Structure of PDB 7nvo Chain G

Receptor sequence
>7nvoG (length=249) Species: 9606 (Homo sapiens) [Search protein sequence]
GRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILR
EIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMH
PTVVISAYRKALDDMISTLKKISIPVPQLVPGGGASEMAVAHALTEKSKA
MTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETW
GVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHK
3D structure
PDB7nvo Snapshots of actin and tubulin folding inside the TRiC chaperonin.
ChainG
Resolution3.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADP G L41 G42 D93 G94 T96 S97 G411 G482 L23 G24 D75 G76 T78 S79 G133 G204
BS02 AF3 G D93 T95 D75 T77
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:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
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:1904871 positive regulation of protein localization to Cajal body
GO:1904874 positive regulation of telomerase RNA localization to Cajal body
Cellular Component
GO:0002199 zona pellucida receptor complex
GO:0005737 cytoplasm
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:7nvo, PDBe:7nvo, PDBj:7nvo
PDBsum7nvo
PubMed35449234
UniProtP49368|TCPG_HUMAN T-complex protein 1 subunit gamma (Gene Name=CCT3)

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