› 2z98

X-ray diffraction
1.4Å resolution

The crystal structure of AzoR (azoreductase) from Escherichia coli: Oxidized AzoR in tetragonal crystals (The resolution has improved from 1.8 (1v4b) to 1.4 angstrom)

Released:
DOI: 10.2210/pdb2z98/pdb
PDB entry 2z98 coloured by chain, front view.
PDB entry 2z98 coloured by chain, side view.
PDB entry 2z98 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Expansion of substrate specificity and catalytic mechanism of azoreductase by X-ray crystallography and site-directed mutagenesis.
Ito K, Nakanishi M, Lee WC, Zhi Y, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M
J Biol Chem 283 13889-96 (2008)
PMID: 18337254

Function and Biology Details

Reaction catalysed: 
Anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH
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-154392 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FMN-dependent NADH:quinone oxidoreductase Chain: A
Molecule details ›
Chain: A
Length: 200 amino acids
Theoretical weight: 21.55 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P41407 (Residues: 2-201; Coverage: 100%)
Gene names: JW1409, acpD, azoR, b1412
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand FMN 1 x FMN
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P42212
Unit cell:
a: 92.204Å b: 92.204Å c: 51.741Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.22
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The influence of the gut microbiota on the bioavailability of oral drugs.
Zhang et al. (2021)
4 more

2 mentions without citation

Identification of NAD(P)H quinone oxidoreductase activity in azoreductases from P. aeruginosa: azoreductases and NAD(P)H quinone oxidoreductases belong to the same FMN-dependent superfamily of enzymes.
Ryan et al. (2014)
1 more