› 2z9c

X-ray diffraction
2.3Å resolution

The crystal structure of AzoR (azoreductase) from Escherichia coli: AzoR in complex with dicoumarol

Released:
DOI: 10.2210/pdb2z9c/pdb
PDB entry 2z9c coloured by chain, front view.
PDB entry 2z9c coloured by chain, side view.
PDB entry 2z9c 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

3 bound ligands:
Ligand FMN 1 x FMN
Ligand DTC 1 x DTC
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P4212
Unit cell:
a: 95.5Å b: 95.5Å c: 54.497Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 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

A novel cytosolic NADH:quinone oxidoreductase from Methanothermobacter marburgensis.
Ullmann et al. (2014)
1 more