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Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution

X-ray diffraction
2Å resolution
PDB entry 1kp8 coloured by chain, front view.
PDB entry 1kp8 coloured by chain, side view.
PDB entry 1kp8 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: 292648.29 Å2
Buried surface area: 68961.23 Å2
Dissociation area: 2,243.81 Å2
Dissociation energy (ΔGdiss): 17.36 kcal/mol
Dissociation entropy (TΔSdiss): 18.56 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: 547 amino acids
Theoretical weight: 57.13 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
Gene names: JW4103, b4143, groEL, groL, mopA
Chaperonin GroEL in PDB entry 1kp8, assembly 1, front view.
Chaperonin GroEL in PDB entry 1kp8, assembly 1, side view.
Chaperonin GroEL in PDB entry 1kp8, assembly 1, top view.
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