› 1dk7

X-ray diffraction
2.02Å resolution

CRYSTAL STRUCTURE OF AN ISOLATED APICAL DOMAIN OF GROEL

Released:
DOI: 10.2210/pdb1dk7/pdb
PDB entry 1dk7 coloured by chain, front view.
PDB entry 1dk7 coloured by chain, side view.
PDB entry 1dk7 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity.
Chen L, Sigler PB
Cell 99 757-68 (1999)
PMID: 10619429

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 146 amino acids
Theoretical weight: 15.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 191-336; Coverage: 27%)
Gene names: JW4103, b4143, groEL, groL, mopA
Structure domains: GroEL

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P3221
Unit cell:
a: 84.859Å b: 84.859Å c: 77.068Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.225 0.225 0.241
Expression system: Escherichia coli

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Citations

30 review citations

Folding of newly translated proteins in vivo: the role of molecular chaperones.
Frydman J. (2001)
29 more