Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB06837"
| Predicate | Value (sorted: default) |
|---|---|
| rdfs:label |
"(2R)-N~4~-hydroxy-2-(3-hydroxybenzyl)-N~1~-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide"
|
| rdf:type | |
| drugbank: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
"
|
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt
The resource does not appear as an object