Structure of PDB 4v4o Chain G

Receptor sequence
>4v4oG (length=525) Species: 274 (Thermus thermophilus) [Search protein sequence]
AKILVFDEAARRALERGVNAVANAVKVTLGPRGRNVVLEKKFGSPTITKD
GVTVAKEVELEDHLENIGAQLLKEVASKTNDVAGDGTTTATVLAQAIVRE
GLKNVAAGANPLALKRGIEKAVEAAVEKIKALAIPVEDRKAIEEVATISA
NDPEVGKLIADAMEKVGKEGIITVEESKSLETELKFVEGYQFDKGYISPY
FVTNPETMEAVLEDAFILIVEKKVSNVRELLPILEQVAQTGKPLLIIAED
VEGEALATLVVNKLRGTLSVAAVKAPGFGDRRKEMLKDIAAVTGGTVISE
ELGFKLENATLSMLGRAERVRITKDETTIVGGKGKKEDIEARINGIKKEL
ETTDSEYAREKLQERLAKLAGGVAVIRVGAATETELKEKKHRFEDALNAT
RAAVEEGIVPGGGVTLLRAISAVEELIKKLEGDEATGAKIVRRALEEPAR
QIAENAGYEGSVIVQQILAETKNPRYGFNAATGEFVDMVEAGIVDPAKVT
RSALQNAASIGALILTTEAVVAEKP
3D structure
PDB4v4o Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity
ChainG
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D52 T89 T90 D397
Catalytic site (residue number reindexed from 1) D50 T87 T88 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 G D87 S151 D85 S149
BS02 ADP G G32 P33 K51 D87 G88 T89 T90 T91 G414 I454 N481 A482 D497 G30 P31 K49 D85 G86 T87 T88 T89 G412 I452 N479 A480 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

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

[Back to BioLiP]