Structure of PDB 6ks6 Chain q

Receptor sequence
>6ks6q (length=541) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
SLRLPQNPNAGLFKQGYNSYSNADGQIIKSIAAIRELHQMCLTSMGPCGR
NKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTN
LVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEIT
DKNDKNELLKMIKPVISSKKYGSEDILSELVSEAVSHVLPVAQQAGEIPY
FNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEGHVKSLSEDKKHKVAVFT
CPLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVA
GAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEE
LGLVETVKTMEIGGDRVTVFKQEQGEISRTSTIILRGATQNNLDDIERAI
DDGVAAVKGLMKPSGGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQ
FAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNVTDHLYKGVDIDGESDEG
VKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAKK
3D structure
PDB6ks6 An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
Chainq
Resolution2.99 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D67 T100 N101 D403
Catalytic site (residue number reindexed from 1) D66 T99 N100 D402
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 P48 D98 G99 S168 S169 G422 A423 L463 I517 M45 P47 D97 G98 S167 S168 G421 A422 L462 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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Cellular Component
External links
PDB RCSB:6ks6, PDBe:6ks6, PDBj:6ks6
PDBsum6ks6
PubMed31492816
UniProtP47079|TCPQ_YEAST T-complex protein 1 subunit theta (Gene Name=CCT8)

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