Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB01742"
| Predicate | Value (sorted: none) |
|---|---|
| drugbank:description |
"
experimental
This compound belongs to the n-acylpiperidines. These are compounds containing an N-acyethanolamine moiety, which is characterized by an acyl group is linked to the nitrogen atom of a piperidine.
N-Acylpiperidines
Organic Compounds
Heterocyclic Compounds
Piperidines
N-Acylpiperidines
Tertiary Carboxylic Acid Amides
Tertiary Amines
Polyamines
Enolates
Carboxylic Acids
tertiary carboxylic acid amide
carboxamide group
tertiary amine
carboxylic acid derivative
polyamine
enolate
carboxylic acid
amine
organonitrogen compound
logP
0.91
ALOGPS
logS
-0.01
ALOGPS
Water Solubility
1.39e+02 g/l
ALOGPS
logP
0.63
ChemAxon
IUPAC Name
1-[(3R)-3-methylpiperidin-1-yl]ethan-1-one
ChemAxon
Traditional IUPAC Name
1-[(3R)-3-methylpiperidin-1-yl]ethanone
ChemAxon
Molecular Weight
141.2108
ChemAxon
Monoisotopic Weight
141.115364107
ChemAxon
SMILES
C[C@@H]1CCCN(C1)C(C)=O
ChemAxon
Molecular Formula
C8H15NO
ChemAxon
InChI
InChI=1S/C8H15NO/c1-7-4-3-5-9(6-7)8(2)10/h7H,3-6H2,1-2H3/t7-/m1/s1
ChemAxon
InChIKey
InChIKey=XKFPNHDGLSYZRC-SSDOTTSWSA-N
ChemAxon
Polar Surface Area (PSA)
20.31
ChemAxon
Refractivity
40.87
ChemAxon
Polarizability
16.56
ChemAxon
Rotatable Bond Count
0
ChemAxon
H Bond Acceptor Count
1
ChemAxon
H Bond Donor Count
0
ChemAxon
pKa (strongest basic)
0.018
ChemAxon
Physiological Charge
0
ChemAxon
Number of Rings
1
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
PubChem Compound
449120
PubChem Substance
46506076
ChemSpider
96569
PDB
1P3
BE0001014
Peptidyl-prolyl cis-trans isomerase A
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
Peptidyl-prolyl cis-trans isomerase A
Posttranslational modification, protein turnover, chaperones
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
PPIA
7p13
Cytoplasm
None
7.97
18013.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9253
GenAtlas
PPIA
GeneCards
PPIA
GenBank Gene Database
Y00052
GenBank Protein Database
30309
UniProtKB
P62937
UniProt Accession
PPIA_HUMAN
Cyclophilin A
Cyclosporin A-binding protein
EC 5.2.1.8
PPIase A
Rotamase A
>Peptidyl-prolyl cis-trans isomerase A
MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGF
MCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE
WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE
>498 bp
ATGGTCAACCCCACCGTGTTCTTCGACATTGCCGTCGACGGCGAGCCCTTGGGCCGCGTC
TCCTTTGAGCTGTTTGCAGACAAGGTCCCAAAGACAGCAGAAAATTTTCGTGCTCTGAGC
ACTGGAGAGAAAGGATTTGGTTATAAGGGTTCCTGCTTTCACAGAATTATTCCAGGGTTT
ATGTGTCAGGGTGGTGACTTCACACGCCATAATGGCACTGGTGGCAAGTCCATCTATGGG
GAGAAATTTGAAGATGAGAACTTCATCCTAAAGCATACGGGTCCTGGCATCTTGTCCATG
GCAAATGCTGGACCCAACACAAATGGTTCCCAGTTTTTCATCTGCACTGCCAAGACTGAG
TGGTTGGATGGCAAGCATGTGGTGTTTGGCAAAGTGAAAGAAGGCATGAATATTGTGGAG
GCCATGGAGCGCTTTGGGTCCAGGAATGGCAAGACCAGCAAGAAGATCACCATTGCTGAC
TGTGGACAACTCGAATAA
PF00160
Pro_isomerase
process
macromolecule metabolism
process
protein metabolism
process
cellular protein metabolism
process
protein folding
process
physiological process
process
metabolism
"
|
| owl:sameAs | |
| rdf:type | |
| rdfs:label |
"(3r)-1-Acetyl-3-Methylpiperidine"
|
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines2/drugbank_small.nt
The resource does not appear as an object