Structure of PDB 4v81 Chain k

Receptor sequence
>4v81k (length=514) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
VFMNASQERTTGRQAQISNITAAKAVADVIRTCLGPKAMLKMLLDPMGGL
VLTNDGHAILREIDVAHPAAKSMLELSRTQDEEVGDGTTTVIILAGEILA
QCAPYLIEKNIHPVIIIQALKKALTDALEVIKQVSKPVDVENDAAMKKLI
QASIGTKYVIHWSEKMCELALDAVKTVRKDLIDIKRYVRVEKIPGGDVLD
SRVLKGVLLNKDVVHPKMSRHIENPRVVLLDCPLEYKKGESQTNIEIEKE
EDWNRILQIEEEQVQLMCEQILAVRPTLVITEKGVSDLAQHYLLKGGCSV
LRRVKKSDNNRIARVTGATIVNRVEDLKESDVGTNCGLFKVEMIGDEYFS
FLDNGSGKACTIMLRGGSKDILNEIDRNLQDAMAVARNVMLSPSLSPGGG
ATEMAVSVKLAEKAKQLEGIQQWPYQAVADAMECIPRTLIQNAGGDPIRL
LSQLRAKHAQGNFTTGIDGDKGKIVDMVSYGIWEPEVIKQQSVKTAIESA
CLLLRVDDIVSGVR
3D structure
PDB4v81 The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.
Chaink
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) D381
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 k L1039 G1040 N1059 D1091 T1094 T1095 A1157 G1416 G1417 L1456 E1501 L34 G35 N54 D86 T89 T90 A152 G399 G400 L439 E484
BS02 BEF k D1091 G1092 T1093 T1094 D86 G87 T88 T89
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:4v81, PDBe:4v81, PDBj:4v81
PDBsum4v81
PubMed21701561
UniProtP39077|TCPG_YEAST T-complex protein 1 subunit gamma (Gene Name=CCT3)

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