Structure of PDB 4v8r Chain BH

Receptor sequence
>4v8rBH (length=519) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
IVVLKEGTDASQGKGQIISNINACVAVQEALKPTLGPLGSDILIVTSNQK
TTISNDGATILKLLDVVHPAAKTLVDISRAQDAEVGDGTTSVTILAGELM
KEAKPFLEEGISSHLIMKGYRKAVSLAVEKINELAVDITSEKSSGRELLE
RCARTAMSSKLIHNNADFFVKMCVDAVLSLDRNDLDDKLIGIKKIPGGAM
EESLFINGVAFKKTFSYAGFEQQPKKFNNPKILSLNVELELKAEKDNAEV
RVEHVEDYQAIVDAEWQLIFEKLRQVEETGANIVLSKLPIGDLATQFFAD
RNIFCAGRVSADDMNRVIQAVGGSIQSTTSDIKPEHLGTCALFEEMQIGS
ERYNLFQGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLI
VAGGGATEMEVSKCLRDYSKTIAGKQQMIINAFAKALEVIPRQLCENAGF
DAIEILNKLRLAHSKGEKWYGVVFETENIGDNFAKFVWEPALVKINALNS
ATEATNLILSVDETITNKG
3D structure
PDB4v8r The Crystal Structures of the Eukaryotic Chaperonin Cct Reveal its Functional Partitioning
ChainBH
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 BH L3044 G3045 G3097 T3098 T3099 S3100 T3164 S3168 G3413 L3453 E3498 L35 G36 G88 T89 T90 S91 T155 S159 G404 L444 E489
BS02 BEF BH N3064 D3096 T3098 T3099 K3169 D3395 N55 D87 T89 T90 K160 D386
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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Cellular Component
External links
PDB RCSB:4v8r, PDBe:4v8r, PDBj:4v8r
PDBsum4v8r
PubMed23478063
UniProtP42943|TCPH_YEAST T-complex protein 1 subunit eta (Gene Name=CCT7)

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