Structure of PDB 7x0v Chain A Binding Site BS02

Receptor Information
>7x0v 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 IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain7x0v Chain A Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7x0v Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM.
Resolution3.2 Å
Binding residue
(original residue number in PDB)		D88 S155
Binding residue
(residue number reindexed from 1)		D86 S153
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:7x0v, PDBe:7x0v, PDBj:7x0v
PDBsum7x0v
PubMed37193829
UniProtP17987|TCPA_HUMAN T-complex protein 1 subunit alpha (Gene Name=TCP1)

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