PDBe 1xck

X-ray diffraction
2.92Å resolution

Crystal structure of apo GroEL

Released:
Source organism: Escherichia coli
Primary publication:
Crystal structure of wild-type chaperonin GroEL.
J. Mol. Biol. 354 940-51 (2005)
PMID: 16288915

Function and Biology Details

Structure analysis Details

Assemblies composition:
homo heptamer (preferred)
homo 14-mer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
60 kDa chaperonin Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 547 amino acids
Theoretical weight: 57.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli str. K-12 substr. W3110
UniProt:
  • Canonical: P0A6F5 (Residues: 2-548; Coverage: 100%)
Gene names: JW4103, b4143, groEL, groL, mopA
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 262.8Å b: 283.6Å c: 135.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.235
Expression system: Escherichia coli str. K-12 substr. W3110