› 1qvr

X-ray diffraction
3Å resolution

Crystal Structure Analysis of ClpB

Released:
DOI: 10.2210/pdb1qvr/pdb
PDB entry 1qvr coloured by chain, front view.
PDB entry 1qvr coloured by chain, side view.
PDB entry 1qvr coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state.
Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT
Cell 115 229-40 (2003)
PMID: 14567920

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193126 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein ClpB Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 854 amino acids
Theoretical weight: 96.39 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RA63 (Residues: 1-854; Coverage: 100%)
Gene names: TTHA1487, clpB
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PT 23 x PT
Ligand ANP 6 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID, NSLS BEAMLINE X25, CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 107.747Å b: 138.482Å c: 212.215Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.265 0.263 0.307
Expression system: Escherichia coli

Quick links

Citations

66 review citations

AAA+ proteins: have engine, will work.
Hanson et al. (2005)
65 more

56 mentions without citation

Classification of intrinsically disordered regions and proteins.
van der Lee et al. (2014)
55 more