Structure of PDB 6ks6 Chain a

Receptor sequence

>6ks6a (length=546) Species: 559292 (Saccharomyces cerevisiae S288C)

QLFNNSRSDTLFLGGEKISGDDIRNQNVLATMAVANVVKSSLGPVGLDKM
LVDDIGDFTVTNDGATILSLLDVQHPAGKILVELAQQQDREIGDGTTSVV
IIASELLKRANELVKNKIHPTTIITGFRVALREAIRFINEVLSTSVDTLG
KETLINIAKTSMSSKIIGADSDFFSNMVVDALLAVKTQNSKGEIKYPVKA
VNVLKAHGKSATESLLVPGYALNCTVASQAMPKRIAGGNVKIACLDLNLQ
KARMAMGVQINIDDPEQLEQIRKREAGIVLERVKKIIDAGAQVVLTTKGI
DDLCLKEFVEAKIMGVRRCKKEDLRRIARATGATLVSSMSNLEGEETFES
SYLGLCDEVVQAKFSDDECILIKGTSKHSSSSIILRGANDYSLDEMERSL
HDSLSVVKRTLESGNVVPGGGCVEAALNIYLDNFATTVGSREQLAIAEFA
AALLIIPKTLAVNAAKDSSELVAKLRSYHAASQMAKPEKRRSYRNYGLDL
IRGKIVDEIHAGVLEPTISKVKSLKSALEACVAILRIDTMITVDPE

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): D63 T96 T97 D402

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	P46 D96 G97 T99 S165 S166 G421 G422 V517	P44 D94 G95 T97 S163 S164 G419 G420 V513
BS02	AF3	a	D65 D96 T98 T99 K167 D404	D63 D94 T96 T97 K165 D402

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)