Structure of PDB 4v4o Chain e

Receptor sequence
>4v4oe (length=526) Species: 274 (Thermus thermophilus) [Search protein sequence]
AKILVFDEAARRALERGVNAVANAVKVTLGPRGRNVVLEKKFGSPTITKD
GVTVAKEVELEDHLENIGAQLLKEVASKTNDVAGDGTTTATVLAQAIVRE
GLKNVAAGANPLALKRGIEKAVEAAVEKIKALAIPVEDRKAIEEVATISA
NDPEVGKLIADAMEKVGKEGIITVEESKSLETELKFVEGYQFDKGYISPY
FVTNPETMEAVLEDAFILIVEKKVSNVRELLPILEQVAQTGKPLLIIAED
VEGEALATLVVNKLRGTLSVAAVKAPGFGDRRKEMLKDIAAVTGGTVISE
ELGFKLENATLSMLGRAERVRITKDETTIVGGKGKKEDIEARINGIKKEL
ETTDSEYAREKLQERLAKLAGGVAVIRVGAATETELKEKKHRFEDALNAT
RAAVEEGIVPGGGVTLLRAISAVEELIKKLEGDEATGAKIVRRALEEPAR
QIAENAGYEGSVIVQQILAETKNPRYGFNAATGEFVDMVEAGIVDPAKVT
RSALQNAASIGALILTTEAVVAEKPE
3D structure
PDB4v4o Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity
Chaine
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D397
Catalytic site (residue number reindexed from 1) D395
Enzyme Commision number 5.6.1.7: chaperonin ATPase.
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 MG e D87 S151 D85 S149
BS02 ADP e P33 K51 D87 G88 T89 T90 T91 G414 D497 P31 K49 D85 G86 T87 T88 T89 G412 D495
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016853 isomerase activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0009408 response to heat
GO:0042026 protein refolding
GO:0051085 chaperone cofactor-dependent protein refolding
Cellular Component
GO:0005737 cytoplasm
GO:1990220 GroEL-GroES complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4v4o, PDBe:4v4o, PDBj:4v4o
PDBsum4v4o
PubMed15296740
UniProtP61490|CH60_THET2 Chaperonin GroEL (Gene Name=groEL)

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