Structure of PDB 7nvn Chain g Binding Site BS01
Receptor Information
>7nvn Chain g (length=523) Species:
9606
(Homo sapiens) [
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PVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMG
GIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEM
LSVAEHFLEQQMHPTVVISAYRKALDDMISTLKKISIPVDISDSDMMLNI
INSSITTKAISRWSSLACNIALDAVKMVQFEENGRKEIDIKKYARVEKIP
GGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTD
IEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLM
RANITAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIKKI
GDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDP
QLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNC
GASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKELGIWEPLAVKLQT
YKTAVETAVLLLRIDDIVSGHKK
Ligand information
Ligand ID
ADP
InChI
InChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKey
XTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341
Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04
O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341
Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
Formula
C10 H15 N5 O10 P2
Name
ADENOSINE-5'-DIPHOSPHATE
ChEMBL
CHEMBL14830
DrugBank
DB16833
ZINC
ZINC000012360703
PDB chain
7nvn Chain g Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
7nvn
Snapshots of actin and tubulin folding inside the TRiC chaperonin.
Resolution
3.0 Å
Binding residue
(original residue number in PDB)
L41 P43 G94 T96 S97 T162 G410 G411 G482 K502
Binding residue
(residue number reindexed from 1)
L36 P38 G89 T91 S92 T157 G405 G406 G477 K497
Annotation score
5
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0003723
RNA binding
GO:0005515
protein binding
GO:0005524
ATP binding
GO:0016887
ATP hydrolysis activity
GO:0044183
protein folding chaperone
GO:0051082
unfolded protein binding
GO:0140662
ATP-dependent protein folding chaperone
Biological Process
GO:0006457
protein folding
GO:0007339
binding of sperm to zona pellucida
GO:0032212
positive regulation of telomere maintenance via telomerase
GO:0050821
protein stabilization
GO:0051086
chaperone mediated protein folding independent of cofactor
GO:0061077
chaperone-mediated protein folding
GO:1904871
positive regulation of protein localization to Cajal body
GO:1904874
positive regulation of telomerase RNA localization to Cajal body
Cellular Component
GO:0002199
zona pellucida receptor complex
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0005832
chaperonin-containing T-complex
GO:0005856
cytoskeleton
GO:0005874
microtubule
GO:0044297
cell body
GO:0070062
extracellular exosome
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:7nvn
,
PDBe:7nvn
,
PDBj:7nvn
PDBsum
7nvn
PubMed
35449234
UniProt
P49368
|TCPG_HUMAN T-complex protein 1 subunit gamma (Gene Name=CCT3)
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