X-ray diffraction
1.53Å resolution

1.5 angstrom crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from Cupriavidus metallidurans

Entry authors: Geng J, Gumpper RH, Huo L, Liu A

Function and Biology Details

Reaction catalysed:
3-hydroxyanthranilate + O(2) = 2-amino-3-carboxymuconate semialdehyde
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
3-hydroxyanthranilate 3,4-dioxygenase Chain: A
Molecule details ›
Chain: A
Length: 174 amino acids
Theoretical weight: 20.06 KDa
Source organism: Cupriavidus metallidurans CH34
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q1LCS4 (Residues: 1-174; Coverage: 100%)
Gene names: Rmet_5193, nbaC
Sequence domains: 3-hydroxyanthranilic acid dioxygenase
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P6522
Unit cell:
a: 58.32Å b: 58.32Å c: 231.849Å
α: 90° β: 90° γ: 120°
R R work R free
0.198 0.197 0.214
Expression system: Escherichia coli BL21(DE3)