› 4z6u

X-ray diffraction
1.48Å resolution

Structure of H200E variant of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum in complex with 4-nitrocatechol at 1.48 Ang resolution

Released:
DOI: 10.2210/pdb4z6u/pdb
PDB entry 4z6u coloured by chain, front view.
PDB entry 4z6u coloured by chain, side view.
PDB entry 4z6u coloured by chain, top view.
Source organism: Brevibacterium fuscum
Primary publication:
Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200.
Kovaleva EG, Rogers MS, Lipscomb JD
Biochemistry 54 5329-39 (2015)
PMID: 26267790

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: 41.75 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 4NC 1 x 4NC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 110.268Å b: 150.875Å c: 95.919Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.12 0.117 0.162
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Rearrangements of organic peroxides and related processes.
Yaremenko et al. (2016)
1 more

1 mention without citation

Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200.
Kovaleva et al. (2015)