› 1jon

X-ray diffraction
2.5Å resolution

GROEL (HSP60 CLASS) FRAGMENT COMPRISING RESIDUES 191-345

Released:
DOI: 10.2210/pdb1jon/pdb
PDB entry 1jon coloured by chain, front view.
PDB entry 1jon coloured by chain, side view.
PDB entry 1jon coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.
Zahn R, Buckle AM, Perrett S, Johnson CM, Corrales FJ, Golbik R, Fersht AR
Proc Natl Acad Sci U S A 93 15024-9 (1996)
PMID: 8986757

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: 155 amino acids
Theoretical weight: 16.64 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 191-345; Coverage: 28%)
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: P3121
Unit cell:
a: 91.67Å b: 91.67Å c: 38.33Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.216 0.287
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones.
Ben-Zvi et al. (2001)
11 more

1 mention without citation

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.
Zahn et al. (1996)