› 3ojj

X-ray diffraction
1.72Å resolution

Structure of Co-substituted Homoprotocatechuate 2,3-Dioxygenase from B.fuscum at 1.72 Ang resolution

Released:
DOI: 10.2210/pdb3ojj/pdb
PDB entry 3ojj coloured by chain, front view.
PDB entry 3ojj coloured by chain, side view.
PDB entry 3ojj 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

Reaction catalysed: 
3,4-dihydroxyphenylacetate + O(2) = 2-hydroxy-5-carboxymethylmuconate semialdehyde
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 CO 4 x CO
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: DIAMOND BEAMLINE I03, SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 110.539Å b: 152.075Å c: 96.491Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.148 0.147 0.176
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

2 mentions without citation

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