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Predicate	Value (sorted: default)
rdfs:label	"(5r)-5-Amino-6-Hydroxyhexylcarbamic Acid"
rdf:type	drugbank:drugs
drugbank:description	" experimental This compound belongs to the polyols. These are organic compounds containing more than one hydroxyl groups. Polyols Organic Compounds Organooxygen Compounds Alcohols and Polyols Polyols 1,2-Aminoalcohols Carbamic Acids Primary Alcohols Polyamines Monoalkylamines polyamine primary alcohol primary amine amine primary aliphatic amine organonitrogen compound logP -2.7 ALOGPS logS -0.83 ALOGPS Water Solubility 2.63e+01 g/l ALOGPS logP -3 ChemAxon IUPAC Name [(5S)-5-amino-6-hydroxyhexyl]carbamic acid ChemAxon Traditional IUPAC Name (5S)-5-amino-6-hydroxyhexylcarbamic acid ChemAxon Molecular Weight 176.2135 ChemAxon Monoisotopic Weight 176.116092388 ChemAxon SMILES N[C@H](CO)CCCCNC(O)=O ChemAxon Molecular Formula C7H16N2O3 ChemAxon InChI InChI=1S/C7H16N2O3/c8-6(5-10)3-1-2-4-9-7(11)12/h6,9-10H,1-5,8H2,(H,11,12)/t6-/m0/s1 ChemAxon InChIKey InChIKey=XHKWPAAHPLALGC-LURJTMIESA-N ChemAxon Polar Surface Area (PSA) 95.58 ChemAxon Refractivity 44.24 ChemAxon Polarizability 19.06 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 4 ChemAxon pKa (strongest acidic) 4.13 ChemAxon pKa (strongest basic) 9.83 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon PubChem Compound 17754062 PubChem Substance 46504643 ChemSpider 3674681 PDB LCX BE0001801 Isoaspartyl dipeptidase 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 Isoaspartyl dipeptidase Nucleotide transport and metabolism Catalyzes the hydrolytic cleavage of a subset of L- isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu iadA Cytoplasm None 4.89 41084.0 Escherichia coli (strain K12) GenBank Gene Database U15029 GenBank Protein Database 640031 UniProtKB P39377 UniProt Accession IADA_ECOLI EC 3.4.19.- >Isoaspartyl dipeptidase MIDYTAAGFTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNCTVVDLSGQIL CPGFIDQHVHLIGGGGEAGPTTRTPEVALSRLTEAGVTSVVGLLGTDSISRHPESLLAKT RALNEEGISAWMLTGAYHVPSRTITGSVEKDVAIIDRVIGVKCAISDHRSAAPDVYHLAN MAAESRVGGLLGGKPGVTVFHMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQ ALEFARKGGTIDITSSIDEPVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLT HIGVAGFETLLETVQVLVKDYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMT PELRIEQVYARGKLMVKDGKACVKGTFETA >1173 bp ATGATTGATTATACCGCAGCCGGTTTTACCCTGCTGCAGGGAGCGCATTTGTATGCGCCG GAAGATCGGGGAATTTGCGATGTCCTCGTCGCTAACGGCAAAATTATCGCCGTTGCCAGC AATATCCCTTCTGACATTGTACCGAACTGCACGGTTGTCGATCTCAGTGGGCAGATCCTC TGCCCAGGTTTTATTGATCAACACGTCCATTTGATTGGCGGTGGCGGCGAAGCAGGTCCC ACGACGCGCACGCCGGAAGTGGCGCTAAGTCGCCTGACGGAAGCGGGCGTCACGTCAGTG GTTGGTCTGCTGGGCACCGACTCTATCTCTCGCCACCCGGAATCCCTGCTCGCCAAGACC CGTGCGCTCAATGAAGAAGGCATCAGCGCCTGGATGCTGACCGGCGCTTATCATGTCCCT TCCCGCACCATTACGGGTTCCGTGGAAAAAGACGTGGCGATTATCGATCGTGTGATTGGC GTGAAATGCGCCATCTCTGATCACCGTTCTGCCGCACCGGACGTTTATCACCTGGCCAAT ATGGCGGCAGAATCCCGCGTTGGCGGTTTGCTCGGCGGTAAACCTGGCGTCACCGTGTTC CACATGGGCGACAGTAAAAAGGCGTTACAGCCTATTTATGACCTGCTGGAAAACTGCGAT GTGCCGATCAGCAAGCTGCTGCCGACCCACGTTAACCGCAACGTACCGTTGTTTGAGCAG GCGCTGGAGTTCGCGCGCAAAGGCGGCACCATCGATATCACCAGCAGCATTGACGAACCG GTCGCCCCTGCCGAAGGTATTGCCCGCGCCGTTCAGGCGGGTATTCCGCTGGCACGCGTC ACCCTCAGCTCCGACGGCAACGGTAGCCAGCCGTTCTTCGATGACGAAGGGAATTTAACC CATATCGGTGTTGCCGGTTTTGAAACGTTGCTGGAAACCGTGCAGGTGCTGGTCAAAGAC TATGATTTCAGTATCAGCGATGCCCTGCGCCCGCTCACCAGTAGCGTAGCCGGTTTCCTT AACCTGACCGGGAAAGGCGAAATTCTGCCAGGCAATGATGCTGACTTGCTGGTCATGACG CCAGAACTGCGCATTGAGCAGGTATACGCTCGCGGCAAACTGATGGTCAAAGACGGCAAA GCCTGCGTGAAAGGAACGTTTGAAACGGCTTAA PF01979 Amidohydro_1 function catalytic activity function hydrolase activity BE0001535 Parathion hydrolase Flavobacterium sp. (strain ATCC 27551) # 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 Parathion hydrolase Involved in zinc ion binding Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate opd Cell membrane; peripheral membrane protein None 8.48 39004.0 Flavobacterium sp. (strain ATCC 27551) GenBank Gene Database M29593 GenBank Protein Database 148713 UniProtKB P0A433 UniProt Accession OPD_FLAS2 EC 3.1.8.1 Parathion hydrolase precursor Phosphotriesterase PTE >Parathion hydrolase precursor MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICG SSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAA DVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQ ELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYL TALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSN DWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSP TLRAS >1098 bp ATGCAAACGAGAAGGGTTGTGCTCAAGTCTGCGGCCGCCGCAGGAACTCTGCTCGGCGGC CTGGCTGGGTGCGCGAGCGTGGCTGGATCGATCGGCACAGGCGATCGGATCAATACCGTG CGCGGTCCTATCACAATCTCTGAAGCGGGTTTCACACTGACTCACGAGCACATCTGCGGC AGCTCGGCAGGATTCTTGCGTGCTTGGCCAGAGTTCTTCGGTAGCCGCAAAGCTCTAGCG GAAAAGGCTGTGAGAGGATTGCGCCGCGCCAGAGCGGCTGGCGTGCGAACGATTGTCGAT GTGTCGACTTTCGATATCGGTCGCGACGTCAGTTTATTGGCCGAGGTTTCGCGGGCTGCC GACGTTCATATCGTGGCGGCGACCGGCTTGTGGTTCGACCCGCCACTTTCGATGCGATTG AGGAGTGTAGAGGAACTCACACAGTTCTTCCTGCGTGAGATTCAATATGGCATCGAAGAC ACCGGAATTAGGGCGGGCATTATCAAGGTCGCGACCACAGGCAAGGCGACCCCCTTTCAG GAGTTAGTGTTAAAGGCGGCCGCCCGGGCCAGCTTGGCCACCGGTGTTCCGGTAACCACT CACACGGCAGCAAGTCAGCGCGATGGTGAGCAGCAGGCCGCCATTTTTGAGTCCGAAGGC TTGAGCCCCTCACGGGTTTGTATTGGTCACAGCGATGATACTGACGATTTGAGCTATCTC ACCGCCCTCGCTGCGCGCGGATACCTCATCGGTCTAGACCACATCCCGCACAGTGCGATT GGTCTAGAAGATAATGCGAGTGCATCAGCCCTCCTGGGCATCCGTTCGTGGCAAACACGG GCTCTCTTGATCAAGGCGCTCATCGACCAAGGCTACATGAAACAAATCCTCGTTTCGAAT GACTGGCTGTTCGGGTTTTCGAGCTATGTCACCAACATCATGGACGTGATGGATCGCGTG AACCCCGACGGGATGGCCTTCATTCCACTGAGAGTGATCCCATTCCTACGAGAGAAGGGC GTCCCACAGGAAACGCTGGCAGGCATCACTGTGACTAACCCGGCGCGGTTCTTGTCACCG ACCTTGCGGGCGTCATGA PF02126 PTE function catalytic activity function hydrolase activity function ion binding function cation binding function transition metal ion binding function zinc ion binding function hydrolase activity, acting on ester bonds function binding process metabolism process catabolism process physiological process BE0000124 Bifunctional protein FolC 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 Bifunctional protein FolC Coenzyme transport and metabolism Conversion of folates to polyglutamate derivatives folC None 5.59 45406.0 Escherichia coli (strain K12) GenBank Gene Database M32445 GenBank Protein Database 146020 UniProtKB P08192 UniProt Accession FOLC_ECOLI EC 6.3.2.17 Folylpoly-gamma-glutamate synthetase FPGS Tetrahydrofolate synthase >FolC bifunctional protein [Includes: Folylpolyglutamate synthase MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGK GTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTASFAEIESARGDIS LTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPD RESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSD AHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVI FDVAHNPHAAEYLTGRMKALPKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGP RGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLVCGSFHTVAHVMEVIDARRSG GK >1269 bp ATGATTATCAAACGCACTCCTCAAGCCGCGTCGCCTCTGGCTTCGTGGCTTTCTTATCTG GAAAACCTGCACAGTAAAACTATCGATCTCGGCCTTGAGCGCGTGAGCCTGGTCGCGGCG CGTCTTGGCGTCCTGAAACCAGCGCCATTTGTGTTTACCGTTGCGGGTACGAATGGCAAA GGCACCACCTGCCGTACGCTGGAGTCGATTCTGATGGCGGCAGGGTACAAAGTGGGCGTC TACAGTTCGCCTCATCTGGTGCGTTATACCGAGCGCGTACGTGTGCAGGGCCAGGAATTG CCGGAATCGGCCCACACCGCCTCTTTTGCGGAGATTGAATCGGCACGCGGTGATATTTCC CTGACCTATTTCGAGTACGGTACGCTGTCGGCGTTGTGGCTGTTCAAGCAGGCACAACTT GACGTGGTGATTCTGGAAGTAGGGCTGGGCGGTCGTCTGGACGCAACCAATATTGTCGAC GCCGATGTCGCGGTAGTAACCAGTATTGCGCTGGATCATACCGACTGGCTGGGTCCAGAT CGCGAAAGTATTGGTCGCGAGAAAGCAGGCATCTTCCGCAGCGAAAAACCGGCAATTGTC GGTGAGCCGGAAATGCCTTCTACCATTGCTGATGTGGCGCAGGAAAAAGGTGCACTGTTA CAACGTCGGGGCGTTGAGTGGAACTATTCCGTCACCGATCATGACTGGGCGTTTAGCGAT GCTCACGGCACGCTGGAAAATCTGCCGTTGCCGCTTGTCCCGCAACCGAATGCCGCAACA GCGCTGGCGGCACTGCGTGCCAGCGGGCTGGAAGTCAGTGAAAATGCCATTCGCGACGGG ATTGCCAGCGCAATTTTGCCGGGACGTTTCCAGATTGTGAGCGAGTCGCCACGCGTTATT TTTGATGTCGCGCATAATCCACATGCGGCGGAATATCTCACCGGGCGTATGAAAGCGCTA CCGAAAAACGGGCGCATGCTGGCGGTTATCGGTATGCTACATGATAAAGATATTGCCGGA ACTCTGGCCTGGTTGAAAAGCGTGGTTGATGACTGGTATTGTGCGCCACTGGAAGGGCCG CGCGGTGCCACGGCAGAACAACTGCTTGAGCATTTGGGTAACGGCAAATCATTTGATAGC GTTGCGCAGGCATGGGATGCCGCAATGGCGGACGCTAAAGCGGAAGACACCGTGCTGGTG TGTGGTTCTTTCCACACGGTCGCACATGTCATGGAAGTGATTGACGCGAGGAGAAGCGGT GGCAAGTAA PF02875 Mur_ligase_C PF08245 Mur_ligase_M function purine nucleotide binding function adenyl nucleotide binding function ATP binding function ligase activity function binding function catalytic activity function ligase activity, forming carbon-nitrogen bonds function acid-amino acid ligase activity function nucleotide binding function tetrahydrofolylpolyglutamate synthase activity process biosynthesis process aromatic compound metabolism process physiological process process folic acid and derivative metabolism process folic acid and derivative biosynthesis process metabolism process cellular metabolism "
owl:sameAs	drug:EXPT02012

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