› 3ojk

X-ray diffraction
1.68Å resolution

Structure of Co-substituted Homoprotocatechuate 2,3-Dioxygenase in complex with 4-nitrocatechol at 1.68 Ang resolution

Released:
DOI: 10.2210/pdb3ojk/pdb
PDB entry 3ojk coloured by chain, front view.
PDB entry 3ojk coloured by chain, side view.
PDB entry 3ojk 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

6 bound ligands:
Ligand CO 4 x CO
Ligand 4NC 3 x 4NC
Ligand CL 4 x CL
Ligand P6G 5 x P6G
Ligand CA 1 x CA
Ligand PG4 3 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 110.102Å b: 150.395Å c: 95.941Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.153 0.182
Expression system: Escherichia coli

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Citations

8 review citations

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

1 mention without citation

A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase.
Fielding et al. (2011)