Structure of PDB 4v94 Chain i

Receptor sequence
>4v94i (length=539) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
QLFNNSRSDTLFLGGEKISGDDIRNQNVLATMAVANVVKSSLGPVGLDKM
LVDDIGDFTVTNDGATILSLLDVQHPAGKILVELAQQQDREIGDGTTSVV
IIASELLKRANELVKNKIHPTTIITGFRVALREAIRFINEVLSTSETLIN
IAKTSMSSKIIGADSDFFSNMVVDALLAVKTQNSKGEIKYPVKAVNVLKA
HGKSATESLLVPGYALNCTVASQAMPKRIAGGNVKIACLDLNLQKARMAM
GVQINIDDPEQLEQIRKREAGIVLERVKKIIDAGAQVVLTTKGIDDLCLK
EFVEAKIMGVRRCKKEDLRRIARATGATLVSSMSNLEGEETFESSYLGLC
DEVVQAKFSDDECILIKGTSKHSSSSIILRGANDYSLDEMERSLHDSLSV
VKRTLESGNVVPGGGCVEAALNIYLDNFATTVGSREQLAIAEFAAALLII
PKTLAVNAAKDSSELVAKLRSYHAASQMAKPEDRSYRNYGLDLIRGKIVD
EIHAGVLEPTISKVKSLKSALEACVAILRIDTMITVDPE
3D structure
PDB4v94 The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
Chaini
Resolution3.8 Å
3D
structure
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Enzymatic activity
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 i L44 P46 D96 G97 T99 S100 T162 S166 G422 V517 L42 P44 D94 G95 T97 S98 T154 S158 G414 V506
BS02 BEF i D96 G97 T98 T99 K167 D404 D94 G95 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4v94, PDBe:4v94, PDBj:4v94
PDBsum4v94
PubMed22503819
UniProtP12612|TCPA_YEAST T-complex protein 1 subunit alpha (Gene Name=TCP1)

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