Structure of PDB 7x3u Chain b Binding Site BS01

Receptor Information
>7x3u Chain b (length=517) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDA
SLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTSVTVLAAEL
LREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSDEVKFRQDL
MNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHIIKKLGGSL
ADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKIFGSRVRVD
STAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPEQLFGAAGV
MAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEEVMIGEDKL
IHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTVKDSRTVYG
GGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIADNAGYDSA
DLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKRQVLLSAAE
AAEVILRVDNIIKAAPR
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 chain7x3u Chain b 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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PDB7x3u Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.
Resolution3.3 Å
Binding residue
(original residue number in PDB)		D97 G98 T100 T165 S168 G410 I493 E495
Binding residue
(residue number reindexed from 1)		D88 G89 T91 T156 S159 G401 I484 E486
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:0031625 ubiquitin protein ligase 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:0051131 chaperone-mediated protein complex assembly
GO:0061077 chaperone-mediated protein folding
GO:0090666 scaRNA localization to Cajal body
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:0005737 cytoplasm
GO:0005829 cytosol
GO:0005832 chaperonin-containing T-complex
GO:0005874 microtubule
GO:0035578 azurophil granule lumen
GO:0044297 cell body
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7x3u, PDBe:7x3u, PDBj:7x3u
PDBsum7x3u
PubMed37193829
UniProtP78371|TCPB_HUMAN T-complex protein 1 subunit beta (Gene Name=CCT2)

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