› 2xsr

X-ray diffraction
1.8Å resolution

Crystal structure of wild type Acinetobacter radioresistens catechol 1,2 dioxygenase

Released:
DOI: 10.2210/pdb2xsr/pdb
PDB entry 2xsr coloured by chain, front view.
PDB entry 2xsr coloured by chain, side view.
PDB entry 2xsr coloured by chain, top view.
Source organism: Acinetobacter radioresistens
Primary publication:
X-ray crystallography, mass spectrometry and single crystal microspectrophotometry: a multidisciplinary characterization of catechol 1,2 dioxygenase.
Micalella C, Martignon S, Bruno S, Pioselli B, Caglio R, Valetti F, Pessione E, Giunta C, Rizzi M
Biochim Biophys Acta 1814 817-23 (2011)
PMID: 20869471

Function and Biology Details

Reaction catalysed: 
Catechol + O(2) = cis,cis-muconate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190233 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
catechol 1,2-dioxygenase Chain: A
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 34.41 KDa
Source organism: Acinetobacter radioresistens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9F103 (Residues: 2-306; Coverage: 100%)
Gene names: FHY67_06370, catA
Sequence domains:
Structure domains: Aromatic compound dioxygenase

Ligands and Environments

2 bound ligands:
Ligand FE 1 x FE
Ligand PIE 1 x PIE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 101.645Å b: 79.447Å c: 83.53Å
α: 90° β: 132.5° γ: 90°
R-values:
R R work R free
0.174 0.173 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

From protein structure to function via single crystal optical spectroscopy.
Ronda et al. (2015)
12 other articles

3 mentions without citation

Biological Inspirations: Iron Complexes Mimicking the Catechol Dioxygenases.
Kałduńska et al. (2021)
2 more