1f1x

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE OF HOMOPROTOCATECHUATE 2,3-DIOXYGENASE FROM BREVIBACTERIUM FUSCUM

Released:

Function and Biology Details

Reaction catalysed:
3,4-dihydroxyphenylacetate + O(2) = 2-hydroxy-5-carboxymethylmuconate semialdehyde
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
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: 322 amino acids
Theoretical weight: 37.16 KDa
Source organism: Brevibacterium fuscum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q45135 (Residues: 1-322; Coverage: 88%)
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I41
Unit cell:
a: 157.1Å b: 157.1Å c: 121.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 0.195
Expression system: Escherichia coli