› 2xve

X-ray diffraction
1.99Å resolution

Crystal structure of bacterial flavin-containing monooxygenase

Released:
DOI: 10.2210/pdb2xve/pdb
Model geometry
Fit model/data
PDB entry 2xve coloured by chain, front view.
PDB entry 2xve coloured by chain, side view.
PDB entry 2xve coloured by chain, top view.
Source organism: Methylophaga aminisulfidivorans
Primary publication:
Structural and functional analysis of bacterial flavin-containing monooxygenase reveals its ping-pong-type reaction mechanism.
Cho HJ, Cho HY, Kim KJ, Kim MH, Kim SW, Kang BS
J Struct Biol 175 39-48 (2011)
PMID: 21527346

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182978 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trimethylamine monooxygenase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 464 amino acids
Theoretical weight: 54.12 KDa
Source organism: Methylophaga aminisulfidivorans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83XK4 (Residues: 1-456; Coverage: 100%)
Sequence domains: Flavin-binding monooxygenase-like
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand NO3 4 x NO3
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: C2
Unit cell:
a: 159.225Å b: 68.991Å c: 140.529Å
α: 90° β: 90.18° γ: 90°
R-values:
R R work R free
0.172 0.17 0.197
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases.
Olucha et al. (2011)
1 more

2 mentions without citation

Increased Thermostability of an Engineered Flavin-Containing Monooxygenase to Remediate Trimethylamine in Fish Protein Hydrolysates.
Goris et al. (2023)
1 more