTTTTGGTCGGATGCCGGAGGCTGAGAAGAGGAAGCTGGTGGCAGGGCTG ACTGCAAACGAGGGGAGCCAGTACAACCCACAGGTGGCCGACCTGAAGGCCTTCTCCAAG CACATCTACAATGCCTACCTGAAAAACTTCAACATGACCAAAAAGAAGGCCCGCAGCATC CTCACCGGCAAAGCCAGCCACACGGCGCCCTTTGTGATCCACGACATCGAGACATTGTGG CAGGCAGAGAAGGGGCTGGTGTGGAAGCAGTTGGTGAATGGCCTGCCTCCCTACAAGGAG ATCAGCGTGCACGTCTTCTACCGCTGCCAGTGCACCACAGTGGAGACCGTGCGGGAGCTC ACTGAGTTCGCCAAGAGCATCCCCAGCTTCAGCAGCCTCTTCCTCAACGACCAGGTTACC CTTCTCAAGTATGGCGTGCACGAGGCCATCTTCGCCATGCTGGCCTCTATCGTCAACAAG GACGGGCTGCTGGTAGCCAACGGCAGTGGCTTTGTCACCCGTGAGTTCCTGCGCAGCCTC CGCAAACCCTTCAGTGATATCATTGAGCCTAAGTTTGAATTTGCTGTCAAGTTCAACGCC CTGGAACTTGATGACAGTGACCTGGCCCTATTCATTGCGGCCATCATTCTGTGTGGAGAC CGGCCAGGCCTCATGAACGTTCCACGGGTGGAGGCTATCCAGGACACCATCCTGCGTGCC CTCGAATTCCACCTGCAGGCCAACCACCCTGATGCCCAGTACCTCTTCCCCAAGCTGCTG CAGAAGATGGCTGACCTGCGGCAACTGGTCACCGAGCACGCCCAGATGATGCAGCGGATC AAGAAGACCGAAACCGAGACCTCGCTGCACCCTCTGCTCCAGGAGATCTACAAGGACATG TACTAA PF00104 Hormone_recep PF00105 zf-C4 component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function transcription factor activity function ligand-dependent nuclear receptor activity function DNA binding function binding function signal transducer activity function receptor activity function nucleic acid binding function steroid hormone receptor activity process regulation of biological process process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent "
drug:{4-[3-(4-acetyl-3-hydroxy-2-propylphenoxy)propoxy]phenoxy}acetic acidrdfs:label"{4-[3-(4-acetyl-3-hydroxy-2-propylphenoxy)propoxy]phenoxy}acetic acid"
drug:{4-[3-(4-acetyl-3-hydroxy-2-propylphenoxy)propoxy]phenoxy}acetic acidrdf:typedrugbank:drugs
drug:{4-[3-(6,7-Diethoxy-Quinazolin-4-Ylamino)-Phenyl]-Thiazol-2-Yl}-Methanoldrugbank:description" experimental This compound belongs to the phenylthiazoles. These are compounds containing a phenylthiazole moiety, which consists of an thiazole ring attacthed to a phenyl group. Phenylthiazoles Organic Compounds Heterocyclic Compounds Azoles Thiazoles Quinazolinamines Phenol Ethers Alkyl Aryl Ethers Aminopyrimidines and Derivatives 2,4-disubstituted Thiazoles Polyamines Primary Alcohols Secondary Amines phenol ether aminopyrimidine 2,4-disubstituted 1,3-thiazole alkyl aryl ether benzene pyrimidine primary alcohol secondary amine ether polyamine alcohol organonitrogen compound amine logP 4.37 ALOGPS logS -5.1 ALOGPS Water Solubility 3.12e-03 g/l ALOGPS logP 3.86 ChemAxon IUPAC Name (4-{3-[(6,7-diethoxyquinazolin-4-yl)amino]phenyl}-1,3-thiazol-2-yl)methanol ChemAxon Traditional IUPAC Name (4-{3-[(6,7-diethoxyquinazolin-4-yl)amino]phenyl}-1,3-thiazol-2-yl)methanol ChemAxon Molecular Weight 422.5 ChemAxon Monoisotopic Weight 422.14126128 ChemAxon SMILES CCOC1=C(OCC)C=C2C(NC3=CC=CC(=C3)C3=CSC(CO)=N3)=NC=NC2=C1 ChemAxon Molecular Formula C22H22N4O3S ChemAxon InChI InChI=1S/C22H22N4O3S/c1-3-28-19-9-16-17(10-20(19)29-4-2)23-13-24-22(16)25-15-7-5-6-14(8-15)18-12-30-21(11-27)26-18/h5-10,12-13,27H,3-4,11H2,1-2H3,(H,23,24,25) ChemAxon InChIKey InChIKey=ZJESXGUODSBHSK-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 89.39 ChemAxon Refractivity 116.14 ChemAxon Polarizability 46.55 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 13.63 ChemAxon pKa (strongest basic) 4.61 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 5740 PubChem Substance 46505789 ChemSpider 5538 PDB PFE BE0002431 Fructose-1,6-bisphosphatase 1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Fructose-1,6-bisphosphatase 1 Involved in phosphoric ester hydrolase activity D-fructose 1,6-bisphosphate + H(2)O = D- fructose 6-phosphate + phosphate FBP1 9q22.3 Cytoplasmic None 6.99 36815.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3606 GenAtlas FBP1 GenBank Gene Database L10320 UniProtKB P09467 UniProt Accession F16P1_HUMAN D-fructose-1,6- bisphosphate 1-phosphohydrolase 1 EC 3.1.3.11 FBPase 1 >Fructose-1,6-bisphosphatase 1 MADQAPFDTDVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGI AGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDP LDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMDC GVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKDFDPAVTEYIQRKKFPPDNSAP YGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGK EAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHSAQ >1017 bp ATGGCTGACCAGGCGCCCTTCGACACGGACGTCAACACCCTGACCCGCTTCGTCATGGAG GAGGGCAGGAAGGCCCGCGGCACGGGCGAGTTGACCCAGCTGCTCAACTCGCTCTGCACA GCAGTCAAAGCCATCTCTTCGGCGGTGCGCAAGGCGGGCATCGCGCACCTCTATGGCATT GCTGGTTCTACCAACGTGACAGGTGATCAAGTTAAGAAGCTGGACGTCCTCTCCAACGAC CTGGTTATGAACATGTTAAAGTCATCCTTTGCCACGTGTGTTCTCGTGTCAGAAGAAGAT AAACACGCCATCATAGTGGAACCGGAGAAAAGGGGTAAATATGTGGTCTGTTTTGATCCC CTTGATGGATCTTCCAACATCGATTGCCTTGTGTCCGTTGGAACCATTTTTGGCATCTAT AGAAAGAAATCAACTGATGAGCCTTCTGAGAAGGATGCTCTGCAACCAGGCCGGAACCTG GTGGCAGCCGGCTACGCACTGTATGGCAGTGCCACCATGCTGGTCCTTGCCATGGACTGT GGGGTCAACTGCTTCATGCTGGACCCGGCCATCGGGGAGTTCATTTTGGTGGACAAGGAT GTGAAGATAAAAAAGAAAGGTAAAATCTACAGCCTTAACGAGGCGTACGCTAAGGACTTT GACCCTGCCGTCACTGAGTACATCCAGAGGAAGAAGTTCCCCCCAGATAATTCAGCTCCT TATGGGGCCCGGTATGTGGGCTCCATGGTGGCTGATGTTCATCGCACTCTGGTCTACGGA GGGATATTTCTGTACCCCGCTAACAAGAAGAGCCCCAATGGAAAGCTGAGACTGCTGTAC GAATGCAACCCCATGGCCTACGTCATGGAGAAGGCTGGGGGAATGGCCACCACTGGGAAG GAGGCCGTGTTAGACGTCATTCCCACAGACATTCACCAGAGGGCGCCGGTGATCTTGGGG TCCCCCGACGACGTGCTCGAGTTCCTGAAGGTGTATGAGAAGCACTCTGCCCAGTGA PF00316 FBPase function hydrolase activity, acting on ester bonds function phosphoric ester hydrolase activity function catalytic activity function hydrolase activity process carbohydrate metabolism process physiological process process metabolism process macromolecule metabolism "
drug:{4-[3-(6,7-Diethoxy-Quinazolin-4-Ylamino)-Phenyl]-Thiazol-2-Yl}-Methanolrdfs:label"{4-[3-(6,7-Diethoxy-Quinazolin-4-Ylamino)-Phenyl]-Thiazol-2-Yl}-Methanol"
drug:{4-[3-(6,7-Diethoxy-Quinazolin-4-Ylamino)-Phenyl]-Thiazol-2-Yl}-Methanolowl:sameAsdrug:EXPT02557
drug:{4-[3-(6,7-Diethoxy-Quinazolin-4-Ylamino)-Phenyl]-Thiazol-2-Yl}-Methanolrdf:typedrugbank:drugs
drug:{4-[4-hydroxy-3-(1-methylethyl)benzyl]-3,5-dimethylphenoxy}acetic aciddrugbank:description" experimental This compound belongs to the diphenylmethanes. These are compounds containing a diphenylmethane moiety, which consists of a methane wherein two hydrogen atoms are replaced by two phenyl groups. Diphenylmethanes Organic Compounds Benzenoids Benzene and Substituted Derivatives Diphenylmethanes Phenoxyacetic Acid Derivatives Cumenes Phenol Ethers Toluenes Phenols and Derivatives Alkyl Aryl Ethers Polyols Enols Polyamines Carboxylic Acids Enolates phenoxyacetate cumene phenol ether toluene alkyl aryl ether phenol derivative polyol polyamine enol ether carboxylic acid carboxylic acid derivative enolate logP 4.23 ALOGPS logS -5.1 ALOGPS Water Solubility 2.61e-03 g/l ALOGPS logP 5.35 ChemAxon IUPAC Name 2-(4-{[4-hydroxy-3-(propan-2-yl)phenyl]methyl}-3,5-dimethylphenoxy)acetic acid ChemAxon Traditional IUPAC Name 4-[(4-hydroxy-3-isopropylphenyl)methyl]-3,5-dimethylphenoxyacetic acid ChemAxon Molecular Weight 328.4022 ChemAxon Monoisotopic Weight 328.167459256 ChemAxon SMILES CC(C)C1=C(O)C=CC(CC2=C(C)C=C(OCC(O)=O)C=C2C)=C1 ChemAxon Molecular Formula C20H24O4 ChemAxon InChI InChI=1S/C20H24O4/c1-12(2)17-9-15(5-6-19(17)21)10-18-13(3)7-16(8-14(18)4)24-11-20(22)23/h5-9,12,21H,10-11H2,1-4H3,(H,22,23) ChemAxon InChIKey InChIKey=QNAZTOHXCZPOSA-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 66.76 ChemAxon Refractivity 94.6 ChemAxon Polarizability 36.6 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 3.93 ChemAxon pKa (strongest basic) -4.9 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Ghose Filter true ChemAxon PubChem Compound 9862248 PubChem Substance 99443896 ChemSpider 8037944 PDB B72 IUPHAR 2639 Guide to Pharmacology 2639 BE0003867 Thyroid hormone receptor, alpha isoform 1 variant Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Thyroid hormone receptor, alpha isoform 1 variant Involved in protein heterodimerization activity Cytoplasmic None 7.97 45440.1 Human HUGO Gene Nomenclature Committee (HGNC) GNC:11796 GenBank Gene Database AB209346 GenBank Protein Database 62088272 UniProtKB Q59FW3 UniProt Accession Q59FW3_HUMAN >Thyroid hormone receptor, alpha isoform 1 variant SEWNSARSPDGKRKRKNGQCSLKTSMSGYIPSYLDKDEQCVVCGDKATGYHYRCITCEGC KGFFRRTIQKNLHPTYSCKYDSCCVIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVA KRKLIEQNRERRRKEEMIRSLQQRPEPTPEEWDLIHIATEAHRSTNAQGSHWKQRRKFLP DDIGQSPIVSMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKG CCMEIMSLRAAVRYDPESDTLTLSGEMAVKREQLKNGGLGVVSDAIFELGKSLSAFNLDD TEVALLQAVLLMSTDRSGLLCVDKIEKSQEAYLLAFEHYVNHRKHNIPHFWPKLLMKVTD LRMIGACHASRFLHMKVECPTELFPPLFLEVFEDQEV PF00104 Hormone_recep PF00105 zf-C4 component nucleus component organelle component membrane-bound organelle component intracellular membrane-bound organelle function receptor activity function nucleic acid binding function steroid hormone receptor activity function transcription factor activity function thyroid hormone receptor activity function ligand-dependent nuclear receptor activity function DNA binding function binding function signal transducer activity process regulation of transcription process regulation of transcription, DNA-dependent process regulation of biological process process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism BE0000315 Thyroid hormone receptor beta Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Thyroid hormone receptor beta Involved in transcription factor activity High affinity receptor for triiodothyronine THRB 3p24.2 Nucleus None 7.11 52788.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:11799 GenAtlas THRB GeneCards THRB GenBank Gene Database X04707 GenBank Protein Database 31207 IUPHAR 589 Guide to Pharmacology 84 UniProtKB P10828 UniProt Accession THB_HUMAN >Thyroid hormone receptor beta-1 MTPNSMTENGLTAWDKPKHCPDREHDWKLVGMSEACLHRKSHSERRSTLKNEQSSPHLIQ TTWTSSIFHLDHDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYR CITCEGCKGFFRRTIQKNLHPSYSCKYEGKCVIDKVTRNQCQECRFKKCIYVGMATDLVL DDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWK QKRKFLPEDIGQAPIVNAPEGGKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCED QIILLKGCCMEIMSLRAAVRYDPESETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSL SSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKYQDSFLLAFEHYINYRKHHVTHFWPK LLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED >1371 bp ATGACAGAAAATGGCCTTACAGCTTGGGACAAACCGAAGCACTGTCCAGACCGAGAACAC GACTGGAAGCTAGTAGGAATGTCTGAAGCCTGCCTACATAGGAAGAGCCATTCAGAGAGG CGCAGCACGTTGAAAAATGAACAGTCGTCGCCACATCTCATCCAGACCACTTGGACTAGC TCAATATTCCATCTGGACCATGATGATGTGAACGACCAGAGTGTCTCAAGTGCCCAGACC TTCCAAACGGAGGAGAAGAAATGTAAAGGGTACATCCCCAGTTACTTAGACAAGGACGAG CTCTGTGTAGTGTGTGGTGACAAAGCCACCGGGTATCACTACCGCTGTATCACGTGTGAA GGCTGCAAGGGTTTCTTTAGAAGAACCATTCAGAAAAATCTCCATCCATCCTATTCCTGT AAATATGAAGGAAAATGTGTCATAGACAAAGTCACGCGAAATCAGTGCCAGGAATGTCGC TTTAAGAAATGCATCTATGTTGGCATGGCAACAGATTTGGTGCTGGATGACAGCAAGAGG CTGGCCAAGAGGAAGCTGATAGAGGAGAACCGGGAGAAAAGACGGCGGGAAGAGCTGCAG AAGTCCATCGGGCACAAGCCAGAGCCCACAGACGAGGAATGGGAGCTCATCAAAACTGTC ACCGAAGCCCATGTGGCGACCAACGCCCAAGGCAGCCACTGGAAGCAAAAACCGAAATTT CTGCCAGAAGACATTGGACAAGCACCAATAGTCAATGCCCCAGAAGGTGGAAAGGTTGAC TTGGAAGCCTTCAGCCATTTTACAAAAATCATCACACCAGCAATTACCAGAGTGGTGGAT TTTGCCAAAAAGTTGCCTATGTTTTGTGAGCTGCCATGTGAAGACCAGATCATCCTCCTC AAAGGCTGCTGCATGGAGATCATGTCCCTTCGCGCTGCTGTGCGCTATGACCCGGAAAGT GAGACTTTAACCTTGAATGGGGAAATGGCAGTGATACGGGGCCAGCTGAAAAATGGGGGT CTTGGGGTGGTGTCAGACGCCATCTTTGACCTAGGCATGTCTCTGTCTTCTTTCAACCTG GATGACACTGAAGTAGCCCTCCTTCAGGCCGTCCTGCTGATGTCTTCAGATCGCCCGGGG CTTGCCTGTGTTGAGAGAATAGAAAAGTACCAAGATAGTTTCCTGCTGGCCTTTGAACAC TATATCAATTACCGAAAACACCACGTGACACACTTTTGGCCAAAACTCCTGATGAAGGTG ACAGATCTGCGGATGATAGGAGCCTGCCATGCCAGCCGCTTCCTGCACATGAAGGTGGAA TGCCCCACAGAACTCCTCCCCCCTTTGTTCCTGGAAGTGTTCGAGGATTAG PF00104 Hormone_recep PF00105 zf-C4 component organelle component membrane-bound organelle component intracellular membrane-bound organelle component nucleus function signal transducer activity function receptor activity function nucleic acid binding function steroid hormone receptor activity function transcription factor activity function thyroid hormone receptor activity function ligand-dependent nuclear receptor activity function DNA binding function binding process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent process regulation of biological process "
drug:{4-[4-hydroxy-3-(1-methylethyl)benzyl]-3,5-dimethylphenoxy}acetic acidrdfs:label"{4-[4-hydroxy-3-(1-methylethyl)benzyl]-3,5-dimethylphenoxy}acetic acid"
drug:{4-[4-hydroxy-3-(1-methylethyl)benzyl]-3,5-dimethylphenoxy}acetic acidrdf:typedrugbank:drugs
drug:{5-(5-AMINO-1H-PYRROLO[3,2-B]PYRIDIN-2-YL)-6-HYDROXY-3'-NITRO-BIPHENYL-3-YL]-ACETIC ACIDdrugbank:description" experimental This compound belongs to the biphenyls and derivatives. These are organic compounds containing to benzene rings linked together by a C-C bond. Biphenyls and Derivatives Organic Compounds Benzenoids Benzene and Substituted Derivatives Biphenyls and Derivatives Phenylpyrroles Phenylacetic Acid Derivatives Nitrobenzenes Pyrrolopyridines Phenols and Derivatives Aminopyridines and Derivatives Primary Aromatic Amines Polyols Nitronic Acids Nitro Compounds Polyamines Enols Enolates Carboxylic Acids Organic Oxoazanium Compounds phenylacetate nitrobenzene pyrrolopyridine aminopyridine phenol derivative pyridine primary aromatic amine substituted pyrrole pyrrole nitronic acid polyol nitro compound enolate carboxylic acid derivative polyamine organic oxoazanium carboxylic acid enol organonitrogen compound primary amine amine logP 3.59 ALOGPS logS -4.3 ALOGPS Water Solubility 1.85e-02 g/l ALOGPS logP 1.62 ChemAxon IUPAC Name 2-(3-{5-amino-1H-pyrrolo[3,2-b]pyridin-2-yl}-4-hydroxy-5-(3-nitrophenyl)phenyl)acetic acid ChemAxon Traditional IUPAC Name (3-{5-amino-1H-pyrrolo[3,2-b]pyridin-2-yl}-4-hydroxy-5-(3-nitrophenyl)phenyl)acetic acid ChemAxon Molecular Weight 404.3755 ChemAxon Monoisotopic Weight 404.112069642 ChemAxon SMILES NC1=CC=C2NC(=CC2=N1)C1=CC(CC(O)=O)=CC(=C1O)C1=CC=CC(=C1)[N+]([O-])=O ChemAxon Molecular Formula C21H16N4O5 ChemAxon InChI InChI=1S/C21H16N4O5/c22-19-5-4-16-18(24-19)10-17(23-16)15-7-11(8-20(26)27)6-14(21(15)28)12-2-1-3-13(9-12)25(29)30/h1-7,9-10,23,28H,8H2,(H2,22,24)(H,26,27) ChemAxon InChIKey InChIKey=BVBGZXXLVHYBKI-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 158.05 ChemAxon Refractivity 110.39 ChemAxon Polarizability 41.28 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 7 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 3.79 ChemAxon pKa (strongest basic) 5.98 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 10135836 PubChem Substance 99444703 ChemSpider 20136275 PDB N1H BE0000333 Coagulation factor VII Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Coagulation factor VII Involved in calcium ion binding Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium F7 13q34 Cytoplasmic None 7.23 51594.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3544 GenAtlas F7 GeneCards F7 GenBank Gene Database M13232 GenBank Protein Database 182801 UniProtKB P08709 UniProt Accession FA7_HUMAN Coagulation factor VII precursor EC 3.4.21.21 Eptacog alfa Proconvertin Serum prothrombin conversion accelerator SPCA >Coagulation factor VII precursor MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRR ANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGS CKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSL LADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGG TLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTN HDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVL NVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTG IVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP >1401 bp ATGGTCTCCCAGGCCCTCAGGCTCCTCTGCCTTCTGCTTGGGCTTCAGGGCTGCCTGGCT GCAGGCGGGGTCGCTAAGGCCTCAGGAGGAGAAACACGGGACATGCCGTGGAAGCCGGGG CCTCACAGAGTCTTCGTAACCCAGGAGGAAGCCCACGGCGTCCTGCACCGGCGCCGGCGC GCCAACGCGTTCCTGGAGGAGCTGCGGCCGGGCTCCCTGGAGAGGGAGTGCAAGGAGGAG CAGTGCTCCTTCGAGGAGGCCCGGGAGATCTTCAAGGACGCGGAGAGGACGAAGCTGTTC TGGATTTCTTACAGTGATGGGGACCAGTGTGCCTCAAGTCCATGCCAGAATGGGGGCTCC TGCAAGGACCAGCTCCAGTCCTATATCTGCTTCTGCCTCCCTGCCTTCGAGGGCCGGAAC TGTGAGACGCACAAGGATGACCAGCTGATCTGTGTGAACGAGAACGGCGGCTGTGAGCAG TACTGCAGTGACCACACGGGCACCAAGCGCTCCTGTCGGTGCCACGAGGGGTACTCTCTG CTGGCAGACGGGGTGTCCTGCACACCCACAGTTGAATATCCATGTGGAAAAATACCTATT CTAGAAAAAAGAAATGCCAGCAAACCCCAAGGCCGAATTGTGGGGGGCAAGGTGTGCCCC AAAGGGGAGTGTCCATGGCAGGTCCTGTTGTTGGTGAATGGAGCTCAGTTGTGTGGGGGG ACCCTGATCAACACCATCTGGGTGGTCTCCGCGGCCCACTGTTTCGACAAAATCAAGAAC TGGAGGAACCTGATCGCGGTGCTGGGCGAGCACGACCTCAGCGAGCACGACGGGGATGAG CAGAGCCGGCGGGTGGCGCAGGTCATCATCCCCAGCACGTACGTCCCGGGCACCACCAAC CACGACATCGCGCTGCTCCGCCTGCACCAGCCCGTGGTCCTCACTGACCATGTGGTGCCC CTCTGCCTGCCCGAACGGACGTTCTCTGAGAGGACGCTGGCCTTCGTGCGCTTCTCATTG GTCAGCGGCTGGGGCCAGCTGCTGGACCGTGGCGCCACGGCCCTGGAGCTCATGGTGCTC AACGTGCCCCGGCTGATGACCCAGGACTGCCTGCAGCAGTCACGGAAGGTGGGAGACTCC CCAAATATCACGGAGTACATGTTCTGTGCCGGCTACTCGGATGGCAGCAAGGACTCCTGC AAGGGGGACAGTGGAGGCCCACATGCCACCCACTACCGGGGCACGTGGTACCTGACGGGC ATCGTCAGCTGGGGCCAGGGCTGCGCAACCGTGGGCCACTTTGGGGTGTACACCAGGGTC TCCCAGTACATCGAGTGGCTGCAAAAGCTCATGCGCTCAGAGCCACGCCCAGGAGTCCTC CTGCGAGCCCCATTTCCCTAG PF00008 EGF PF00594 Gla PF00089 Trypsin component extracellular region function endopeptidase activity function ion binding function serine-type endopeptidase activity function cation binding function binding function catalytic activity function calcium ion binding function hydrolase activity function peptidase activity process macromolecule metabolism process proteolysis process protein metabolism process cellular protein metabolism process organismal physiological process process regulation of body fluids process physiological process process hemostasis process blood coagulation process metabolism BE0001178 Tissue factor Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Tissue factor Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade F3 1p22-p21 Membrane; single-pass type I membrane protein 252-274 7.09 33068.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:3541 GenAtlas F3 GeneCards F3 GenBank Gene Database M16553 GenBank Protein Database 339504 UniProtKB P13726 UniProt Accession TF_HUMAN CD142 antigen Coagulation factor III TF Thromboplastin Tissue factor precursor >Tissue factor precursor METPAWPRVPRPETAVARTLLLGWVFAQVAGASGTTNTVAAYNLTWKSTNFKTILEWEPK PVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTGS AGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFG KDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVE CMGQEKGEFREIFYIIGAVVFVVIILVIILAISLHKCRKAGVGQSWKENSPLNVS >888 bp ATGGAGACCCCTGCCTGGCCCCGGGTCCCGCGCCCCGAGACCGCCGTCGCTCGGACGCTC CTGCTCGGCTGGGTCTTCGCCCAGGTGGCCGGCGCTTCAGGCACTACAAATACTGTGGCA GCATATAATTTAACTTGGAAATCAACTAATTTCAAGACAATTTTGGAGTGGGAACCCAAA CCCGTCAATCAAGTCTACACTGTTCAAATAAGCACTAAGTCAGGAGATTGGAAAAGCAAA TGCTTTTACACAACAGACACAGAGTGTGACCTCACCGACGAGATTGTGAAGGATGTGAAG CAGACGTACTTGGCACGGGTCTTCTCCTACCCGGCAGGGAATGTGGAGAGCACCGGTTCT GCTGGGGAGCCTCTGTATGAGAACTCCCCAGAGTTCACACCTTACCTGGAGACAAACCTC GGACAGCCAACAATTCAGAGTTTTGAACAGGTGGGAACAAAAGTGAATGTGACCGTAGAA GATGAACGGACTTTAGTCAGAAGGAACAACACTTTCCTAAGCCTCCGGGATGTTTTTGGC AAGGACTTAATTTATACACTTTATTATTGGAAATCTTCAAGTTCAGGAAAGAAAACAGCC AAAACAAACACTAATGAGTTTTTGATTGATGTGGATAAAGGAGAAAACTACTGTTTCAGT GTTCAAGCAGTGATTCCCTCCCGAACAGTTAACCGGAAGAGTACAGACAGCCCGGTAGAG TGTATGGGCCAGGAGAAAGGGGAATTCAGAGAAATATTCTACATCATTGGAGCTGTGGCA TTTGTGGTCATCATCCTTGTCATCATCCTGGCTATATCTCTACACAAGTGTAGAAAGGCA GGAGTGGGGCAGAGCTGGAAGGAGAACTCCCCACTGAATGTTTCATAA PF01108 Tissue_fac component intrinsic to membrane component integral to membrane component membrane component cell process organismal physiological process process regulation of body fluids process hemostasis process blood coagulation process physiological process "
drug:{5-(5-AMINO-1H-PYRROLO[3,2-B]PYRIDIN-2-YL)-6-HYDROXY-3'-NITRO-BIPHENYL-3-YL]-ACETIC ACIDrdfs:label"{5-(5-AMINO-1H-PYRROLO[3,2-B]PYRIDIN-2-YL)-6-HYDROXY-3'-NITRO-BIPHENYL-3-YL]-ACETIC ACID"
drug:{5-(5-AMINO-1H-PYRROLO[3,2-B]PYRIDIN-2-YL)-6-HYDROXY-3'-NITRO-BIPHENYL-3-YL]-ACETIC ACIDrdf:typedrugbank:drugs
drug:{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Aciddrugbank:description" experimental This compound belongs to the monosaccharide phosphates. These are monosaccharides comprising a phosphated group linked tot he carbohydrate unit. Monosaccharide Phosphates Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Monosaccharides Hexoses Organic Phosphoric Acids Organophosphate Esters Organic Phosphonic Acids Tertiary Amines 1,2-Diols Secondary Alcohols Carbonyl Hydrates Polyamines phosphoric acid ester organic phosphate phosphonic acid phosphonic acid derivative tertiary amine polyol 1,2-diol secondary alcohol carbonyl hydrate polyamine amine alcohol organonitrogen compound logP -1.9 ALOGPS logS -1.4 ALOGPS Water Solubility 1.78e+01 g/l ALOGPS logP -7 ChemAxon IUPAC Name {[(2,2-dihydroxyethyl)[(2R,3S,4S,5R)-2,3,4,5-tetrahydroxy-6-(phosphonooxy)hexyl]amino]methyl}phosphonic acid ChemAxon Traditional IUPAC Name [(2,2-dihydroxyethyl)[(2R,3S,4S,5R)-2,3,4,5-tetrahydroxy-6-(phosphonooxy)hexyl]amino]methylphosphonic acid ChemAxon Molecular Weight 415.2253 ChemAxon Monoisotopic Weight 415.064462851 ChemAxon SMILES OC(O)CN(C[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)COP(O)(O)=O)CP(O)(O)=O ChemAxon Molecular Formula C9H23NO13P2 ChemAxon InChI InChI=1S/C9H23NO13P2/c11-5(1-10(2-7(13)14)4-24(17,18)19)8(15)9(16)6(12)3-23-25(20,21)22/h5-9,11-16H,1-4H2,(H2,17,18,19)(H2,20,21,22)/t5-,6-,8+,9+/m1/s1 ChemAxon InChIKey InChIKey=ATILYNKCRYHYEP-YGBUUZGLSA-N ChemAxon Polar Surface Area (PSA) 248.91 ChemAxon Refractivity 78.9 ChemAxon Polarizability 33.79 ChemAxon Rotatable Bond Count 12 ChemAxon H Bond Acceptor Count 13 ChemAxon H Bond Donor Count 10 ChemAxon pKa (strongest acidic) -0.8 ChemAxon pKa (strongest basic) 5.55 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 0 ChemAxon Bioavailability 0 ChemAxon PubChem Compound 46936381 PubChem Substance 46508017 ChemSpider 2535660 PDB PAI BE0001394 2-dehydro-3-deoxyphosphooctonate aldolase Shigella flexneri # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown 2-dehydro-3-deoxyphosphooctonate aldolase Cell wall/membrane/envelope biogenesis Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate kdsA Cytoplasm None 6.79 30833.0 Shigella flexneri GenBank Gene Database AE005674 GenBank Protein Database 24051519 UniProtKB P0A716 UniProt Accession KDSA_SHIFL 3-deoxy-D-manno-octulosonic acid 8- phosphate synthetase EC 2.5.1.55 KDO 8-P synthase KDO-8-phosphate synthetase KDOPS Phospho-2- dehydro-3-deoxyoctonate aldolase >2-dehydro-3-deoxyphosphooctonate aldolase MKQKVVSIGDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDK ANRSSIHSYRGPGLEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLAR QTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDRGANFGYDNLVVD MLGFSIMKKVSGNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEA HPDPEHAKCDGPSALPLAKLEPFLKQMKAIDDLVKGFEELDTSK >855 bp ATGAAACAAAAAGTGGTTAGCATTGGCGACATCAACGTAGCAAATGACCTGCCGTTCGTA CTGTTTGGCGGTATGAACGTGCTGGAATCTCGCGATCTGGCGATGCGCATTTGCGAGCAC TACGTAACTGTGACCCAGAAACTGGGTATCCCTTACGTGTTCAAAGCCTCTTTTGACAAA GCCAACCGCTCCTCCATCCACTCTTATCGTGGACCGGGCCTGGAAGAAGGGATGAAAATC TTCCAGGAGTTGAAGCAGACTTTTGGCGTGAAAATTATCACCGACGTTCACGAACCAAGT CAGGCACAGCCCGTTGCTGATGTCGTGGATGTGATTCAGTTGCCGGCGTTTCTTGCTCGC CAGACTGACCTGGTTGAAGCCATGGCGAAAACCGGTGCGGTAATTAACGTCAAGAAACCA CAGTTTGTCAGCCCGGGACAGATGGGTAATATCGTTGATAAATTCAAAGAAGGCGGCAAC GAAAAAGTGATTCTTTGCGATCGTGGTGCTAACTTCGGCTATGACAACCTGGTTGTCGAT ATGCTGGGCTTCAGCATTATGAAGAAAGTGTCTGGTAACTCGCCGGTGATTTTCGACGTG ACCCACGCACTGCAATGCCGCGATCCGTTTGGCGCAGCTTCCGGTGGTCGTCGTGCTCAG GTGGCTGAGCTGGCACGAGCCGGTATGGCGGTAGGTCTGGCGGGGCTGTTTATTGAAGCG CATCCGGATCCGGAACATGCGAAATGTGATGGTCCATCCGCGCTGCCGCTGGCTAAACTG GAACCGTTCCTCAAGCAGATGAAAGCGATTGATGATCTGGTGAAAGGTTTCGAAGAACTG GATACCAGCAAGTAA PF00793 DAHP_synth_1 component cell component intracellular component cytoplasm function transferase activity function transferase activity, transferring alkyl or aryl (other than methyl) groups function 3-deoxy-8-phosphooctulonate synthase activity function catalytic activity process metabolism process biosynthesis process physiological process BE0001253 2-dehydro-3-deoxyphosphooctonate aldolase Aquifex aeolicus (strain VF5) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown 2-dehydro-3-deoxyphosphooctonate aldolase Cell wall/membrane/envelope biogenesis Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate kdsA Cytoplasm None 6.68 29735.0 Aquifex aeolicus (strain VF5) GenBank Gene Database AE000657 GenBank Protein Database 2982835 UniProtKB O66496 UniProt Accession KDSA_AQUAE 3-deoxy-D-manno-octulosonic acid 8- phosphate synthetase EC 2.5.1.55 KDO 8-P synthase KDO-8-phosphate synthetase KDOPS Phospho-2- dehydro-3-deoxyoctonate aldolase >2-dehydro-3-deoxyphosphooctonate aldolase MEKFLVIAGPCAIESEELLLKVGEEIKRLSEKFKEVEFVFKSSFDKANRSSIHSFRGHGL EYGVKALRKVKEEFGLKITTDIHESWQAEPVAEVADIIQIPAFLCRQTDLLLAAAKTGRA VNVKKGQFLAPWDTKNVVEKLKFGGAKEIYLTERGTTFGYNNLVVDFRSLPIMKQWAKVI YDATHSVQLPGGLGDKSGGMREFIFPLIRAAVAVGCDGVFMETHPEPEKALSDASTQLPL SQLEGIIEAILEIREVASKYYETIPVK >804 bp ATGGAAAAGTTTTTAGTGATAGCTGGACCCTGCGCGATAGAGAGCGAGGAACTTCTCCTA AAGGTAGGGGAGGAGATAAAGCGTTTATCGGAGAAGTTCAAAGAAGTTGAGTTCGTATTT AAGTCTTCCTTTGATAAAGCGAACCGCTCCTCAATACATTCCTTCAGGGGGCACGGTCTT GAATACGGGGTAAAGGCTCTGAGGAAGGTAAAGGAAGAGTTCGGACTGAAGATTACCACG GATATTCACGAGAGCTGGCAAGCTGAACCAGTTGCAGAAGTTGCGGACATAATCCAGATA CCTGCCTTTTTATGCAGGCAGACTGACCTCCTCCTTGCGGCTGCAAAAACGGGAAGGGCT GTAAACGTGAAGAAGGGTCAGTTTTTAGCCCCTTGGGACACGAAGAACGTGGTTGAAAAA TTAAAGTTCGGCGGTGCTAAGGAGATATACCTCACGGAGAGAGGAACTACCTTCGGATAC AACAACCTCGTTGTAGATTTCAGGAGCCTACCCATAATGAAACAGTGGGCAAAGGTTATA TACGACGCCACCCACAGCGTCCAGCTCCCCGGAGGTCTCGGGGACAAATCAGGAGGAATG AGGGAGTTTATATTCCCCTTAATCCGTGCTGCGGTTGCGGTAGGTTGTGACGGTGTGTTT ATGGAAACACACCCAGAACCAGAAAAGGCACTCTCGGACGCATCAACTCAGCTTCCCCTC TCCCAGCTGGAAGGGATAATAGAGGCTATCCTTGAGATAAGGGAAGTGGCTTCAAAGTAT TACGAAACAATTCCCGTTAAATGA PF00793 DAHP_synth_1 component cell component intracellular component cytoplasm function transferase activity function transferase activity, transferring alkyl or aryl (other than methyl) groups function 3-deoxy-8-phosphooctulonate synthase activity function catalytic activity process metabolism process biosynthesis process physiological process "
drug:{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acidrdfs:label"{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acid"
drug:{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acidowl:sameAsdrug:EXPT02492
drug:{[(2,2-Dihydroxy-Ethyl)-(2,3,4,5-Tetrahydroxy-6-Phosphonooxy-Hexyl)-Amino]-Methyl}-Phosphonic Acidrdf:typedrugbank:drugs
drug:{[(2,6-difluorophenyl)carbonyl]amino}-N-(4-fluorophenyl)-1H-pyrazole-3-carboxamidedrugbank:description" experimental This compound belongs to the anilides. These are organic heterocyclic compounds derived from oxoacids RkE(=O)l(OH)m (l not 0) by replacing an OH group by the NHPh group or derivative formed by ring substitution. Anilides Organic Compounds Benzenoids Benzene and Substituted Derivatives Anilides Benzamides Benzoyl Derivatives Fluorobenzenes Aryl Fluorides Pyrazoles Secondary Carboxylic Acid Amides Carboxylic Acids Polyamines Enolates Organofluorides benzoyl fluorobenzene aryl fluoride aryl halide pyrazole azole carboxamide group secondary carboxylic acid amide polyamine carboxylic acid derivative enolate carboxylic acid organohalogen amine organofluoride organonitrogen compound logP 3.01 ALOGPS logS -4.9 ALOGPS Water Solubility 4.35e-03 g/l ALOGPS logP 3.28 ChemAxon IUPAC Name 4-C-(2,6-difluorobenzene)-3-N-(4-fluorophenyl)-1H-pyrazole-3,4-dicarboxamide ChemAxon Traditional IUPAC Name 4-C-(2,6-difluorobenzene)-3-N-(4-fluorophenyl)-1H-pyrazole-3,4-dicarboxamide ChemAxon Molecular Weight 360.29 ChemAxon Monoisotopic Weight 360.083410231 ChemAxon SMILES FC1=CC=C(NC(=O)C2=NNC=C2NC(=O)C2=C(F)C=CC=C2F)C=C1 ChemAxon Molecular Formula C17H11F3N4O2 ChemAxon InChI InChI=1S/C17H11F3N4O2/c18-9-4-6-10(7-5-9)22-17(26)15-13(8-21-24-15)23-16(25)14-11(19)2-1-3-12(14)20/h1-8H,(H,21,24)(H,22,26)(H,23,25) ChemAxon InChIKey InChIKey=BDRDBXXWQDFXEC-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 86.88 ChemAxon Refractivity 91.09 ChemAxon Polarizability 31.06 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 9.22 ChemAxon pKa (strongest basic) -0.82 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 24864079 PubChem Substance 99444609 ChemSpider 22377575 PDB LZ9 BE0001072 Cyclin-dependent kinase 2 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Cyclin-dependent kinase 2 Involved in protein kinase activity ATP + a protein = ADP + a phosphoprotein CDK2deltaT None 9.76 30061.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1771 GenAtlas CDK2deltaT GeneCards CDK2deltaT GenBank Gene Database AB012305 GenBank Protein Database 3551191 UniProtKB P24941 UniProt Accession CDK2_HUMAN EC 2.7.11.22 p33 protein kinase >Cell division protein kinase 2 MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL >897 bp ATGGAGAACTTCCAAAAGGTGGAAAAGATCGGAGAGGGCACGTACGGAGTTGTGTACAAA GCCAGAAACAAGTTGACGGGAGAGGTGGTGGCGCTTAAGAAAATCCGCCTGGACACTGAG ACTGAGGGTGTGCCCAGTACTGCCATCCGAGAGATCTCTCTGCTTAAGGAGCTTAACCAT CCTAATATTGTCAAGCTGCTGGATGTCATTCACACAGAAAATAAACTCTACCTGGTTTTT GAATTTCTGCACCAAGATCTCAAGAAATTCATGGATGCCTCTGCTCTCACTGGCATTCCT CTTCCCCTCATCAAGAGCTATCTGTTCCAGCTGCTCCAGGGCCTAGCTTTCTGCCATTCT CATCGGGTCCTCCACCGAGACCTTAAACCTCAGAATCTGCTTATTAACACAGAGGGGGCC ATCAAGCTAGCAGACTTTGGACTAGCCAGAGCTTTTGGAGTCCCTGTTCGTACTTACACC CATGAGGTGGTGACCCTGTGGTACCGAGCTCCTGAAATCCTCCTGGGCTCGAAATATTAT TCCACAGCTGTGGACATCTGGAGCCTGGGCTGCATCTTTGCTGAGATGGTGACTCGCCGG GCCCTGTTCCCTGGAGATTCTGAGATTGACCAGCTCTTCCGGATCTTTCGGACTCTGGGG ACCCCAGATGAGGTGGTGTGGCCAGGAGTTACTTCTATGCCTGATTACAAGCCAAGTTTC CCCAAGTGGGCCCGGCAAGATTTTAGTAAAGTTGTACCTCCCCTGGATGAAGATGGACGG AGCTTGTTATCGCAAATGCTGCACTACGACCCTAACAAGCGGATTTCGGCCAAGGCAGCC CTGGCTCACCCTTTCTTCCAGGATGTGACCAAGCCAGTACCCCATCTTCGACTCTGA PF00069 Pkinase function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification process physiological process process metabolism process macromolecule metabolism "
drug:{[(2,6-difluorophenyl)carbonyl]amino}-N-(4-fluorophenyl)-1H-pyrazole-3-carboxamiderdfs:label"{[(2,6-difluorophenyl)carbonyl]amino}-N-(4-fluorophenyl)-1H-pyrazole-3-carboxamide"
drug:{[(2,6-difluorophenyl)carbonyl]amino}-N-(4-fluorophenyl)-1H-pyrazole-3-carboxamiderdf:typedrugbank:drugs
drug:{[2-(1h-1,2,3-Benzotriazol-1-Yl)-2-(3,4-Difluorophenyl)Propane-1,3-Diyl]Bis[4,1-Phenylene(Difluoromethylene)]}Bis(Phosphonic Acid)drugbank:description" experimental This compound belongs to the stilbenes. These are organic compounds containing a 1,2-diphenylethylene moiety. Stilbenes (C6-C2-C6 ) are derived from the common phenylpropene (C6-C3) skeleton building block. The introduction of one or more hydroxyl groups to a phenyl ring lead to stilbenoids. Stilbenes Organic Compounds Phenylpropanoids and Polyketides Stilbenes Phenylpropylamines Amphetamines and Derivatives Benzotriazoles Fluorobenzenes Aryl Fluorides Triazoles Organic Phosphonic Acids Polyamines Organofluorides Alkyl Fluorides phenylpropylamine amphetamine or derivative benzotriazole fluorobenzene aryl fluoride benzene aryl halide phosphonic acid derivative azole 1,2,3-triazole phosphonic acid polyamine amine organohalogen organofluoride alkyl halide alkyl fluoride organonitrogen compound logP 3.64 ALOGPS logS -4.5 ALOGPS Water Solubility 2.02e-02 g/l ALOGPS logP 5.12 ChemAxon IUPAC Name ({4-[2-(1H-1,2,3-benzotriazol-1-yl)-3-{4-[difluoro(phosphono)methyl]phenyl}-2-(3,4-difluorophenyl)propyl]phenyl}difluoromethyl)phosphonic acid ChemAxon Traditional IUPAC Name {4-[2-(1,2,3-benzotriazol-1-yl)-3-{4-[difluoro(phosphono)methyl]phenyl}-2-(3,4-difluorophenyl)propyl]phenyl}difluoromethylphosphonic acid ChemAxon Molecular Weight 685.4474 ChemAxon Monoisotopic Weight 685.096627737 ChemAxon SMILES OP(O)(=O)C(F)(F)C1=CC=C(CC(CC2=CC=C(C=C2)C(F)(F)P(O)(O)=O)(N2N=NC3=C2C=CC=C3)C2=CC=C(F)C(F)=C2)C=C1 ChemAxon Molecular Formula C29H23F6N3O6P2 ChemAxon InChI InChI=1S/C29H23F6N3O6P2/c30-23-14-13-22(15-24(23)31)27(38-26-4-2-1-3-25(26)36-37-38,16-18-5-9-20(10-6-18)28(32,33)45(39,40)41)17-19-7-11-21(12-8-19)29(34,35)46(42,43)44/h1-15H,16-17H2,(H2,39,40,41)(H2,42,43,44) ChemAxon InChIKey InChIKey=BTAGTGWPDROBMG-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 145.77 ChemAxon Refractivity 166.06 ChemAxon Polarizability 57.53 ChemAxon Rotatable Bond Count 10 ChemAxon H Bond Acceptor Count 8 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) -0.0069 ChemAxon pKa (strongest basic) 0.47 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 5 ChemAxon Bioavailability 0 ChemAxon MDDR-Like Rule true ChemAxon PubChem Compound 448024 PubChem Substance 46507391 ChemSpider 394956 BindingDB 13596 PDB P27 BE0000623 Tyrosine-protein phosphatase non-receptor type 1 Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Tyrosine-protein phosphatase non-receptor type 1 Involved in protein tyrosine phosphatase activity May play an important role in CKII- and p60c-src-induced signal transduction cascades PTPN1 20q13.1-q13.2 Endoplasmic reticulum; endoplasmic reticulum membrane; peripheral membrane protein; cytoplasmic side 409-431 6.21 49967.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9642 GenAtlas PTPN1 GeneCards PTPN1 GenBank Gene Database M31724 GenBank Protein Database 190742 UniProtKB P18031 UniProt Accession PTN1_HUMAN EC 3.1.3.48 Protein-tyrosine phosphatase 1B PTP-1B >Tyrosine-protein phosphatase non-receptor type 1 MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLH QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK CAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWP DFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKD PSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLE PPPEHIPPPPRPPKRILEPHNGKCREFFPNHQWVKEETQEDKDCPIKEEKGSPLNAAPYG IESMSQDTEVRSRVVGGSLRGAQAASPAKGEPSLPEKDEDHALSYWKPFLVNMCVATVLT AGAYLCYRFLFNSNT >1308 bp ATGGAGATGGAAAAGGAGTTCGAGCAGATCGACAAGTCCGGGAGCTGGGCGGCCATTTAC CAGGATATCCGACATGAAGCCAGTGACTTCCCATGTAGAGTGGCCAAGCTTCCTAAGAAC AAAAACCGAAATAGGTACAGAGACGTCAGTCCCTTTGACCATAGTCGGATTAAACTACAT CAAGAAGATAATGACTATATCAACGCTAGTTTGATAAAAATGGAAGAAGCCCAAAGGAGT TACATTCTTACCCAGGGCCCTTTGCCTAACACATGCGGTCACTTTTGGGAGATGGTGTGG GAGCAGAAAAGCAGGGGTGTCGTCATGCTCAACAGAGTGATGGAGAAAGGTTCGTTAAAA TGCGCACAATACTGGCCACAAAAAGAAGAAAAAGAGATGATCTTTGAAGACACAAATTTG AAATTAACATTGATCTCTGAAGATATCAAGTCATATTATACAGTGCGACAGCTAGAATTG GAAAACCTTACAACCCAAGAAACTCGAGAGATCTTACATTTCCACTATACCACATGGCCT GACTTTGGAGTCCCTGAATCACCAGCCTCATTCTTGAACTTTCTTTTCAAAGTCCGAGAG TCAGGGTCACTCAGCCCGGAGCACGGGCCCGTTGTGGTGCACTGCAGTGCAGGCATCGGC AGGTCTGGAACCTTCTGTCTGGCTGATACCTGCCTCCTGCTGATGGACAAGAGGAAAGAC CCTTCTTCCGTTGATATCAAGAAAGTGCTGTTAGAAATGAGGAAGTTTCGGATGGGGTTG ATCCAGACAGCCGACCAGCTGCGCTTCTCCTACCTGGCTGTGATCGAAGGTGCCAAATTC ATCATGGGGGACTCTTCCGTGCAGGATCAGTGGAAGGAGCTTTCCCACGAGGACCTGGAG CCCCCACCCGAGCATATCCCCCCACCTCCCCGGCCACCCAAACGAATCCTGGAGCCACAC AATGGGAAATGCAGGGAGTTCTTCCCAAATCACCAGTGGGTGAAGGAAGAGACCCAGGAG GATAAAGACTGCCCCATCAAGGAAGAAAAAGGAAGCCCCTTAAATGCCGCACCCTACGGC ATCGAAAGCATGAGTCAAGACACTGAAGTTAGAAGTCGGGTCGTGGGGGGAAGTCTTCGA GGTGCCCAGGCTGCCTCCCCAGCCAAAGGGGAGCCGTCACTGCCCGAGAAGGACGAGGAC CATGCACTGAGTTACTGGAAGCCCTTCCTGGTCAACATGTGCGTGGCTACGGTCCTCACG GCCGGCGCTTACCTCTGCTACAGGTTCCTGTTCAACAGCAACACATAG PF00102 Y_phosphatase function hydrolase activity, acting on ester bonds function phosphoric ester hydrolase activity function phosphoric monoester hydrolase activity function phosphoprotein phosphatase activity function catalytic activity function protein tyrosine phosphatase activity function hydrolase activity process physiological process process metabolism process protein amino acid dephosphorylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification "
drug:{[2-(1h-1,2,3-Benzotriazol-1-Yl)-2-(3,4-Difluorophenyl)Propane-1,3-Diyl]Bis[4,1-Phenylene(Difluoromethylene)]}Bis(Phosphonic Acid)rdfs:label"{[2-(1h-1,2,3-Benzotriazol-1-Yl)-2-(3,4-Difluorophenyl)Propane-1,3-Diyl]Bis[4,1-Phenylene(Difluoromethylene)]}Bis(Phosphonic Acid)"
drug:{[2-(1h-1,2,3-Benzotriazol-1-Yl)-2-(3,4-Difluorophenyl)Propane-1,3-Diyl]Bis[4,1-Phenylene(Difluoromethylene)]}Bis(Phosphonic Acid)owl:sameAsdrug:EXPT02473
drug:{[2-(1h-1,2,3-Benzotriazol-1-Yl)-2-(3,4-Difluorophenyl)Propane-1,3-Diyl]Bis[4,1-Phenylene(Difluoromethylene)]}Bis(Phosphonic Acid)rdf:typedrugbank:drugs
drug:{[4-AMINO-2-(3-CHLOROANILINO)-1,3-THIAZOL-5-YL](4-FLUOROPHENYL)METHANONEdrugbank:description" experimental This compound belongs to the acetophenones. These are organic compounds containing the acetophenone structure. Acetophenones Organic Compounds Benzenoids Benzene and Substituted Derivatives Acetophenones Thiazolecarboxylic Acids and Derivatives Benzoyl Derivatives 2,4,5-trisubstituted Thiazoles Fluorobenzenes Chlorobenzenes Aryl Chlorides Aminothiazoles Aryl Fluorides Primary Aromatic Amines Ketones Enolates Secondary Amines Polyamines Organofluorides Organochlorides 2,4,5-trisubstituted 1,3-thiazole thiazolecarboxylic acid or derivative benzoyl chlorobenzene fluorobenzene primary aromatic amine aryl halide aryl fluoride 1,3-thiazolamine aryl chloride thiazole azole ketone secondary amine enolate polyamine organohalogen primary amine carbonyl group organochloride organofluoride organonitrogen compound amine logP 1.87 ALOGPS logS -5.8 ALOGPS Water Solubility 6.74e-04 g/l ALOGPS logP 5.51 ChemAxon IUPAC Name 4-amino-2-[(3-chlorophenyl)amino]-5-[(4-fluorophenyl)carbonyl]-1,3-thiazol-3-ium ChemAxon Traditional IUPAC Name 4-amino-2-[(3-chlorophenyl)amino]-5-[(4-fluorophenyl)carbonyl]-1,3-thiazol-3-ium ChemAxon Molecular Weight 348.802 ChemAxon Monoisotopic Weight 348.037363623 ChemAxon SMILES NC1=C(SC(NC2=CC(Cl)=CC=C2)=[NH+]1)C(=O)C1=CC=C(F)C=C1 ChemAxon Molecular Formula C16H12ClFN3OS ChemAxon InChI InChI=1S/C16H11ClFN3OS/c17-10-2-1-3-12(8-10)20-16-21-15(19)14(23-16)13(22)9-4-6-11(18)7-5-9/h1-8H,19H2,(H,20,21)/p+1 ChemAxon InChIKey InChIKey=WWGPTHOMFHDEEC-UHFFFAOYSA-O ChemAxon Polar Surface Area (PSA) 69.26 ChemAxon Refractivity 99.5 ChemAxon Polarizability 34.34 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 12.12 ChemAxon pKa (strongest basic) 1.92 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Ghose Filter true ChemAxon PubChem Compound 10062702 PubChem Substance 99443960 ChemSpider 8238249 PDB BRQ BE0003958 Casein kinase I isoform gamma-3 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Casein kinase I isoform gamma-3 Involved in ATP binding Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling (By similarity) CSNK1G3 5q23 Cytoplasm None 9.63 51388.1 Human HUGO Gene Nomenclature Committee (HGNC) GNC:2456 GeneCards CSNK1G3 GenBank Gene Database AF049089 GenBank Protein Database 4590040 UniProtKB Q9Y6M4 UniProt Accession KC1G3_HUMAN CKI-gamma 3 >Casein kinase I isoform gamma-3 MENKKKDKDKSDDRMARPSGRSGHNTRGTGSSSSGVLMVGPNFRVGKKIGCGNFGELRLG KNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLG PSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKTQQV IHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFM YFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEMATYLRYVRRLDFFEKPD YDYLRKLFTDLFDRKGYMFDYEYDWIGKQLPTPVGAVQQDPALSSNREAHQHRDKMQQSK NQSADHRAAWDSQQANPHHLRAHLAADRHGGSVQVVSSTNGELNTDDPTAGRSNAPITAP TEVEVMDETKCCCFFKRRKRKTIQRHK >1344 bp ATGGAAAATAAAAAGAAAGACAAGGACAAATCAGATGATAGAATGGCACGACCTAGTGGT CGATCGGGACACAACACTCGAGGAACTGGGTCTTCATCGTCTGGAGTTTTAATGGTTGGA CCTAACTTTAGAGTTGGAAAAAAAATTGGATGTGGCAATTTTGGAGAATTACGATTAGGG AAAAATTTATACACAAATGAATATGTGGCAATTAAGTTGGAGCCCATGAAATCAAGAGCA CCACAGCTACATTTGGAATACAGATTCTATAAGCAGTTAGGATCTGGAGATGGTATACCT CAAGTTTACTATTTCGGCCCTTGTGGTAAATACAATGCTATGGTGCTGGAACTGCTGGGA CCTAGTTTGGAAGACTTGTTTGACTTGTGTGACAGAACATTTTCTCTTAAAACAGTTCTC ATGATAGCTATACAACTGATTTCTCGCATGGAATATGTCCATTCAAAGAACTTGATATAC AGAGATGTAAAACCTGAGAACTTCTTAATAGGACGACCAAGAAACAAAACCCAGCAAGTT ATTCACATTATAGATTTTGGTTTGGCAAAGGAATATATTGATCCGGAGACAAAGAAACAC ATACCATACAGAGAACACAAGAGCCTTACAGGAACAGCTAGATATATGAGCATAAACACA CATTTAGGAAAAGAACAAAGTAGAAGAGACGATTTAGAAGCTTTAGGTCATATGTTCATG TATTTTCTGAGAGGCAGTCTTCCTTGGCAAGGCTTAAAGGCTGACACATTAAAGGAGAGG TATCAGAAAATTGGAGATACAAAACGGGCTACACCAATAGAAGTGTTATGTGAAAATTTT CCAGAAATGGCAACATATCTTCGTTATGTAAGAAGGCTAGATTTTTTTGAAAAACCAGAC TATGAATACTTAAGAAAGCTTTTTACTGACTTGTTTGATCGAAAAGGATATATGTTTGAT TATGAATATGACTGGATTGGTAAACAGTTGCCTACTCCAGTGGGTGCAGTTCAGCAAGAT CCTGCTCTGTCATCAAACAGAGAAGCACATCAACACAGAGATAAGATGCAACAATCCAAA AACCAGTCGGCAGACCACAGGGCAGCTTGGGACTCCCAGCAGGCAAATCCCCACCATTTG AGAGCTCACCTTGCAGCAGACAGACATGGTGGCTCGGTACAGGTTGTAAGTTCTACAAAT GGAGAGTTAAACACAGATGACCCCACCGCAGGACGTTCAAATGCACCCATCACAGCCCCT ACTGAAGTAGAAGTGATGGATGAAACCAAGTGCTGCTGCTTTTTCAAACGAAGGAAAAGG AAAACCATACAGCGCCACAAATGA PF00069 Pkinase function ATP binding function catalytic activity function transferase activity, transferring phosphorus-containing groups function kinase activity function protein kinase activity function protein serine/threonine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity process physiological process process metabolism process macromolecule metabolism process biopolymer metabolism process protein amino acid phosphorylation process biopolymer modification process protein modification "
drug:{[4-AMINO-2-(3-CHLOROANILINO)-1,3-THIAZOL-5-YL](4-FLUOROPHENYL)METHANONErdfs:label"{[4-AMINO-2-(3-CHLOROANILINO)-1,3-THIAZOL-5-YL](4-FLUOROPHENYL)METHANONE"
drug:{[4-AMINO-2-(3-CHLOROANILINO)-1,3-THIAZOL-5-YL](4-FLUOROPHENYL)METHANONErdf:typedrugbank:drugs
drug:{[5-(5-NITRO-2-FURYL)-1,3,4-OXADIAZOL-2-YL]THIO}ACETIC ACIDdrugbank:description" experimental This compound belongs to the nitrofurans. These are compounds containing a furan ring which bears a nitro group. Nitrofurans Organic Compounds Heterocyclic Compounds Furans Nitrofurans Oxadiazoles Nitronic Acids Nitro Compounds Organic Oxoazanium Compounds Polyamines Thioethers Enolates Carboxylic Acids azole oxadiazole nitronic acid nitro compound polyamine enolate thioether carboxylic acid organic oxoazanium carboxylic acid derivative amine organonitrogen compound logP 0.66 ALOGPS logS -3.2 ALOGPS Water Solubility 1.71e-01 g/l ALOGPS logP 0.55 ChemAxon IUPAC Name 2-{[5-(5-nitrofuran-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}acetic acid ChemAxon Traditional IUPAC Name {[5-(5-nitrofuran-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}acetic acid ChemAxon Molecular Weight 271.207 ChemAxon Monoisotopic Weight 270.989905597 ChemAxon SMILES OC(=O)CSC1=NN=C(O1)C1=CC=C(O1)[N+]([O-])=O ChemAxon Molecular Formula C8H5N3O6S ChemAxon InChI InChI=1S/C8H5N3O6S/c12-6(13)3-18-8-10-9-7(17-8)4-1-2-5(16-4)11(14)15/h1-2H,3H2,(H,12,13) ChemAxon InChIKey InChIKey=ITBNJCVIFHSKRL-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 135.18 ChemAxon Refractivity 69.52 ChemAxon Polarizability 22.99 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 3.11 ChemAxon pKa (strongest basic) -3.1 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon ChEBI 43741 PubChem Compound 2817424 PubChem Substance 99444569 ChemSpider 2095728 PDB LIT BE0000747 Aldose reductase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Aldose reductase Involved in oxidoreductase activity Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies AKR1B1 7q35 Cytoplasm None 6.99 35723.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:381 GenAtlas AKR1B1 GeneCards AKR1B1 GenBank Gene Database J04795 GenBank Protein Database 178487 UniProtKB P15121 UniProt Accession ALDR_HUMAN Aldehyde reductase AR EC 1.1.1.21 >Aldose reductase ASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQE KLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKE FFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPA VNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKH NKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCAL LSCTSHKDYPFHEEF >951 bp ATGGCAAGCCGTCTCCTGCTCAACAACGGCGCCAAGATGCCCATCCTGGGGTTGGGTACC TGGAAGTCCCCTCCAGGGCAGGTGACTGAGGCCGTGAAGGTGGCCATTGACGTCGGGTAC CGCCACATCGACTGTGCCCATGTGTACCAGAATGAGAATGAGGTGGGGGTGGCCATTCAG GAGAAGCTCAGGGAGCAGGTGGTGAAGCGTGAGGAGCTCTTCATCGTCAGCAAGCTGTGG TGCACGTACCATGAGAAGGGCCTGGTGAAAGGAGCCTGCCAGAAGACACTCAGCGACCTG AAGCTGGACTACCTGGACCTCTACCTTATTCACTGGCCGACTGGCTTTAAGCCTGGGAAG GAATTTTTCCCATTGGATGAGTCGGGCAATGTGGTTCCCAGTGACACCAACATTCTGGAC ACGTGGGCGGCCATGGAAGAGCTGGTGGATGAAGGGCTGGTGAAAGCTATTGGCATCTCC AACTTCAACCATCTCCAGGTGGAGATGATCTTAAACAAACCTGGCTTGAAGTATAAGCCT GCAGTTAACCAGATTGAGTGCCACCCATATCTCACTCAGGAGAAGTTAATCCAGTACTGC CAGTCCAAAGGCATCGTGGTGACCGCCTACAGCCCCCTCGGCTCTCCTGACAGGCCCTGG GCCAAGCCCGAGGACCCTTCTCTCCTGGAGGATCCCAGGATCAAGGCGATCGCAGCCAAG CACAATAAAACTACAGCCCAGGTCCTGATCCGGTTCCCCATGCAGAGGAACTTGGTGGTG ATCCCCAAGTCTGTGACACCAGAACGCATTGCTGAGAACTTTAAGGTCTTTGACTTTGAA CTGAGCAGCCAGGATATGACCACCTTACTCAGCTACAACAGGAACTGGAGGGTCTGTGCC TTGTTGAGCTGTACCTCCCACAAGGATTACCCCTTCCATGAAGAGTTTTGA PF00248 Aldo_ket_red function catalytic activity function oxidoreductase activity "
drug:{[5-(5-NITRO-2-FURYL)-1,3,4-OXADIAZOL-2-YL]THIO}ACETIC ACIDrdfs:label"{[5-(5-NITRO-2-FURYL)-1,3,4-OXADIAZOL-2-YL]THIO}ACETIC ACID"
drug:{[5-(5-NITRO-2-FURYL)-1,3,4-OXADIAZOL-2-YL]THIO}ACETIC ACIDrdf:typedrugbank:drugs
drug:{[7-(Difluoro-Phosphono-Methyl)-Naphthalen-2-Yl]-Difluoro-Methyl}-Phosphonic Aciddrugbank:description" experimental This compound belongs to the naphthalenes. These are compounds containing a naphthalene moiety, which consists of two fused benzene rings. Naphthalenes Organic Compounds Benzenoids Acenes and Derivatives Naphthalenes Benzene and Substituted Derivatives Organic Phosphonic Acids Polyamines Organofluorides Alkyl Fluorides benzene phosphonic acid derivative phosphonic acid polyamine organofluoride organohalogen alkyl halide alkyl fluoride logP 1.85 ALOGPS logS -2.7 ALOGPS Water Solubility 8.28e-01 g/l ALOGPS logP 1.63 ChemAxon IUPAC Name ({7-[difluoro(phosphono)methyl]naphthalen-2-yl}difluoromethyl)phosphonic acid ChemAxon Traditional IUPAC Name {7-[difluoro(phosphono)methyl]naphthalen-2-yl}difluoromethylphosphonic acid ChemAxon Molecular Weight 388.1453 ChemAxon Monoisotopic Weight 387.988873896 ChemAxon SMILES OP(O)(=O)C(F)(F)C1=CC2=CC(=CC=C2C=C1)C(F)(F)P(O)(O)=O ChemAxon Molecular Formula C12H10F4O6P2 ChemAxon InChI InChI=1S/C12H10F4O6P2/c13-11(14,23(17,18)19)9-3-1-7-2-4-10(6-8(7)5-9)12(15,16)24(20,21)22/h1-6H,(H2,17,18,19)(H2,20,21,22) ChemAxon InChIKey InChIKey=VHKBLEYUHBIBNR-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 115.06 ChemAxon Refractivity 75.95 ChemAxon Polarizability 28.24 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 6 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 0.19 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 446662 PubChem Substance 46505029 ChemSpider 393958 PDB FNP BE0000623 Tyrosine-protein phosphatase non-receptor type 1 Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Tyrosine-protein phosphatase non-receptor type 1 Involved in protein tyrosine phosphatase activity May play an important role in CKII- and p60c-src-induced signal transduction cascades PTPN1 20q13.1-q13.2 Endoplasmic reticulum; endoplasmic reticulum membrane; peripheral membrane protein; cytoplasmic side 409-431 6.21 49967.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9642 GenAtlas PTPN1 GeneCards PTPN1 GenBank Gene Database M31724 GenBank Protein Database 190742 UniProtKB P18031 UniProt Accession PTN1_HUMAN EC 3.1.3.48 Protein-tyrosine phosphatase 1B PTP-1B >Tyrosine-protein phosphatase non-receptor type 1 MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLH QEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLK CAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWP DFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKD PSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLE PPPEHIPPPPRPPKRILEPHNGKCREFFPNHQWVKEETQEDKDCPIKEEKGSPLNAAPYG IESMSQDTEVRSRVVGGSLRGAQAASPAKGEPSLPEKDEDHALSYWKPFLVNMCVATVLT AGAYLCYRFLFNSNT >1308 bp ATGGAGATGGAAAAGGAGTTCGAGCAGATCGACAAGTCCGGGAGCTGGGCGGCCATTTAC CAGGATATCCGACATGAAGCCAGTGACTTCCCATGTAGAGTGGCCAAGCTTCCTAAGAAC AAAAACCGAAATAGGTACAGAGACGTCAGTCCCTTTGACCATAGTCGGATTAAACTACAT CAAGAAGATAATGACTATATCAACGCTAGTTTGATAAAAATGGAAGAAGCCCAAAGGAGT TACATTCTTACCCAGGGCCCTTTGCCTAACACATGCGGTCACTTTTGGGAGATGGTGTGG GAGCAGAAAAGCAGGGGTGTCGTCATGCTCAACAGAGTGATGGAGAAAGGTTCGTTAAAA TGCGCACAATACTGGCCACAAAAAGAAGAAAAAGAGATGATCTTTGAAGACACAAATTTG AAATTAACATTGATCTCTGAAGATATCAAGTCATATTATACAGTGCGACAGCTAGAATTG GAAAACCTTACAACCCAAGAAACTCGAGAGATCTTACATTTCCACTATACCACATGGCCT GACTTTGGAGTCCCTGAATCACCAGCCTCATTCTTGAACTTTCTTTTCAAAGTCCGAGAG TCAGGGTCACTCAGCCCGGAGCACGGGCCCGTTGTGGTGCACTGCAGTGCAGGCATCGGC AGGTCTGGAACCTTCTGTCTGGCTGATACCTGCCTCCTGCTGATGGACAAGAGGAAAGAC CCTTCTTCCGTTGATATCAAGAAAGTGCTGTTAGAAATGAGGAAGTTTCGGATGGGGTTG ATCCAGACAGCCGACCAGCTGCGCTTCTCCTACCTGGCTGTGATCGAAGGTGCCAAATTC ATCATGGGGGACTCTTCCGTGCAGGATCAGTGGAAGGAGCTTTCCCACGAGGACCTGGAG CCCCCACCCGAGCATATCCCCCCACCTCCCCGGCCACCCAAACGAATCCTGGAGCCACAC AATGGGAAATGCAGGGAGTTCTTCCCAAATCACCAGTGGGTGAAGGAAGAGACCCAGGAG GATAAAGACTGCCCCATCAAGGAAGAAAAAGGAAGCCCCTTAAATGCCGCACCCTACGGC ATCGAAAGCATGAGTCAAGACACTGAAGTTAGAAGTCGGGTCGTGGGGGGAAGTCTTCGA GGTGCCCAGGCTGCCTCCCCAGCCAAAGGGGAGCCGTCACTGCCCGAGAAGGACGAGGAC CATGCACTGAGTTACTGGAAGCCCTTCCTGGTCAACATGTGCGTGGCTACGGTCCTCACG GCCGGCGCTTACCTCTGCTACAGGTTCCTGTTCAACAGCAACACATAG PF00102 Y_phosphatase function hydrolase activity, acting on ester bonds function phosphoric ester hydrolase activity function phosphoric monoester hydrolase activity function phosphoprotein phosphatase activity function catalytic activity function protein tyrosine phosphatase activity function hydrolase activity process physiological process process metabolism process protein amino acid dephosphorylation process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification "
drug:{[7-(Difluoro-Phosphono-Methyl)-Naphthalen-2-Yl]-Difluoro-Methyl}-Phosphonic Acidrdfs:label"{[7-(Difluoro-Phosphono-Methyl)-Naphthalen-2-Yl]-Difluoro-Methyl}-Phosphonic Acid"
drug:{[7-(Difluoro-Phosphono-Methyl)-Naphthalen-2-Yl]-Difluoro-Methyl}-Phosphonic Acidowl:sameAsdrug:EXPT01463
drug:{[7-(Difluoro-Phosphono-Methyl)-Naphthalen-2-Yl]-Difluoro-Methyl}-Phosphonic Acidrdf:typedrugbank:drugs