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Structure of GroEL-nucleotide complex in ADP-like conformation plunged 50 ms after mixing with ATP

Electron Microscopy
4Å resolution
PDB entry 8ble coloured by chain, front view.
PDB entry 8ble coloured by chain, side view.
PDB entry 8ble coloured by chain, top view.
Source organism: Escherichia coli
Assembly composition:
homo tetradecamer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Chaperonin GroEL
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Multimeric state: homo tetradecamer
Accessible surface area: 282039.8 Å2
Buried surface area: 60073.85 Å2
Dissociation area: 2,291.06 Å2
Dissociation energy (ΔGdiss): 15.99 kcal/mol
Dissociation entropy (TΔSdiss): 18.53 kcal/mol
Symmetry number: 14
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: 57.39 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
Chaperonin GroEL in PDB entry 8ble, assembly 1, front view.
Chaperonin GroEL in PDB entry 8ble, assembly 1, side view.
Chaperonin GroEL in PDB entry 8ble, assembly 1, top view.
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