› 1ss8

X-ray diffraction
2.7Å resolution

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 tetradecamer
homo heptamer (preferred)
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
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 524 amino acids
Theoretical weight: 55.15 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 2-525; Coverage: 96%)
Gene names: JW4103, b4143, groEL, groL, mopA
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 178.38Å b: 204.98Å c: 280.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.215 0.249
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Advances in kinetic protein crystallography.
Bourgeois et al. (2005)
8 more

18 mentions without citation

Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery.
Wang et al. (2020)
17 more