Structure of PDB 4v8r Chain BQ

Receptor sequence
>4v8rBQ (length=523) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
QNPNAGLFKQGYNSYSNADGQIIKSIAAIRELHQMCLTSMGPCGRNKIIV
NHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMIL
AGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEITDKNDK
NELLKMIKPVISSKKYGSEDILSELVSEAVSHVLPVAFNVDSIRVVKIMG
GSLSNSTVIKGMVFNREPEGHVKSLSEDKKHKVAVFTCPLDIANTETKGT
VLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLN
RYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEELGLVETVKTMEIG
GDRVTVFKQEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKP
SGGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLA
ETAGLDVNEVLPNLYAAHNDHLYKGVDIDDEGVKDIREENIYDMLATKKF
AINVATEAATTVLSIDQIIMAKK
3D structure
PDB4v8r The Crystal Structures of the Eukaryotic Chaperonin Cct Reveal its Functional Partitioning
ChainBQ
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 BQ M3046 G3047 D3098 G3099 T3100 N3101 L3102 P3165 S3169 G3422 A3423 I3501 D3519 M40 G41 D92 G93 T94 N95 L96 P159 S163 G408 A409 I478 D493
BS02 BEF BQ D3067 D3098 T3100 K3170 D3403 D61 D92 T94 K164 D389
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
GO:0051086 chaperone mediated protein folding independent of cofactor
Cellular Component
GO:0005737 cytoplasm
GO:0005832 chaperonin-containing T-complex

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Biological Process
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Cellular Component
External links
PDB RCSB:4v8r, PDBe:4v8r, PDBj:4v8r
PDBsum4v8r
PubMed23478063
UniProtP47079|TCPQ_YEAST T-complex protein 1 subunit theta (Gene Name=CCT8)

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