Structure of PDB 7x0s Chain a Binding Site BS02

Receptor Information
>7x0s Chain a (length=537) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GPLSVFGDRSTGETIRSQNVMAAASIANIVKSSLGPVGLDKMLVDDIGDV
TITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLK
NADELVKQKIHPTSVISGYRLACKEAVRYINENLIVNTDELGRDCLINAA
KTSMSSKIIGINGDFFANMVVDAVLAIKYTDIRGQPRYPVNSVNILKAHG
RSQMESMLISGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQV
VITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMCLKYFVE
AGAMAVRRVLKRDLKRIAKASGATILSTLANLEGEETFEAAMLGQAEEVV
QERICDDELILIKNTKARTSASIILRGANDFMCDEMERSLHDALCVVKRV
LESKSVVPGGGAVEAALSIYLENYATSMGSREQLAIAEFARSLLVIPNTL
AVNAAQDSTDLVAKLRAFHNEAQVNPERKNLKWIGLDLSNGKPRDNKQAG
VFEPTIVKVKSLKFATEAAITILRIDDLIKLHPESKD
Ligand information
Ligand IDAF3
InChIInChI=1S/Al.3FH/h;3*1H/q+3;;;/p-3
InChIKeyKLZUFWVZNOTSEM-UHFFFAOYSA-K
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		F[Al](F)F
FormulaAl F3
NameALUMINUM FLUORIDE
ChEMBL
DrugBank
ZINC
PDB chain7x0s Chain a Residue 603 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)		D57 T90 T91 K159 D394
Binding residue
(residue number reindexed from 1)		D55 T88 T89 K157 D392
Annotation score1
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
PDBsum7x0s
PubMed37193829
UniProtP17987|TCPA_HUMAN T-complex protein 1 subunit alpha (Gene Name=TCP1)

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