Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB03900"

Predicate	Value (sorted: none)
rdf:type	drugbank:drugs
owl:sameAs	drug:EXPT03021
drugbank:description	" experimental This compound belongs to the tertiary alcohols. These are compounds in which a hydroxy group, -OH, is attached to a saturated carbon atom R3COH (R not H ). Tertiary Alcohols Organic Compounds Organooxygen Compounds Alcohols and Polyols Tertiary Alcohols Polyamines polyamine logP 0.7 ALOGPS logS 0.32 ALOGPS Water Solubility 1.54e+02 g/l ALOGPS logP 0.54 ChemAxon IUPAC Name 2-methylpropan-2-ol ChemAxon Traditional IUPAC Name 2-methyl-2-propanol ChemAxon Molecular Weight 74.1216 ChemAxon Monoisotopic Weight 74.073164942 ChemAxon SMILES CC(C)(C)O ChemAxon Molecular Formula C4H10O ChemAxon InChI InChI=1S/C4H10O/c1-4(2,3)5/h5H,1-3H3 ChemAxon InChIKey InChIKey=DKGAVHZHDRPRBM-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 20.23 ChemAxon Refractivity 22.07 ChemAxon Polarizability 8.94 ChemAxon Rotatable Bond Count 0 ChemAxon H Bond Acceptor Count 1 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) 18.09 ChemAxon pKa (strongest basic) -1.4 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 6386 PubChem Substance 46507480 PDB TBU BE0003317 Ribonuclease pancreatic 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 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 BE0003844 Triosephosphate isomerase 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 Triosephosphate isomerase Carbohydrate transport and metabolism D-glyceraldehyde 3-phosphate = glycerone phosphate TPI1 12p13 None 6.91 26669.3 Human HUGO Gene Nomenclature Committee (HGNC) GNC:12009 GeneCards TPI1 GenBank Gene Database M10036 GenBank Protein Database 339841 UniProtKB P60174 UniProt Accession TPIS_HUMAN TIM Triose-phosphate isomerase >Triosephosphate isomerase MAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKI AVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAE GLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQ QAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE FVDIINAKQ >750 bp GCGACACTGACCTTCAGCGCCTCGGCTCGGCCATGGCGCCCTCCAGGAAGTTCTTCGTTG GGGGAAACTGGAAGATGAACGGGCGGAAGCAGAGTCTGGGGGAGCTCATCGGCACTCTGA ACGCGGCCAAGGTGCCGGCCGACACCGAGGTGGTTTGTGCTCCCCCTACTGCCTATATCG ACTTCGCCCGGCAGAAGCTAGATCCCAAGATTGCTGTGGCTGCGCAGAACTGCTACAAAG TGACTAATGGGGCTTTTACTGGGGAGATCAGCCCTGGCATGATCAAAGACTGCGGAGCCA CGTGGGTGGTCCTGGGACACTCAGAGAGAAGGCATGTCTTTGGGGAGTCAGATGAGCTGA TTGGGCAGAAAGTGGCCCATGCTCTGGCAGAGGGACTCGGAGTAATCGCCTGCATTGGGG AGAAGCTAGATGAAAGGGAAGCTGGCATCACTGAGAAGGTTGTTTTCGAGCAGACAAAGG TCATCGCAGATAACGTGAAGGACTGGAGCAAGGTCGTCCTCGCCTATGAGCCTGTGTGGG CCATTGGTACTGGCAAGACTGCAACACCCCAACAGGCCCAGGAAGTACACGAGAAGCTCC GAGGATGGCTGAAGTCCAACGTCTCTGATGCGGTGGCTCAGAGCACCCGTATCATTTATG GAGGCTCTGTGACTGGGGCAACCTGCAAGGAGCTGGCCAGCCAGCCTGATGTGGATGGCT TCCTTGTGGGTGGTGCTTCCCTCAAGCCCG PF00121 TIM function isomerase activity function intramolecular oxidoreductase activity function intramolecular oxidoreductase activity, interconverting aldoses and ketoses function triose-phosphate isomerase activity function catalytic activity process metabolism process physiological process BE0001534 Methionine aminopeptidase 2 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 Methionine aminopeptidase 2 Translation, ribosomal structure and biogenesis Removes the amino-terminal methionine from nascent proteins METAP2 12q22 Cytoplasmic None 5.57 52892.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:16672 GenAtlas METAP2 GeneCards METAP2 GenBank Gene Database U29607 GenBank Protein Database 903982 UniProtKB P50579 UniProt Accession MAP2_HUMAN EC 3.4.11.18 Initiation factor 2-associated 67 kDa glycoprotein MetAP 2 p67 p67eIF2 Peptidase M 2 >Methionine aminopeptidase 2 MAGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSAAGEQEPDKES GASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKKKKKKKKRGPKVQTDPPSVPI CDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVR KYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTT VLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDV GEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEV YAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWL DRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY >1437 bp ATGGCGGGCGTGGAGGAGGTAGCGGCCTCCGGGAGCCACCTGAATGGCGACCTGGATCCA GACGACAGGGAAGAAGGAGCTGCCTCTACGGCTGAGGAAGCAGCCAAGAAAAAAAGACGA AAGAAGAAGAAGAGCAAAGGGCCTTCTGCAGCAGGGGAACAGGAACCTGATAAAGAATCA GGAGCCTCAGTGGATGAAGTAGCAAGACAGTTGGAAAGATCAGCATTGGAAGATAAAGAA AGAGATGAAGATGATGAAGATGGAGATGGCGATGGAGATGGAGCAACTGGAAAGAAGAAG AAAAAGAAGAAGAAGAAGAGAGGACCAAAAGTTCAAACAGACCCTCCCTCAGTTCCAATA TGTGACCTGTATCCTAATGGTGTATTTCCCAAAGGACAAGAATGCGAATACCCACCCACA CAAGATGGGCGAACAGCTGCTTGGAGAACTACAAGTGAAGAAAAGAAAGCATTAGATCAG GCAAGTGAAGAGATTTGGAATGATTTTCGAGAAGCTGCAGAAGCACATCGACAAGTTAGA AAATACGTAATGAGCTGGATCAAGCCTGGGATGACAATGATAGAAATCTGTGAAAAGTTG GAAGACTGTTCACGCAAGTTAATAAAAGAGAATGGATTAAATGCAGGCCTGGCATTTCCT ACTGGATGTTCTCTCAATAATTGTGCTGCCCATTATACTCCCAATGCCGGTGACACAACA GTATTACAGTATGATGACATCTGTAAAATAGACTTTGGAACACATATAAGTGGTAGGATT ATTGACTGTGCTTTTACTGTCACTTTTAATCCCAAATATGATACGTTATTAAAAGCTGTA AAAGATGCTACTAACACTGGAATAAAGTGTGCTGGAATTGATGTTCGTCTGTGTGATGTT GGTGAGGCCATCCAAGAAGTTATGGAGTCCTATGAAGTTGAAATAGATGGGAAGACATAT CAAGTGAAACCAATCCGTAATCTAAATGGACATTCAATTGGGCAATATAGAATACATGCT GGAAAAACAGTGCCGATTGTGAAAGGAGGGGAGGCAACAAGAATGGAGGAAGGAGAAGTA TATGCAATTGAAACCTTTGGTAGTACAGGAAAAGGTGTTGTTCATGATGATATGGAATGT TCACATTACATGAAAAATTTTGATGTTGGACATGTGCCAATAAGGCTTCCAAGAACAAAA CACTTGTTAAATGTCATCAATGAAAACTTTGGAACCCTTGCCTTCTGCCGCAGATGGCTG GATCGCTTGGGAGAAAGTAAATACTTGATGGCTCTGAAGAATCTGTGTGACTTGGGCATT GTAGATCCATATCCACCATTATGTGACATTAAAGGATCATATACAGCGCAATTTGAACAT ACCATCCTGTTGCGTCCAACATGTAAAGAAGTTGTCAGCAGAGGAGATGACTATTAA PF00557 Peptidase_M24 function peptidase activity function metallopeptidase activity function exopeptidase activity function metalloexopeptidase activity function catalytic activity function aminopeptidase activity function methionyl aminopeptidase activity function hydrolase activity process protein metabolism process cellular protein metabolism process proteolysis process physiological process process metabolism process macromolecule metabolism BE0001308 Biphenyl-2,3-diol 1,2-dioxygenase Burkholderia xenovorans (strain LB400) # 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 Biphenyl-2,3-diol 1,2-dioxygenase Amino acid transport and metabolism Shows a preference for catechols with groups immediately adjacent to the hydroxyl substituents bphC None 5.99 32471.0 Burkholderia xenovorans (strain LB400) GenBank Gene Database X66122 GenBank Protein Database 397884 UniProtKB P47228 UniProt Accession BPHC_BURXL 2,3-dihydroxybiphenyl dioxygenase 23OHBP oxygenase DHBD EC 1.13.11.39 >Biphenyl-2,3-diol 1,2-dioxygenase MSIRSLGYMGFAVSDVAAWRSFLTQKLGLMEAGTTDNGDLFRIDSRAWRIAVQQGEVDDL AFAGYEVADAAGLAQMADKLKQAGIAVTTGDASLARRRGVTGLITFADPFGLPLEIYYGA SEVFEKPFLPGAAVSGFLTGEQGLGHFVRCVPDSDKALAFYTDVLGFQLSDVIDMKMGPD VTVPAYFLHCNERHHTLAIAAFPLPKRIHHFMLEVASLDDVGFAFDRVDADGLITSTLGR HTNDHMVSFYASTPSGVEVEYGWSARTVDRSWVVVRHDSPSMWGHKSVRDKAAARNKA >897 bp ATGAGCATCAGAAGTTTGGGATACATGGGGTTTGCGGTCAGCGACGTAGCTGCTTGGCGT TCGTTTCTGACGCAGAAACTGGGCTTGATGGAAGCGGGCACGACCGACAACGGCGACCTG TTCCGCATCGATTCGAGAGCCTGGCGGATCGCCGTTCAGCAGGGCGAGGTTGACGATCTG GCCTTTGCCGGCTACGAGGTGGCCGATGCGGCAGGGCTGGCGCAGATGGCTGACAAGCTC AAACAGGCCGGTATCGCAGTCACCACCGGCGATGCCTCATTGGCCAGGCGCCGCGGGGTG ACCGGATTGATCACCTTTGCCGACCCGTTTGGCCTGCCGTTGGAAATTTACTATGGCGCC AGCGAGGTGTTCGAAAAACCGTTCCTGCCTGGTGCGGCCGTGTCGGGTTTCCTGACCGGC GAGCAAGGGCTGGGGCATTTCGTGCGCTGCGTTCCGGATTCGGACAAGGCGCTGGCGTTT TATACCGACGTGCTCGGCTTCCAGTTGTCTGACGTCATCGACATGAAAATGGGGCCGGAC GTGACGGTTCCTGCGTACTTCCTGCACTGCAACGAACGCCACCACACCCTGGCAATTGCG GCATTCCCGCTGCCAAAACGCATTCATCACTTCATGCTCGAAGTCGCCTCGCTCGATGAC GTCGGCTTTGCATTTGATCGGGTTGACGCGGACGGCTTGATCACCTCCACGCTGGGGCGC CACACCAATGACCACATGGTGTCGTTCTATGCCTCGACCCCGTCCGGAGTAGAGGTCGAG TATGGCTGGAGTGCCCGTACCGTTGACCGCTCCTGGGTTGTGGTGAGGCACGACAGTCCG AGCATGTGGGGCCACAAGTCTGTGCGCGACAAAGCAGCTGCGCGCAACAAAGCATGA PF00903 Glyoxalase function catalytic activity function ion binding function cation binding function transition metal ion binding function iron ion binding function ferrous iron binding function binding process metabolism process cellular metabolism process aromatic compound metabolism process physiological process BE0000418 Calmodulin 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 Calmodulin Involved in calcium ion binding Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases CALM1 14q24-q31 None 3.84 16707.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:1442 GenAtlas CALM1 GeneCards CALM1 GenBank Gene Database J04046 GenBank Protein Database 179888 UniProtKB P62158 UniProt Accession CALM_HUMAN CaM >Calmodulin ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEEFVQMMTAK >450 bp ATGGCTGACCAGCTGACTGAGGAGCAGATTGCAGAGTTCAAGGAGGCCTTCTCCCTCTTT GACAAGGATGGAGATGGCACTATCACCACCAAGGAGTTGGGGACAGTGATGAGATCCCTG GGACAGAACCCCACTGAAGCAGAGCTGCAGGATATGATCAATGAGGTGGATGCAGATGGG AACGGGACCATTGACTTCCCGGAGTTCCTGACCATGATGGCCAGAAAGATGAAGGACACA GACAGTGAGGAGGAGATCCGAGAGGCGTTCCGTGTCTTTGACAAGGATGGGAATGGCTAC ATCAGCGCCGCAGAGCTGCGTCACGTAATGACGAACCTGGGGGAGAAGCTGACCGATGAG GAGGTGGATGAGATGATCAGGGAGGCTGACATCGATGGAGATGGCCAGGTCAATTATGAA GAGTTTGTACAGATGATGACTGCAAAGTGA PF00036 efhand function cation binding function calcium ion binding function binding function ion binding "
rdfs:label	"2-Methyl-2-Propanol"

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

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