› 1yfx

X-ray diffraction
2Å resolution

Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from Ralstonia metallidurans complexed with 4-chloro-3-hydroxyanthranilic acid and NO

Released:
DOI: 10.2210/pdb1yfx/pdb
PDB entry 1yfx coloured by chain, front view.
PDB entry 1yfx coloured by chain, side view.
PDB entry 1yfx coloured by chain, top view.
Source organism: Cupriavidus metallidurans
Primary publication:
Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis.
Zhang Y, Colabroy KL, Begley TP, Ealick SE
Biochemistry 44 7632-43 (2005)
PMID: 15909978

Function and Biology Details

Reaction catalysed: 
3-hydroxyanthranilate + O(2) = 2-amino-3-carboxymuconate semialdehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172948 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-hydroxyanthranilate 3,4-dioxygenase Chain: A
Molecule details ›
Chain: A
Length: 174 amino acids
Theoretical weight: 20.06 KDa
Source organism: Cupriavidus metallidurans
Expression system: Escherichia coli
UniProt:
  • 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

4 bound ligands:
Ligand FE 2 x FE
Ligand NO 1 x NO
Ligand TRS 1 x TRS
Ligand 4AA 1 x 4AA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 8-BM
Spacegroup: P6522
Unit cell:
a: 57.9Å b: 57.9Å c: 230.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.244 0.291
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
Clifton et al. (2006)
17 more

2 mentions without citation

Crystal structures of YkuI and its complex with second messenger cyclic Di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains.
Minasov et al. (2009)
1 more