Structure of PDB 7x0s Chain E Binding Site BS01

Receptor Information
>7x0s Chain E (length=535) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPN
GLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDG
TTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSV
LVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVD
FELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPQMPKKVEDAKIAILTCPF
EPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWG
FDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGF
AGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDA
LCVIRNLIRDNRVVYGGGAAEISCALAVSQEADKCPTLEQYAMRAFADAL
EVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQH
VIETLIGKKQQISLATQMVRMILKIDDIRKPGESE
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 chain7x0s Chain E 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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PDB7x0s Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		L50 G51 P52 D102 G103 T104 T105 G420 I489 D490 V504 E506
Binding residue
(residue number reindexed from 1)		L47 G48 P49 D99 G100 T101 T102 G417 I486 D487 V501 E503
Annotation score5
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0003730 mRNA 3'-UTR binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0031681 G-protein beta-subunit binding
GO:0044183 protein folding chaperone
GO:0048027 mRNA 5'-UTR binding
GO:0048487 beta-tubulin 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:0009615 response to virus
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:0005813 centrosome
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7x0s, PDBe:7x0s, PDBj:7x0s
PDBsum7x0s
PubMed37193829
UniProtP48643|TCPE_HUMAN T-complex protein 1 subunit epsilon (Gene Name=CCT5)

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