› 5bwg

X-ray diffraction
1.75Å resolution

Structure of H200C variant of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum at 1.75 Ang resolution

Released:
DOI: 10.2210/pdb5bwg/pdb
PDB entry 5bwg coloured by chain, front view.
PDB entry 5bwg coloured by chain, side view.
PDB entry 5bwg coloured by chain, top view.
Source organism: Brevibacterium fuscum
Primary publication:
A Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization by Mössbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods.
Meier KK, Rogers MS, Kovaleva EG, Mbughuni MM, Bominaar EL, Lipscomb JD, Münck E
Inorg Chem 54 10269-80 (2015)
PMID: 26485328

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: 41.72 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 CL 4 x CL
Ligand P6G 5 x P6G
Ligand MPO 3 x MPO
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 110.748Å b: 150.627Å c: 96.269Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.146 0.145 0.179
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Mono- and binuclear non-heme iron chemistry from a theoretical perspective.
Rokob et al. (2016)
6 other articles

1 mention without citation

A Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization by Mössbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods.
Meier et al. (2015)