› 1jbk

X-ray diffraction
1.8Å resolution

Crystal Structure of the First Nucelotide Binding Domain of ClpB

Released:
DOI: 10.2210/pdb1jbk/pdb
PDB entry 1jbk coloured by chain, front view.
PDB entry 1jbk coloured by chain, side view.
PDB entry 1jbk coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity.
Li J, Sha B
J Mol Biol 318 1127-37 (2002)
PMID: 12054807

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159078 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • 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:
Ligand MG 1 x MG
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-values:
R R work R free
0.225 0.222 0.247
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine.
Lee et al. (2004)
6 more

6 mentions without citation

A History of Molecular Chaperone Structures in the Protein Data Bank.
Bascos et al. (2019)
5 more