X-ray diffraction
1.8Å resolution

Crystal Structure of ClpA, an AAA+ Chaperone-like Regulator of ClpAP protease implication to the functional difference of two ATPase domains

Source organism: Escherichia coli
Primary publication:
Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease.
J. Biol. Chem. 277 46743-52 (2002)
PMID: 12205096

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
ATP-dependent Clp protease ATP-binding subunit ClpA Chain: A
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 16.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P0ABH9 (Residues: 1-143; Coverage: 19%)
Gene names: JW0866, b0882, clpA, lopD
Sequence domains: Clp amino terminal domain, pathogenicity island component
Structure domains: Clp, N-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P212121
Unit cell:
a: 36.021Å b: 51.965Å c: 65.1Å
α: 90° β: 90° γ: 90°
R R work R free
0.214 0.214 0.263
Expression system: Escherichia coli