Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB07648"
| Predicate | Value (sorted: none) |
|---|---|
| rdf:type | |
| ns1:description |
"
experimental
This compound belongs to the stilbenes. These are organic compounds containing a 1,2-diphenylethylene moiety. Stilbenes (C6-C2-C6 ) are derived from the common phenylpropene (C6-C3) skeleton building block. The introduction of one or more hydroxyl groups to a phenyl ring lead to stilbenoids.
Stilbenes
Organic Compounds
Phenylpropanoids and Polyketides
Stilbenes
Phenylpyrroles
Pyrrolopyrimidines
Aminopyrimidines and Derivatives
Benzene and Substituted Derivatives
1,2-Diols
Secondary Alcohols
1,2-Aminoalcohols
Polyamines
Primary Alcohols
Secondary Amines
3-phenylpyrrole
2-phenylpyrrole
pyrrolopyrimidine
aminopyrimidine
pyrimidine
substituted pyrrole
benzene
pyrrole
1,2-aminoalcohol
secondary alcohol
1,2-diol
secondary amine
polyamine
primary alcohol
alcohol
amine
organonitrogen compound
logP
2.58
ALOGPS
logS
-4.1
ALOGPS
Water Solubility
2.75e-02 g/l
ALOGPS
logP
2.48
ChemAxon
IUPAC Name
(2R)-3-({5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl}amino)propane-1,2-diol
ChemAxon
Traditional IUPAC Name
(2R)-3-({5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl}amino)propane-1,2-diol
ChemAxon
Molecular Weight
360.4091
ChemAxon
Monoisotopic Weight
360.158625904
ChemAxon
SMILES
[H][C@](O)(CO)CNC1=C2C(NC(=C2C2=CC=CC=C2)C2=CC=CC=C2)=NC=N1
ChemAxon
Molecular Formula
C21H20N4O2
ChemAxon
InChI
InChI=1S/C21H20N4O2/c26-12-16(27)11-22-20-18-17(14-7-3-1-4-8-14)19(15-9-5-2-6-10-15)25-21(18)24-13-23-20/h1-10,13,16,26-27H,11-12H2,(H2,22,23,24,25)/t16-/m1/s1
ChemAxon
InChIKey
InChIKey=TWEONIHFGKSPLC-MRXNPFEDSA-N
ChemAxon
Polar Surface Area (PSA)
94.06
ChemAxon
Refractivity
106.67
ChemAxon
Polarizability
38.77
ChemAxon
Rotatable Bond Count
6
ChemAxon
H Bond Acceptor Count
5
ChemAxon
H Bond Donor Count
4
ChemAxon
pKa (strongest acidic)
12.27
ChemAxon
pKa (strongest basic)
7.07
ChemAxon
Physiological Charge
1
ChemAxon
Number of Rings
4
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
Ghose Filter
true
ChemAxon
MDDR-Like Rule
true
ChemAxon
PubChem Compound
4369435
PubChem Substance
99444119
ChemSpider
3571997
PDB
DF2
BE0003382
Serine/threonine-protein kinase Chk1
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
Serine/threonine-protein kinase Chk1
Involved in protein kinase activity
Required for checkpoint mediated cell cycle arrest in response to DNA damage or the presence of unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Recognizes the substrate consensus sequence [R-X-X- S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser- 293' promotes proteolysis of CDC25A. Inhibition of CDC25 activity leads to increased inhibitory tyrosine phosphorylation of CDK- cyclin complexes and blocks cell cycle progression. Binds to and phosphorylates RAD51 at 'Thr-309', which may enhance the association of RAD51 with chromatin and promote DNA repair by homologous recombination. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may affect chromatin assembly during S phase or DNA repair. May also phosphorylate multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and enhances suppression of cellular proliferation
CHEK1
11q24-q24
Nucleus. Cytoplasm
None
8.38
54420.0
Human
HUGO Gene Nomenclature Committee (HGNC)
HGNC:1925
GenAtlas
CHEK1
GenBank Gene Database
AF016582
UniProtKB
O14757
UniProt Accession
CHK1_HUMAN
EC 2.7.11.1
>Serine/threonine-protein kinase Chk1
MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINK
MLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVY
LHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLK
RREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLA
LLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGFSKHIQSNLDF
SPVNSASSEENVKYSSSQPEPRTGLSLWDTSPSYIDKLVQGISFSQPTCPDHMLLNSQLL
GTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETCEKLGYQWKKSCMNQVTISTTDRR
NNKLIFKVNLLEMDDKILVDFRLSKGDGLEFKRHFLKIKGKLIDIVSSQKVWLPAT
>1431 bp
ATGGCAGTGCCCTTTGTGGAAGACTGGGACTTGGTGCAAACCCTGGGAGAAGGTGCCTAT
GGAGAAGTTCAACTTGCTGTGAATAGAGTAACTGAAGAAGCAGTCGCAGTGAAGATTGTA
GATATGAAGCGTGCCGTAGACTGTCCAGAAAATATTAAGAAAGAGATCTGTATCAATAAA
ATGCTAAATCATGAAAATGTAGTAAAATTCTATGGTCACAGGAGAGAAGGCAATATCCAA
TATTTATTTCTGGAGTACTGTAGTGGAGGAGAGCTTTTTGACAGAATAGAGCCAGACATA
GGCATGCCTGAACCAGATGCTCAGAGATTCTTCCATCAACTCATGGCAGGGGTGGTTTAT
CTGCATGGTATTGGAATAACTCACAGGGATATTAAACCAGAAAATCTTCTGTTGGATGAA
AGGGATAACCTCAAAATCTCAGACTTTGGCTTGGCAACAGTATTTCGGTATAATAATCGT
GAGCGTTTGTTGAACAAGATGTGTGGTACTTTACCATATGTTGCTCCAGAACTTCTGAAG
AGAAGAGAATTTCATGCAGAACCAGTTGATGTTTGGTCCTGTGGAATAGTACTTACTGCA
ATGCTCGCTGGAGAATTGCCATGGGACCAACCCAGTGACAGCTGTCAGGAGTATTCTGAC
TGGAAAGAAAAAAAAACATACCTCAACCCTTGGAAAAAAATCGATTCTGCTCCTCTAGCT
CTGCTGCATAAAATCTTAGTTGAGAATCCATCAGCAAGAATTACCATTCCAGACATCAAA
AAAGATAGATGGTACAACAAACCCCTCAAGAAAGGGGCAAAAAGGCCCCGAGTCACTTCA
GGTGGTGTGTCAGAGTCTCCCAGTGGATTTTCTAAGCACATTCAATCCAATTTGGACTTC
TCTCCAGTAAACAGTGCTTCTAGTGAAGAAAATGTGAAGTACTCCAGTTCTCAGCCAGAA
CCCCGCACAGGTCTTTCCTTATGGGATACCAGCCCCTCATACATTGATAAATTGGTACAA
GGGATCAGCTTTTCCCAGCCCACATGTCCTGATCATATGCTTTTGAATAGTCAGTTACTT
GGCACCCCAGGATCCTCACAGAACCCCTGGCAGCGGTTGGTCAAAAGAATGACACGATTC
TTTACCAAATTGGATGCAGACAAATCTTATCAATGCCTGAAAGAGACTTGTGAGAAGTTG
GGCTATCAATGGAAGAAAAGTTGTATGAATCAGGTTACTATATCAACAACTGATAGGAGA
AACAATAAACTCATTTTCAAAGTGAATTTGTTAGAAATGGATGATAAAATATTGGTTGAC
TTCCGGCTTTCTAAGGGTGATGGATTGGAGTTCAAGAGACACTTCCTGAAGATTAAAGGG
AAGCTGATTGATATTGTGAGCAGCCAGAAGGTTTGGCTTCCTGCCACATGA
PF00069
Pkinase
function
nucleotide binding
function
purine nucleotide binding
function
adenyl nucleotide binding
function
binding
function
transferase activity
function
ATP binding
function
catalytic activity
function
transferase activity, transferring phosphorus-containing groups
function
kinase activity
function
protein kinase activity
function
protein serine/threonine kinase activity
process
protein modification
process
physiological process
process
metabolism
process
macromolecule metabolism
process
biopolymer metabolism
process
protein amino acid phosphorylation
process
biopolymer modification
"
|
| rdfs:label |
"(2R)-3-{[(4Z)-5,6-DIPHENYL-6,7-DIHYDRO-4H-PYRROLO[2,3-D]PYRIMIDIN-4-YLIDENE]AMINO}PROPANE-1,2-DIOL"
|
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines/drugbank_small.nt
The resource does not appear as an object