› 1vq0

X-ray diffraction
2.2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194782 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
33 kDa chaperonin Chains: A, B
Molecule details ›
Chains: A, B
Length: 302 amino acids
Theoretical weight: 34.04 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X1B4 (Residues: 1-290; Coverage: 100%)
Gene names: TM_1394, hslO
Sequence domains: Hsp33 protein
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ZN 2 x ZN
Ligand CL 2 x CL
Ligand UNL 2 x UNL
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 76.213Å b: 101.673Å c: 113.686Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.241
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Zinc center as redox switch--new function for an old motif.
Ilbert et al. (2006)
5 other articles

5 mentions without citation

Data processing and analysis with the autoPROC toolbox.
Vonrhein et al. (2011)
4 more