X-ray diffraction
1.95Å resolution

Structure of oxidized SidA ornithine hydroxylase with the FAD "in" and complexed with NADP


Function and Biology Details

Reaction catalysed:
L-ornithine + NAD(P)H + O(2) = N(5)-hydroxy-L-ornithine + NAD(P)(+) + H(2)O
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
L-ornithine N(5)-monooxygenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 501 amino acids
Theoretical weight: 56.96 KDa
Source organism: Aspergillus fumigatus Af293
Expression system: Escherichia coli
  • Canonical: E9QYP0 (Residues: 1-501; Coverage: 100%)
Gene names: Afu2g07680, sidA
Sequence domains: L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase

Ligands and Environments

Cofactor: Ligand FAD 4 x FAD

Cofactor: Ligand NAP 4 x NAP
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 80.507Å b: 154.868Å c: 90.483Å
α: 90° β: 109.25° γ: 90°
R R work R free
0.17 0.168 0.211
Expression system: Escherichia coli