Structure of PDB 7nvo Chain h

Receptor sequence
>7nvoh (length=252) Species: 9606 (Homo sapiens) [Search protein sequence]
TDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDG
ATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYV
EEGLHPQIIIRAFRTATQLAVNKIKEIAVTDSVVAGGGAIEMELSKYLRD
YSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGG
TWYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKN
PR
3D structure
PDB7nvo Snapshots of actin and tubulin folding inside the TRiC chaperonin.
Chainh
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 h P42 D92 G93 G408 G409 L449 I479 V492 E494 P30 D80 G81 G136 G137 L177 I207 V220 E222
BS02 AF3 h T94 T95 T82 T83
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein 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: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:0005737 cytoplasm
GO:0005829 cytosol
GO:0005832 chaperonin-containing T-complex
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
UniProtQ99832|TCPH_HUMAN T-complex protein 1 subunit eta (Gene Name=CCT7)

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