› 4usq

X-ray diffraction
2.39Å 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:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyridine nucleotide-disulfide oxidoreductase Chains: A, F
Molecule details ›
Chains: A, F
Length: 361 amino acids
Theoretical weight: 39.48 KDa
Source organism: Cellvibrio sp. BR
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: I3IEE4 (Residues: 1-361; Coverage: 100%)
Gene name: O59_000450
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: C2
Unit cell:
a: 115.41Å b: 95.09Å c: 92.37Å
α: 90° β: 126.26° γ: 90°
R-values:
R R work R free
0.248 0.246 0.287
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

2 mentions 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)
1 more