› 1la1

X-ray diffraction
2.06Å 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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141313 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin GroEL Chain: A
Molecule details ›
Chain: A
Length: 192 amino acids
Theoretical weight: 20.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 188-379; Coverage: 35%)
Gene names: JW4103, b4143, groEL, groL, mopA
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains: GroEL

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 48.62Å b: 61.95Å c: 75.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.257
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Investigation of intact protein complexes by mass spectrometry.
Heck et al. (2004)
6 more