Structure of PDB 7x0s Chain A Binding Site BS01
Receptor Information
>7x0s Chain A (length=537) Species:
9606
(Homo sapiens) [
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GPLSVFGDRSTGETIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDV
TITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLK
NADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAA
KTSMSSKIIGINGDFFANMVVDAVLAIKYTDIRGQPRYPVNSVNILKAHG
RSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQV
VITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVE
AGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEETFEAAMLGQAEEVV
QERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRV
LESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTL
AVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLSNGKPRDNKQAG
VFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKD
Ligand information
Ligand ID
ADP
InChI
InChI=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
InChIKey
XTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
c1nc(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 3.341
Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04
O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341
Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
Formula
C10 H15 N5 O10 P2
Name
ADENOSINE-5'-DIPHOSPHATE
ChEMBL
CHEMBL14830
DrugBank
DB16833
ZINC
ZINC000012360703
PDB chain
7x0s Chain A Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
7x0s
Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.
Resolution
3.1 Å
Binding residue
(original residue number in PDB)
L36 G37 P38 D88 G89 T90 T91 T154 G412 E505
Binding residue
(residue number reindexed from 1)
L34 G35 P36 D86 G87 T88 T89 T152 G410 E503
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: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:0007021
tubulin complex assembly
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:0090666
scaRNA localization to Cajal body
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:0000242
pericentriolar material
GO:0000792
heterochromatin
GO:0001669
acrosomal vesicle
GO:0002199
zona pellucida receptor complex
GO:0005737
cytoplasm
GO:0005794
Golgi apparatus
GO:0005813
centrosome
GO:0005815
microtubule organizing center
GO:0005829
cytosol
GO:0005832
chaperonin-containing T-complex
GO:0005856
cytoskeleton
GO:0005874
microtubule
GO:0044297
cell body
GO:0070062
extracellular exosome
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:7x0s
,
PDBe:7x0s
,
PDBj:7x0s
PDBsum
7x0s
PubMed
37193829
UniProt
P17987
|TCPA_HUMAN T-complex protein 1 subunit alpha (Gene Name=TCP1)
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