Structure of PDB 6ks6 Chain Q

Receptor sequence
>6ks6Q (length=548) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
SLRLPQNPNAGLFKQGYNSYSNADGQIIKSIAAIRELHQMCLTSMGPCGR
NKIIVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTN
LVMILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEIT
DKNDKNELLKMIKPVISSKKYGSEDILSELVSEAVSHVLPVAQQAGEIPY
FNVDSIRVVKIMGGSLSNSTVIKGMVFNREPEGHVKSLSEDKKHKVAVFT
CPLDIANTETKGTVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVA
GAGVGELALHYLNRYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEE
LGLVETVKTMEIGGDRVTVFKQEQGEISRTSTIILRGATQNNLDDIERAI
DDGVAAVKGLMKPSGGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQ
FAVAFEVVPRTLAETAGLDVNEVLPNLYAAHNVTEPGAVKTDHLYKGVDI
DGESDEGVKDIREENIYDMLATKKFAINVATEAATTVLSIDQIIMAKK
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 T100 N101 S169 K170 A423 I517 D519 M45 P47 D97 G98 T99 N100 S168 K169 A422 I516 D518
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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Biological Process
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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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