Structure of PDB 4v81 Chain a

Receptor sequence
>4v81a (length=544) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SRSDTLFLGGEKISGDDIRNQNVLATMAVANVVKSSLGPVGLDKMLVDDI
GDFTVTNDGATILSLLDVQHPAGKILVELAQQQDREIGDGTTSVVIIASE
LLKRANELVKNKIHPTTIITGFRVALREAIRFINEVLSTSVDTKETLINI
AKTSMSSKIIGADSDFFSNMVVDALLAVKTQNSKGEIKYPVKAVNVLKAH
GKSATESLLVPGYALNCTVASQAMPKRIAGGNVKIACLDLNLQKARMAMG
VQINIDDPEQLEQIRKREAGIVLERVKKIIDAGAQVVLTTKGIDDLCLKE
FVEAKIMGVRRCKKEDLRRIARATGATLVSSMSNLEGEETFESSYLGLCD
EVVQAKFSDDECILIKGTSKHSSSSIILRGANDYSLDEMERSLHDSLSVV
KRTLESGNVVPGGGCVEAALNIYLDNFATTVGSREQLAIAEFAAALLIIP
KTLAVNAAKDSSELVAKLRSYHAASQMAKKRRSYRNYGLDLIRGKIVDEI
HAGVLEPTISKVKSLKSALEACVAILRIDTMITVDPEPPKEDPH
3D structure
PDB4v81 The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.
Chaina
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 a L1044 P1046 D1096 T1099 T1162 S1165 G1422 V1517 L37 P39 D89 T92 T153 S156 G413 V504
BS02 BEF a D1065 D1096 G1097 T1099 D1404 D58 D89 G90 T92 D395
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:4v81, PDBe:4v81, PDBj:4v81
PDBsum4v81
PubMed21701561
UniProtP12612|TCPA_YEAST T-complex protein 1 subunit alpha (Gene Name=TCP1)

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