Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB07627"

Predicate	Value (sorted: default)
rdfs:label	"(2S)-4-METHYL-2-(3-PHENYLTHIOUREIDO)-N-((3S)-TETRAHYDRO-2-HYDROXY-3-FURANYL)PENTANAMIDE"
rdf:type	drugbank:drugs
drugbank: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 Benzene and Substituted Derivatives Tetrahydrofurans Oxolanes Organic Thiocarbonic Acid Derivatives Secondary Carboxylic Acid Amides Hemiacetals Enolates Carboxylic Acids Polyamines benzene oxolane tetrahydrofuran secondary carboxylic acid amide thiocarbonic acid derivative carboxamide group hemiacetal ether polyamine enolate carboxylic acid amine organonitrogen compound logP 1.38 ALOGPS logS -4 ALOGPS Water Solubility 3.75e-02 g/l ALOGPS logP 2.46 ChemAxon IUPAC Name (2S)-N-[(3S,5S)-5-hydroxyoxolan-3-yl]-4-methyl-2-[(phenylcarbamothioyl)amino]pentanamide ChemAxon Traditional IUPAC Name (2S)-N-[(3S,5S)-5-hydroxyoxolan-3-yl]-4-methyl-2-[(phenylcarbamothioyl)amino]pentanamide ChemAxon Molecular Weight 351.464 ChemAxon Monoisotopic Weight 351.161662371 ChemAxon SMILES [H][C@@](CC(C)C)(NC(=S)NC1=CC=CC=C1)C(=O)N[C@]1([H])CO[C@]([H])(O)C1 ChemAxon Molecular Formula C17H25N3O3S ChemAxon InChI InChI=1S/C17H25N3O3S/c1-11(2)8-14(16(22)18-13-9-15(21)23-10-13)20-17(24)19-12-6-4-3-5-7-12/h3-7,11,13-15,21H,8-10H2,1-2H3,(H,18,22)(H2,19,20,24)/t13-,14-,15-/m0/s1 ChemAxon InChIKey InChIKey=DBPWWBMTZYJGGV-KKUMJFAQSA-N ChemAxon Polar Surface Area (PSA) 82.62 ChemAxon Refractivity 97.68 ChemAxon Polarizability 38 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 9.43 ChemAxon pKa (strongest basic) -2.7 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 2 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 6857711 PubChem Substance 99444098 ChemSpider 21613589 PDB D5G BE0003346 Calpain-1 catalytic subunit 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 Calpain-1 catalytic subunit Involved in calcium ion binding Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodelling and signal transduction CAPN1 11q13 Cytoplasm (By similarity). Cell membrane (By similarity) None 5.35 81891.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1476 GenAtlas CAPN1 GenBank Gene Database X04366 UniProtKB P07384 UniProt Accession CAN1_HUMAN Calcium-activated neutral proteinase 1 Calpain mu-type Calpain-1 large subunit CANP 1 EC 3.4.22.52 Micromolar-calpain muCANP >Calpain-1 catalytic subunit MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEA FPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAA IASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHS AEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILK ALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGE VEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKS RTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFV LALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINL REVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSE EEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRD GNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELII TRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA >2145 bp ATGTCGGAGGAGATCATCACGCCGGTGTACTGCACTGGGGTGTCAGCCCAAGTGCAGAAG CAGCGGGCCAGGGAGCTGGGCCTGGGCCGCCATGAGAATGCCATCAAGTACCTGGGCCAG GATTATGAGCAGCTGCGGGTGCGATGCCTGCAGAGTGGGACCCTCTTCCGTGATGAGGCC TTCCCCCCGGTACCCCAGAGCCTGGGTTACAAGGACCTGGGTCCCAATTCCTCCAAGACC TATGGCATCAAGTGGAAGCGTCCCACGGAACTGCTGTCAAACCCCCAGTTCATTGTGGAT GGAGCTACCCGCACAGACATCTGCCAGGGAGCACTGGGGGACTGCTGGCTCTTGGCGGCC ATTGCCTCCCTCACTCTCAACGACACCCTCCTGCACCGAGTGGTTCCGCACGGCCAGAGC TTCCAGAATGGCTATGCCGGCATCTTCCATTTCCAGCTGTGGCAATTTGGGGAGTGGGTG GACGTGGTCGTGGATGACCTGCTGCCCATCAAGGACGGGAAGCTAGTGTTCGTGCACTCT GCCGAAGGCAACGAGTTCTGGAGCGCCCTGCTTGAGAAGGCCTATGCCAAGGTAAATGGC AGCTACGAGGCCCTGTCAGGGGGCAGCACCTCAGAGGGCTTTGAGGACTTCACAGGCGGG GTTACCGAGTGGTACGAGTTGCGCAAGGCTCCCAGTGACCTCTACCAGATCATCCTCAAG GCGCTGGAGCGGGGCTCCCTGCTGGGCTGCTCCATAGACATCTCCAGCGTTCTAGACATG GAGGCCATCACTTTCAAGAAGTTGGTGAAGGGCCATGCCTACTCTGTGACCGGGGCCAAG CAGGTGAACTACCGAGGCCAGGTGGTGAGCCTGATCCGGATGCGGAACCCCTGGGGCGAG GTGGAGTGGACGGGAGCCTGGAGCGACAGCTCCTCAGAGTGGAACAACGTGGACCCATAT GAACGGGACCAGCTCCGGGTCAAGATGGAGGACGGGGAGTTCTGGATGTCATTCCGAGAC TTCATGCGGGAGTTCACCCGCCTGGAGATCTGCAACCTCACACCCGACGCCCTCAAGAGC CGGACCATCCGCAAATGGAACACCACACTCTACGAAGGCACCTGGCGGCGGGGGAGCACC GCGGGGGGCTGCCGAAACTACCCAGCCACCTTCTGGGTGAACCCTCAGTTCAAGATCCGG CTGGATGAGACGGATGACCCGGACGACTACGGGGACCGCGAGTCAGGCTGCAGCTTCGTG CTCGCCCTTATGCAGAAGCACCGTCGCCGCGAGCGCCGCTTCGGCCGCGACATGGAGACT ATTGGCTTCGCGGTCTACGAGGTCCCTCCGGAGCTGGTGGGCCAGCCGGCCGTACACTTG AAGCGTGACTTCTTCCTGGCCAATGCGTCTCGGGCGCGCTCAGAGCAGTTCATCAACCTG CGAGAGGTCAGCACCCGCTTCCGCCTGCCACCCGGGGAGTATGTGGTGGTGCCCTCCACC TTCGAGCCCAACAAGGAGGGCGACTTCGTGCTGCGCTTCTTCTCAGAGAAGAGTGCTGGG ACTGTGGAGCTGGATGACCAGATCCAGGCCAATCTCCCCGATGAGCAAGTGCTCTCAGAA GAGGAGATTGACGAGAACTTCAAGGCCCTCTTCAGGCAGCTGGCAGGGGAGGACATGGAG ATCAGCGTGAAGGAGTTGCGGACAATCCTCAATAGGATCATCAGCAAACACAAAGACCTG CGGACCAAGGGCTTCAGCCTAGAGTCGTGCCGCAGCATGGTGAACCTCATGGATCGTGAT GGCAATGGGAAGCTGGGCCTGGTGGAGTTCAACATCCTGTGGAACCGCATCCGGAATTAC CTGTCCATCTTCCGGAAGTTTGACCTGGACAAGTCGGGCAGCATGAGTGCCTACGAGATG CGGATGGCCATTGAGTCGGCAGGCTTCAAGCTCAACAAGAAGCTGTACGAGCTCATCATC ACCCGCTACTCGGAGCCCGACCTGGCGGTCGACTTTGACAATTTCGTTTGCTGCCTGGTG CGGCTAGAGACCATGTTCCGATTTTTCAAAACTCTGGACACAGATCTGGATGGAGTTGTG ACCTTTGACTTGTTTAAGTGGTTGCAGCTGACCATGTTTGCATGA PF00036 efhand PF01067 Calpain_III PF00648 Peptidase_C2 component cell component intracellular function catalytic activity function peptidase activity function endopeptidase activity function hydrolase activity function cysteine-type endopeptidase activity function ion binding function calpain activity function cation binding function binding function calcium ion binding process metabolism process proteolysis process macromolecule metabolism process protein metabolism process cellular protein metabolism process physiological process "

All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt

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