› 4usr

X-ray diffraction
1.83Å resolution

Function and Biology Details

Reaction catalysed: 
N,N-dimethylaniline + NADPH + O(2) = N,N-dimethylaniline N-oxide + NADP(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125976 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Monooxygenase Chain: A
Molecule details ›
Chain: A
Length: 361 amino acids
Theoretical weight: 39.88 KDa
Source organism: Pseudomonas stutzeri NF13
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: M2V3J0 (Residues: 1-358; Coverage: 100%)
Gene name: B381_09411
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P3221
Unit cell:
a: 63.56Å b: 63.56Å c: 189.82Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.162 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Protein Engineering for Nicotinamide Coenzyme Specificity in Oxidoreductases: Attempts and Challenges.
Chánique et al. (2018)
1 more

1 mention without citation

Exploring nicotinamide cofactor promiscuity in NAD(P)H-dependent flavin containing monooxygenases (FMOs) using natural variation within the phosphate binding loop. Structure and activity of FMOs from Cellvibrio sp. BR and Pseudomonas stutzeri NF13.
Jensen et al. (2014)