Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB07986"

Predicate	Value (sorted: default)
rdfs:label	"[4-(4-PHENYL-PIPERIDIN-1-YL)-BENZENESULFONYLAMINO]-ACETIC ACID"
rdf:type	drugbank:drugs
drugbank:description	" experimental This compound belongs to the phenylpiperidines. These are compounds containing a phenylpiperidine skeleton, which consists of a piperidine bound to a phenyl group. Phenylpiperidines Organic Compounds Heterocyclic Compounds Piperidines Phenylpiperidines Aminobenzenesulfonamides Alpha Amino Acids and Derivatives Sulfonamides Sulfonyls Tertiary Amines Carboxylic Acids Enolates Polyamines alpha-amino acid or derivative benzenesulfonamide benzene sulfonic acid derivative sulfonamide sulfonyl tertiary amine polyamine carboxylic acid derivative carboxylic acid enolate amine organonitrogen compound logP 2.14 ALOGPS logS -4.5 ALOGPS Water Solubility 1.27e-02 g/l ALOGPS logP 1.97 ChemAxon IUPAC Name 2-{[4-(4-phenylpiperidin-1-yl)benzene]sulfonamido}acetic acid ChemAxon Traditional IUPAC Name 4-(4-phenylpiperidin-1-yl)benzenesulfonamidoacetic acid ChemAxon Molecular Weight 374.454 ChemAxon Monoisotopic Weight 374.130027892 ChemAxon SMILES OC(=O)CNS(=O)(=O)C1=CC=C(C=C1)N1CCC(CC1)C1=CC=CC=C1 ChemAxon Molecular Formula C19H22N2O4S ChemAxon InChI InChI=1S/C19H22N2O4S/c22-19(23)14-20-26(24,25)18-8-6-17(7-9-18)21-12-10-16(11-13-21)15-4-2-1-3-5-15/h1-9,16,20H,10-14H2,(H,22,23) ChemAxon InChIKey InChIKey=GNSLACGSDSJAIQ-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 86.71 ChemAxon Refractivity 100.41 ChemAxon Polarizability 40.03 ChemAxon Rotatable Bond Count 5 ChemAxon H Bond Acceptor Count 5 ChemAxon H Bond Donor Count 2 ChemAxon pKa (strongest acidic) 2.61 ChemAxon pKa (strongest basic) 3.24 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 3 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 1948 PubChem Substance 99444457 ChemSpider 1872 PDB IN7 BE0001116 Stromelysin-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 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 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 "

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

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