› 3bza

X-ray diffraction
1.7Å resolution

Structure of Mn-substituted Homoprotocatechuate 2,3-Dioxygenase from B.fuscum at 1.7 Ang resolution

Released:
DOI: 10.2210/pdb3bza/pdb
PDB entry 3bza coloured by chain, front view.
PDB entry 3bza coloured by chain, side view.
PDB entry 3bza coloured by chain, top view.
Source organism: Brevibacterium fuscum
Primary publication:
Swapping metals in Fe- and Mn-dependent dioxygenases: evidence for oxygen activation without a change in metal redox state.
Emerson JP, Kovaleva EG, Farquhar ER, Lipscomb JD, Que L
Proc Natl Acad Sci U S A 105 7347-52 (2008)
PMID: 18492808

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 domain:

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

4 bound ligands:
Ligand MN 4 x MN
Ligand CL 4 x CL
Ligand GOL 6 x GOL
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21212
Unit cell:
a: 110.502Å b: 152.191Å c: 96.278Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.197
Expression system: Escherichia coli

Quick links

Citations

12 review citations

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

2 mentions without citation

Swapping metals in Fe- and Mn-dependent dioxygenases: evidence for oxygen activation without a change in metal redox state.
Emerson et al. (2008)
1 more