Structure of PDB 4v8r Chain AA

Receptor sequence
>4v8rAA (length=537) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
FNNSRSDTLFLGGEKISGDDIRNQNVLATMAVANVVKSSLGPVGLDKMLV
DDIGDFTVTNDGATILSLLDVQHPAGKILVELAQQQDREIGDGTTSVVII
ASELLKRANELVKNKIHPTTIITGFRVALREAIRFINEVLSTSVETLINI
AKTSMSSKIIGADSDFFSNMVVDALLAVKTQNSKGEIKYPVKAVNVLKAH
GKSATESLLVPGYALNCTVASQAMPKRIAGGNVKIACLDLNLQKARMAMG
VQINIDDPEQLEQIRKREAGIVLERVKKIIDAGAQVVLTTKGIDDLCLKE
FVEAKIMGVRRCKKEDLRRIARATGATLVSSMSNLEGEETFESSYLGLCD
EVVQAKFSDDECILIKGTSKHSSSSIILRGANDYSLDEMERSLHDSLSVV
KRTLESGNVVPGGGCVEAALNIYLDNFATTVGSREQLAIAEFAAALLIIP
KTLAVNAAKDSSELVAKLRSYHAASQMAKKRRSYRNYGLDLIRGKIVDEI
HAGVLEPTISKVKSLKSALEACVAILRIDTMITVDPE
3D structure
PDB4v8r The Crystal Structures of the Eukaryotic Chaperonin Cct Reveal its Functional Partitioning
ChainAA
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 AA L44 P46 D96 G97 T99 S100 T162 S165 S166 G421 G422 L462 V517 E519 L40 P42 D92 G93 T95 S96 T153 S156 S157 G412 G413 L453 V504 E506
BS02 BEF AA N64 D96 T98 T99 K167 D404 N60 D92 T94 T95 K158 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:4v8r, PDBe:4v8r, PDBj:4v8r
PDBsum4v8r
PubMed23478063
UniProtP12612|TCPA_YEAST T-complex protein 1 subunit alpha (Gene Name=TCP1)

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