Structure of PDB 4v4o Chain a Binding Site BS01

Receptor Information
>4v4o Chain a (length=527) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKILVFDEAARRALERGVNAVANAVKVTLGPRGRNVVLEKKFGSPTITKD
GVTVAKEVELEDHLENIGAQLLKEVASKTNDVAGDGTTTATVLAQAIVRE
GLKNVAAGANPLALKRGIEKAVEAAVEKIKALAIPVEDRKAIEEVATISA
NDPEVGKLIADAMEKVGKEGIITVEESKSLETELKFVEGYQFDKGYISPY
FVTNPETMEAVLEDAFILIVEKKVSNVRELLPILEQVAQTGKPLLIIAED
VEGEALATLVVNKLRGTLSVAAVKAPGFGDRRKEMLKDIAAVTGGTVISE
ELGFKLENATLSMLGRAERVRITKDETTIVGGKGKKEDIEARINGIKKEL
ETTDSEYAREKLQERLAKLAGGVAVIRVGAATETELKEKKHRFEDALNAT
RAAVEEGIVPGGGVTLLRAISAVEELIKKLEGDEATGAKIVRRALEEPAR
QIAENAGYEGSVIVQQILAETKNPRYGFNAATGEFVDMVEAGIVDPAKVT
RSALQNAASIGALILTTEAVVAEKPEK
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain4v4o Chain a Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4v4o Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity
Resolution2.8 Å
Binding residue
(original residue number in PDB)		D87 S151
Binding residue
(residue number reindexed from 1)		D85 S149
Annotation score4
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.
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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