Structure of PDB 6ks6 Chain A

Receptor sequence

>6ks6A (length=550) Species: 559292 (Saccharomyces cerevisiae S288C)

MSQLFNNSRSDTLFLGGEKISGDDIRNQNVLATMAVANVVKSSLGPVGLD
KMLVDDIGDFTVTNDGATILSLLDVQHPAGKILVELAQQQDREIGDGTTS
VVIIASELLKRANELVKNKIHPTTIITGFRVALREAIRFINEVLSTSVDT
LGKETLINIAKTSMSSKIIGADSDFFSNMVVDALLAVKTQNSKGEIKYPV
KAVNVLKAHGKSATESLLVPGYALNCTVASQAMPKRIAGGNVKIACLDLN
LQKARMAMGVQINIDDPEQLEQIRKREAGIVLERVKKIIDAGAQVVLTTK
GIDDLCLKEFVEAKIMGVRRCKKEDLRRIARATGATLVSSMSNLEGEETF
ESSYLGLCDEVVQAKFSDDECILIKGTSKHSSSSIILRGANDYSLDEMER
SLHDSLSVVKRTLESGNVVPGGGCVEAALNIYLDNFATTVGSREQLAIAE
FAAALLIIPKTLAVNAAKDSSELVAKLRSYHAASQMAKPEDVKRRSYRNY
GLDLIRGKIVDEIHAGVLEPTISKVKSLKSALEACVAILRIDTMITVDPE

3D structure

• PDB: 6ks6 An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
• Chain: A
• Resolution: 2.99 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D65 T98 T99 D404
• Catalytic site (residue number reindexed from 1): D65 T98 T99 D404

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	A	L44 P46 G97 T99 T162 S165 S166 G421 G422 V517	L44 P46 G97 T99 T162 S165 S166 G421 G422 V517
BS02	AF3	A	D65 T98 T99 K167 D404	D65 T98 T99 K167 D404

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• 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
• GO:0005886 plasma membrane

External links

• PDB: RCSB:6ks6, PDBe:6ks6, PDBj:6ks6
• PDBsum: 6ks6
• PubMed: 31492816
• UniProt: P12612|TCPA_YEAST T-complex protein 1 subunit alpha (Gene Name=TCP1)