› 3ojt

X-ray diffraction
1.7Å resolution

Structure of native Fe-containing Homoprotocatechuate 2,3-Dioxygenase at 1.70 Ang resolution

Released:
DOI: 10.2210/pdb3ojt/pdb
PDB entry 3ojt coloured by chain, front view.
PDB entry 3ojt coloured by chain, side view.
PDB entry 3ojt coloured by chain, top view.
Source organism: Brevibacterium fuscum
Primary publication:
A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase.
Fielding AJ, Kovaleva EG, Farquhar ER, Lipscomb JD, Que L
J Biol Inorg Chem 16 341-55 (2011)
PMID: 21153851

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175045 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
VOC domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 365 amino acids
Theoretical weight: 41.76 KDa
Source organism: Brevibacterium fuscum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45135 (Residues: 1-365; Coverage: 100%)
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand FE2 4 x FE2
Ligand P6G 5 x P6G
Ligand CL 4 x CL
Ligand CA 1 x CA
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA, SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 110.747Å b: 151.229Å c: 96.385Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.188
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Superoxide dismutases and superoxide reductases.
Sheng et al. (2014)
5 more

7 mentions without citation

A two-electron-shell game: intermediates of the extradiol-cleaving catechol dioxygenases.
Fielding et al. (2014)
6 more