X-ray diffraction
1.8Å resolution

Crystal Structure of the First Nucelotide Binding Domain of ClpB


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Chaperone protein ClpB Chain: A
Molecule details ›
Chain: A
Length: 195 amino acids
Theoretical weight: 21.53 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P63284 (Residues: 159-351; Coverage: 23%)
Gene names: JW2573, b2592, clpB, htpM
Sequence domains: ATPase family associated with various cellular activities (AAA)
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 38.488Å b: 65.686Å c: 79.087Å
α: 90° β: 90° γ: 90°
R R work R free
0.225 0.222 0.247
Expression system: Escherichia coli BL21(DE3)