› 3lt5

X-ray diffraction
2.3Å resolution

X-ray Crystallographic structure of a Pseudomonas Aeruginosa Azoreductase in complex with balsalazide

Released:
DOI: 10.2210/pdb3lt5/pdb
PDB entry 3lt5 coloured by chain, front view.
PDB entry 3lt5 coloured by chain, side view.
PDB entry 3lt5 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
A novel mechanism for azoreduction.
Ryan A, Laurieri N, Westwood I, Wang CJ, Lowe E, Sim E
J Mol Biol 400 24-37 (2010)
PMID: 20417637

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FMN-dependent NAD(P)H:quinone oxidoreductase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 212 amino acids
Theoretical weight: 23.08 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9I5F3 (Residues: 1-212; Coverage: 100%)
Gene names: PA0785, azoR1
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
Ligand FMN 2 x FMN
Ligand GOL 3 x GOL
Ligand BLQ 2 x BLQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P3121
Unit cell:
a: 83.097Å b: 83.097Å c: 109.05Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.157 0.154 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Arylamine N-acetyltransferases: from drug metabolism and pharmacogenetics to drug discovery.
Sim et al. (2014)
2 more

5 mentions without citation

Azoreductases in drug metabolism.
Ryan A. (2017)
4 more