Structure of PDB 7x0v Chain J Binding Site BS01

Receptor Information
>7x0v Chain J (length=527) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HVPKAPGFAQMLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMN
KMVINHLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVGDGTNF
VLVFAGALLELAEELLRIGLSVSEVIEGYEIACRKAHEILPNLVCCSAKN
LRDIDEVSSLLRTSIMSKQYGNEVFLAKLIAQACVSIFPDSGHFNVDNIR
VCKILGSGISSSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITET
KGTVLIKTAEELMNFSKGEENLMDAQVKAIADTGANVVVTGGKVADMALH
YANKYNIMLVRLNSKWDLRRLCKTVGATALPRLTPPVLEEMGHCDSVYLS
EVGDTQVVVFKHEKEDGAISTIVLRGSTDNLMDDIERAVDDGVNTFKVLT
RDKRLVPGGGATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALA
ENSGVKANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDMLEAGILDTYLG
KYWAIKLATNAAVTVLRVDQIIMAKPA
Ligand information
Ligand IDADP
InChIInChI=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
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(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 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain7x0v Chain J Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB7x0v Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.
Resolution3.2 Å
Binding residue
(original residue number in PDB)		Y47 G48 P49 D99 G100 T101 N102 F103 M169 G412 L452 I482 I497
Binding residue
(residue number reindexed from 1)		Y44 G45 P46 D96 G97 T98 N99 F100 M166 G409 L449 I479 I494
Annotation score5
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0044183 protein folding chaperone
GO:0045296 cadherin binding
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:0005576 extracellular region
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005813 centrosome
GO:0005829 cytosol
GO:0005832 chaperonin-containing T-complex
GO:0005856 cytoskeleton
GO:0005874 microtubule
GO:0005929 cilium
GO:0034774 secretory granule lumen
GO:0035578 azurophil granule lumen
GO:0044297 cell body
GO:0045111 intermediate filament cytoskeleton
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7x0v, PDBe:7x0v, PDBj:7x0v
PDBsum7x0v
PubMed37193829
UniProtP50990|TCPQ_HUMAN T-complex protein 1 subunit theta (Gene Name=CCT8)

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