Structure of PDB 4v8r Chain Ag

Receptor sequence
>4v8rAg (length=509) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
ERTTGRQAQISNITAAKAVADVIRTCLGPKAMLKMLLDPMGGLVLTNDGH
AILREIDVAHPAAKSMLELSRTQDEEVGDGTTTVIILAGEILAQCAPYLI
EKNIHPVIIIQALKKALTDALEVIKQVSKPVDVENDAAMKKLIQASIGTK
YVIHWSEKMCELALDAVKTVRKDLGQNFEIDIKRYVRVEKIPGGDVLDSR
VLKGVLLNKDVVHPKMSRHIENPRVVLLDCPLEYKKGESQTNIEIEKEED
WNRILQIEEEQVQLMCEQILAVRPTLVITEKGVSDLAQHYLLKGGCSVLR
RVKKSDNNRIARVTGATIVNRVEDLKESDVGTNCGLFKVEMIGDEYFSFL
DNCKACTIMLRGGSKDILNEIDRNLQDAMAVARNVMLSPSLSPGGGATEM
AVSVKLAEKAKQLEGIQQWPYQAVADAMECIPRTLIQNAGGDPIRLLSQL
RAKHAQGNFTTGIDGDKGKIVDMVSYGIWEPEVIKQQSVKTAIESACLLL
RVDDIVSGV
3D structure
PDB4v8r The Crystal Structures of the Eukaryotic Chaperonin Cct Reveal its Functional Partitioning
ChainAg
Resolution3.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D1398
Catalytic site (residue number reindexed from 1) D377
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 Ag L1039 G1092 T1093 T1094 T1095 T1161 G1415 G1416 G1486 E1501 L27 G80 T81 T82 T83 T149 G394 G395 G465 E480
BS02 BEF Ag D1060 D1091 T1093 K1162 D1398 D48 D79 T81 K150 D377
Gene Ontology
Molecular Function
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4v8r, PDBe:4v8r, PDBj:4v8r
PDBsum4v8r
PubMed23478063
UniProtP39077|TCPG_YEAST T-complex protein 1 subunit gamma (Gene Name=CCT3)

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