X-ray diffraction
1.5Å resolution

Pseudomonas fluorescens kynurenine 3-monooxygenase (KMO) in complex with the enzyme substrate L-kynurenine


Function and Biology Details

Reaction catalysed:
L-kynurenine + NADPH + O(2) = 3-hydroxy-L-kynurenine + NADP(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Kynurenine 3-monooxygenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 461 amino acids
Theoretical weight: 50.74 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli
  • Canonical: Q84HF5 (Residues: 1-461; Coverage: 100%)
Gene names: kmo, qbsG
Sequence domains: FAD binding domain
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 69.93Å b: 52.62Å c: 137.99Å
α: 90° β: 104.07° γ: 90°
R R work R free
0.19 0.188 0.21
Expression system: Escherichia coli