Structure of PDB 7x3j Chain Z Binding Site BS01
Receptor Information
>7x3j Chain Z (length=514) Species:
9606
(Homo sapiens) [
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VARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNV
LLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISE
GLHPRIITEGFEAAKEKALQFLEEVKVSREMDRETLIDVARTSLRTKVHA
ELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVL
DHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKA
ERKFIEDRVKKIIELKRKVCGDSDKGFVVINQKGIDPFSLDALSKEGIVA
LRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTF
IEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAG
AVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQET
LVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIA
TNILLVDEIMRAGM
Ligand information
Ligand ID
ATP
InChI
InChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKey
ZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=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[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04
O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341
Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
Formula
C10 H16 N5 O13 P3
Name
ADENOSINE-5'-TRIPHOSPHATE
ChEMBL
CHEMBL14249
DrugBank
DB00171
ZINC
ZINC000004261765
PDB chain
7x3j Chain Z Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
7x3j
Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.
Resolution
4.2 Å
Binding residue
(original residue number in PDB)
L38 G39 D90 G91 T92 T93 R157 T158 A411 D496
Binding residue
(residue number reindexed from 1)
L26 G27 D78 G79 T80 T81 R145 T146 A399 D484
Annotation score
5
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
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Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:7x3j
,
PDBe:7x3j
,
PDBj:7x3j
PDBsum
7x3j
PubMed
37193829
UniProt
P40227
|TCPZ_HUMAN T-complex protein 1 subunit zeta (Gene Name=CCT6A)
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