Structure of PDB 7x0s Chain K Binding Site BS01

Receptor Information
>7x0s Chain K (length=525) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGA
GDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGE
LLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMDRETLIDV
ARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSE
TDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYK
SAEEREKLVKAERKFIEDRVKKIIELKRKVCGDSDKGFVVINQKGIDPFS
LDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVY
EYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNA
IDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVL
AQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVK
KQLLHSCTVIATNILLVDEIMRAGM
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 K Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
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)		L38 P40 D90 G91 T93 T154 T158 A411 L481
Binding residue
(residue number reindexed from 1)		L37 P39 D89 G90 T92 T153 T157 A410 L480
Annotation score5
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:0071987 WD40-repeat domain binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
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:1904851 positive regulation of establishment of protein localization to telomere
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: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
UniProtP40227|TCPZ_HUMAN T-complex protein 1 subunit zeta (Gene Name=CCT6A)

[Back to BioLiP]