Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB07045"
| Predicate | Value (sorted: default) |
|---|---|
| rdfs:label |
"(2R,3R,4S,5R)-2-[6-amino-8-[(3,4-dichlorophenyl)methylamino]purin-9-yl]-5-(hydroxymethyl)oxolane-3,4-diol"
|
| rdf:type | |
| ns1:description |
"
experimental
This compound belongs to the purine nucleosides and analogues. These are compounds comprising a purine base attached to a sugar.
Purine Nucleosides and Analogues
Organic Compounds
Organooxygen Compounds
Carbohydrates and Carbohydrate Conjugates
Glycosyl Compounds
Pentoses
Purines and Purine Derivatives
Dichlorobenzenes
Aminopyrimidines and Derivatives
Aminoimidazoles
Aryl Chlorides
N-substituted Imidazoles
Primary Aromatic Amines
Tetrahydrofurans
Oxolanes
1,2-Diols
Secondary Alcohols
Primary Alcohols
Polyamines
Ethers
Secondary Amines
Organochlorides
pentose monosaccharide
imidazopyrimidine
purine
1,2-dichlorobenzene
aminopyrimidine
chlorobenzene
aminoimidazole
primary aromatic amine
aryl halide
aryl chloride
n-substituted imidazole
benzene
monosaccharide
pyrimidine
tetrahydrofuran
azole
imidazole
oxolane
secondary alcohol
1,2-diol
polyamine
secondary amine
primary alcohol
ether
primary amine
amine
alcohol
organochloride
organonitrogen compound
organohalogen
logP
1.39
ALOGPS
logS
-2.9
ALOGPS
Water Solubility
5.11e-01 g/l
ALOGPS
logP
1
ChemAxon
IUPAC Name
(2R,3R,4S,5R)-2-(6-amino-8-{[(3,4-dichlorophenyl)methyl]amino}-9H-purin-9-yl)-5-(hydroxymethyl)oxolane-3,4-diol
ChemAxon
Traditional IUPAC Name
(2R,3R,4S,5R)-2-(6-amino-8-{[(3,4-dichlorophenyl)methyl]amino}purin-9-yl)-5-(hydroxymethyl)oxolane-3,4-diol
ChemAxon
Molecular Weight
441.269
ChemAxon
Monoisotopic Weight
440.076658508
ChemAxon
SMILES
[H][C@]1(CO)O[C@@]([H])(N2C(NCC3=CC=C(Cl)C(Cl)=C3)=NC3=C(N)N=CN=C23)[C@]([H])(O)[C@]1([H])O
ChemAxon
Molecular Formula
C17H18Cl2N6O4
ChemAxon
InChI
InChI=1S/C17H18Cl2N6O4/c18-8-2-1-7(3-9(8)19)4-21-17-24-11-14(20)22-6-23-15(11)25(17)16-13(28)12(27)10(5-26)29-16/h1-3,6,10,12-13,16,26-28H,4-5H2,(H,21,24)(H2,20,22,23)/t10-,12-,13-,16-/m1/s1
ChemAxon
InChIKey
InChIKey=VBJKVZXRYLCYGQ-XNIJJKJLSA-N
ChemAxon
Polar Surface Area (PSA)
151.57
ChemAxon
Refractivity
107.08
ChemAxon
Polarizability
42.57
ChemAxon
Rotatable Bond Count
5
ChemAxon
H Bond Acceptor Count
9
ChemAxon
H Bond Donor Count
5
ChemAxon
pKa (strongest acidic)
12.45
ChemAxon
pKa (strongest basic)
4.7
ChemAxon
Physiological Charge
0
ChemAxon
Number of Rings
4
ChemAxon
Bioavailability
1
ChemAxon
Rule of Five
true
ChemAxon
Ghose Filter
true
ChemAxon
PubChem Compound
25195347
PubChem Substance
99443516
ChemSpider
23337032
PDB
3BK
BE0003774
BAG family molecular chaperone regulator 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
BAG family molecular chaperone regulator 1
Involved in protein binding
Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli
BAG1
9p12
Isoform 2:Cytoplasm. Nucleus
None
8.34
38877.6
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:937
GeneCards
BAG1
GenBank Gene Database
Z35491
GenBank Protein Database
1143476
UniProtKB
Q99933
UniProt Accession
BAG1_HUMAN
BAG-1
Bcl-2-associated athanogene 1
Glucocorticoid receptor-associated protein RAP46
>BAG family molecular chaperone regulator 1
MAQRGGARRPRGDRERLGSRLRALRPGREPRQSEPPAQRGPPPSRRPPARSTASGHDRPT
RGAAAGARRPRMKKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQ
EVTRDEESTRSEEVTREEMAAAGLTVTVTHSNEKHDLHVTSQQGSSEPVVQDLAQVVEEV
IGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLIGKKNSPQEEVELKKLKHLEKSV
EKIADQLEELNKELTGIQQGFLPKDLQAEALCKLDRRVKATIEQFMKILEEIDTLILPEN
FKDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFALAE
>825 bp
ATGAAGAAGAAAACCCGGCGCCGCTCGACCCGGAGCGAGGAGTTGACCCGGAGCGAGGAG
TTGACCCTGAGTGAGGAAGCGACCTGGAGTGAAGAGGCGACCCAGAGTGAGGAGGCGACC
CAGGGCGAAGAGATGAATCGGAGCCAGGAGGTGACCCGGGACGAGGAGTCGACCCGGAGC
GAGGAGGTGACCAGGGAGGAAATGGCGGCAGCTGGGCTCACCGTGACTGTCACCCACAGC
AATGAGAAGCACGACCTTCATGTTACCTCCCAGCAGGGCAGCAGTGAACCAGTTGTCCAA
GACCTGGCCCAGGTTGTTGAAGAGGTCATAGGGGTTCCACAGTCTTTTCAGAAACTCATA
TTTAAGGGAAAATCTCTGAAGGAAATGGAAACACCGTTGTCAGCACTTGGAATACAAGAT
GGTTGCCGGGTCATGTTAATTGGGAAAAAGAACAGTCCACAGGAAGAGGTTGAACTAAAG
AAGTTGAAACATTTGGAGAAGTCTGTGGAGAAGATAGCTGACCAGCTGGAAGAGTTGAAT
AAAGAGCTTACTGGAATCCAGCAGGGTTTTCTGCCCAAGGATTTGCAAGCTGAAGCTCTC
TGCAAACTTGATAGGAGAGTAAAAGCCACAATAGAGCAGTTTATGAAGATCTTGGAGGAG
ATTGACACACTGATCCTGCCAGAAAATTTCAAAGACAGTAGATTGAAAAGGAAAGGCTTG
GTAAAAAAGGTTCAGGCATTCCTAGCCGAGTGTGACACAGTGGAGCAGAACATCTGCCAG
GAGACTGAGCGGCTGCAGTCTACAAACTTTGCCCTGGCCGAGTGA
PF00240
ubiquitin
PF02179
BAG
function
protein binding
function
binding
process
biopolymer modification
process
protein modification
process
death
process
cell death
process
programmed cell death
process
apoptosis
process
physiological process
process
metabolism
process
macromolecule metabolism
process
biopolymer metabolism
BE0003775
Heat shock cognate 71 kDa protein
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
Heat shock cognate 71 kDa protein
Posttranslational modification, protein turnover, chaperones
Chaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co-chaperones
HSPA8
11q24.1
Cytoplasm. Melanosome
None
5.16
70897.6
Human
HUGO Gene Nomenclature Committee (HGNC)
GNC:5241
GeneCards
HSPA8
GenBank Gene Database
AB034951
GenBank Protein Database
11526573
UniProtKB
P11142
UniProt Accession
HSP7C_HUMAN
Heat shock 70 kDa protein 8
>Heat shock cognate 71 kDa protein
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA
MNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVS
SMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAA
IAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH
FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRA
RFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELN
KSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTI
PTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDI
DANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKN
SLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELE
KVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
>1482 bp
ATGTCCAAGGGACCTGCAGTTGGTATTGATCTTGGCACCACCTACTCTTGTGTGGGTGTT
TTCCAGCACGGAAAAGTCGAGATAATTGCCAATGATCAGGGAAACCGAACCACTCCAAGC
TATGTCGCCTTTACGGACACTGAACGGTTGATCGGTGATGCCGCAAAGAATCAAGTTGCA
ATGAACCCCACCAACACAGTTTTTGATGCCAAACGTCTGATTGGACGCAGATTTGATGAT
GCTGTTGTCCAGTCTGATATGAAACATTGGCCCTTTATGGTGGTGAATGATGCTGGCAGG
CCCAAGGTCCAAGTAGAATACAAGGGAGAGACCAAAAGCTTCTATCCAGAGGAGGTGTCT
TCTATGGTTCTGACAAAGATGAAGGAAATTGCAGAAGCCTACCTTGGGAAGACTGTTACC
AATGCTGTGGTCACAGTGCCAGCTTACTTTAATGACTCTCAGCGTCAGGCTACCAAAGAT
GCTGGAACTATTGCTGGTCTCAATGTACTTAGAATTATTAATGAGCCAACTGCTGCTGCT
ATTGCTTACGGCTTAGACAAAAAGGTTGGAGCAGAAAGAAACGTGCTCATCTTTGACCTG
GGAGGTGGCACTTTTGATGTGTCAATCCTCACTATTGAGGATGGAATCTTTGAGGTCAAG
TCTACAGCTGGAGACACCCACTTGGGTGGAGAAGATTTTGACAACCGAATGGTCAACCAT
TTTATTGCTGAGTTTAAGCGCAAGCATAAGAAGGACATCAGTGAGAACAAGAGAGCTGTA
AGACGCCTCCGTACTGCTTGTGAACGTGCTAAGCGTACCCTCTCTTCCAGCACCCAGGCC
AGTATTGAGATCGATTCTCTCTATGAAGGAATCGACTTCTATACCTCCATTACCCGTGCC
CGATTTGAAGAACTGAATGCTGACCTGTTCCGTGGCACCCTGGACCCAGTAGAGAAAGCC
CTTCGAGATGCCAAACTAGACAAGTCACAGATTCATGATATTGTCCTGGTTGGTGGTTCT
ACTCGTATCCCCAAGATTCAGAAGCTTCTCCAAGACTTCTTCAATGGAAAAGAACTGAAT
AAGAGCATCAACCCTGATGAAGCTGTTGCTTATGGTGCAGCTGTCCAGGCAGCCATCTTG
TCTGGAGACAAGTCTGAGAATGTTCAAGATTTGCTGCTCTTGGATGTCACTCCTCTTTCC
CTTGGTATTGAAACTGCTGGTGGAGTCATGACTGTCCTCATCAAGCGTAATACCACCATT
CCTACCAAGCAGACACAGACCTTCACTACCTATTCTGACAACCAGCCTGGTGTGCTTATT
CAGGTTTATGAAGGCGAGCGTGCCATGACAAAGGATAACAACCTGCTTGGCAAGTTTGAA
CTCACAGGCATGCCAGGAGGAATGCCTGGGGGATTTCCTGGTGGTGGAGCTCCTCCCTCT
GGTGGTGCTTCCTCAGGGCCCACCATTGAAGAGGTTGATTAA
PF00012
HSP70
function
purine nucleotide binding
function
adenyl nucleotide binding
function
ATP binding
function
binding
function
nucleotide binding
"
|
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines/drugbank_small.nt
The resource does not appear as an object