› › Structure analysis

ATP-triggered molecular mechanics of the chaperonin GroEL

Electron Microscopy
8.5Å resolution
PDB entry 4aau coloured by chain, front view.
PDB entry 4aau coloured by chain, side view.
PDB entry 4aau coloured by chain, top view.
Source organism: Escherichia coli
Assembly composition:
homo tetradecamer (preferred)
Entry contents: 1 distinct polypeptide molecule

Quick links

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Assembly Name: Chaperonin GroEL
hide full assembly name
Multimeric state: homo tetradecamer
Accessible surface area: 291923.12 Å2
Buried surface area: 39717.84 Å2
Dissociation area: 4,598.17 Å2
Dissociation energy (ΔGdiss): -43.81 kcal/mol
Dissociation entropy (TΔSdiss): 110.33 kcal/mol
Symmetry number: 7
PDBe Complex ID: PDB-CPX-141315

Macromolecules

Chaperonin GroEL
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 548 amino acids
Theoretical weight: 57.35 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 1-548; Coverage: 100%)
Gene names: JW4103, b4143, groEL, groL, mopA
Pfam: TCP-1/cpn60 chaperonin family
InterPro:
Chaperonin GroEL in PDB entry 4aau, assembly 1, front view.
Chaperonin GroEL in PDB entry 4aau, assembly 1, side view.
Chaperonin GroEL in PDB entry 4aau, assembly 1, top view.
Molecule details ›

Search similar proteins

Quick links