› 1sx3

X-ray diffraction
2Å 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

Assembly composition:
homo tetradecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141315 (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: 525 amino acids
Theoretical weight: 55.28 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 2-526; Coverage: 96%)
Gene names: JW4103, b4143, groEL, groL, mopA
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 14 x MG
Ligand K 16 x K
Ligand AGS 14 x AGS
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 135.571Å b: 260.112Å c: 150.2Å
α: 90° β: 101.14° γ: 90°
R-values:
R R work R free
0.246 0.246 0.265
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

9 mentions without citation

The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning.
Kalisman et al. (2013)
8 more