Structure of PDB 4v94 Chain I

Receptor sequence

>4v94I (length=539) Species: 559292 (Saccharomyces cerevisiae S288C)

QLFNNSRSDTLFLGGEKISGDDIRNQNVLATMAVANVVKSSLGPVGLDKM
LVDDIGDFTVTNDGATILSLLDVQHPAGKILVELAQQQDREIGDGTTSVV
IIASELLKRANELVKNKIHPTTIITGFRVALREAIRFINEVLSTSETLIN
IAKTSMSSKIIGADSDFFSNMVVDALLAVKTQNSKGEIKYPVKAVNVLKA
HGKSATESLLVPGYALNCTVASQAMPKRIAGGNVKIACLDLNLQKARMAM
GVQINIDDPEQLEQIRKREAGIVLERVKKIIDAGAQVVLTTKGIDDLCLK
EFVEAKIMGVRRCKKEDLRRIARATGATLVSSMSNLEGEETFESSYLGLC
DEVVQAKFSDDECILIKGTSKHSSSSIILRGANDYSLDEMERSLHDSLSV
VKRTLESGNVVPGGGCVEAALNIYLDNFATTVGSREQLAIAEFAAALLII
PKTLAVNAAKDSSELVAKLRSYHAASQMAKPEDRSYRNYGLDLIRGKIVD
EIHAGVLEPTISKVKSLKSALEACVAILRIDTMITVDPE

3D structure

• PDB: 4v94 The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
• Chain: I
• Resolution: 3.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D65 T98 T99 D404
• Catalytic site (residue number reindexed from 1): D63 T96 T97 D396

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	MG	I	D96 K167	D94 K159
BS02	ADP	I	P46 D96 G97 T99 S100 S166 G421 G422	P44 D94 G95 T97 S98 S158 G413 G414
BS03	BEF	I	D96 T98 T99 K167 D404	D94 T96 T97 K159 D396

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:4v94, PDBe:4v94, PDBj:4v94
• PDBsum: 4v94
• PubMed: 22503819
• UniProt: P12612|TCPA_YEAST T-complex protein 1 subunit alpha (Gene Name=TCP1)