Structure of PDB 7nvn Chain H Binding Site BS01
Receptor Information
>7nvn Chain H (length=524) Species:
9606
(Homo sapiens) [
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MMPTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIV
DGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLL
AAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKADKVE
QRKLLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKV
QGGALEDSQLVAGVAFKKTFSYAGFEMQPKKYHNPKIALLNVELELKAEK
DNAEIRVHTVEDYQAIVDAEWNILYDKLEKIHHSGAKVVLSKLPIGDVAT
QYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSADVLGRCQVFEE
TQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAI
KNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLC
DNAGFDATNILNKLRARHAQGGTWYGVDINNEDIADNFEAFVWEPAMVRI
NALTAASEAACLIVSVDETIKNPR
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 H 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)
G41 D92 G93 T95 S164 S165 G408 G409 V492 E494 R499
Binding residue
(residue number reindexed from 1)
G41 D92 G93 T95 S164 S165 G408 G409 V492 E494 R499
Annotation score
5
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0005515
protein binding
GO:0005524
ATP binding
GO:0016887
ATP hydrolysis activity
GO:0042802
identical protein binding
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:0005737
cytoplasm
GO:0005829
cytosol
GO:0005832
chaperonin-containing T-complex
GO:0005874
microtubule
GO:0044297
cell body
GO:0070062
extracellular exosome
View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:7nvn
,
PDBe:7nvn
,
PDBj:7nvn
PDBsum
7nvn
PubMed
35449234
UniProt
Q99832
|TCPH_HUMAN T-complex protein 1 subunit eta (Gene Name=CCT7)
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