Structure of PDB 7yly Chain q

Receptor sequence
>7ylyq (length=541) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SLRLPQNPNAGLFKQGYNSYSNADGQIIKSIAAIRELHQMCLTSMGPCGR
NKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTN
LVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEIT
DKNDKNELLKMIKPVISSKKYGSEDILSELVSEAVSHVLPVAQQAGEIPY
FNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEGHVKSLSEDKKHKVAVFT
CPLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVA
GAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEE
LGLVETVKTMEIGGDRVTVFKQEQGEISRTSTIILRGATQNNLDDIERAI
DDGVAAVKGLMKPSGGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQ
FAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNVTDHLYKGVDIDGESDEG
VKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAKK
3D structure
PDB7yly Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.
Chainq
Resolution3.05 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 q M46 D98 G99 N101 S169 A423 I517 M45 D97 G98 N100 S168 A422 I509
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0051086 chaperone mediated protein folding independent of cofactor
Cellular Component
GO:0005737 cytoplasm
GO:0005832 chaperonin-containing T-complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7yly, PDBe:7yly, PDBj:7yly
PDBsum7yly
PubMed36921056
UniProtP47079|TCPQ_YEAST T-complex protein 1 subunit theta (Gene Name=CCT8)

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