4v43

X-ray diffraction
3.52Å resolution

Structural and mechanistic basis for allostery in the bacterial chaperonin GroEL

Released:
Source organism: Escherichia coli
Entry author: Wang J

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetradecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141315 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin GroEL Chains: 1, 2, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z
Molecule details ›
Chains: 1, 2, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z
Length: 547 amino acids
Theoretical weight: 57.16 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 2-548; Coverage: 100%)
Gene names: JW4103, b4143, groEL, groL, mopA
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 137.666Å b: 264.235Å c: 294.799Å
α: 90° β: 92.39° γ: 90°
R-values:
R R work R free
0.291 0.291 0.298
Expression system: Escherichia coli