› 1xck

X-ray diffraction
2.92Å resolution

Crystal structure of apo GroEL

Released:
DOI: 10.2210/pdb1xck/pdb
PDB entry 1xck coloured by chain, front view.
PDB entry 1xck coloured by chain, side view.
PDB entry 1xck coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of wild-type chaperonin GroEL.
Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H
J Mol Biol 354 940-51 (2005)
PMID: 16288915

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo heptamer (preferred)
homo tetradecamer
Assembly name:
PDBe Complex ID:
PDB-CPX-141322 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin GroEL 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

4 bound ligands:
Ligand SO4 43 x SO4
Ligand K 14 x K
Ligand MPD 31 x MPD
Ligand PEG 1 x PEG
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

Quick links

Citations

7 review citations

Phospholipase D: enzymology, functionality, and chemical modulation.
Selvy et al. (2011)
6 more

35 mentions without citation

Selective targeting of the stress chaperome as a therapeutic strategy.
Taldone et al. (2014)
34 more