4b63

X-ray diffraction
1.9Å resolution

A. fumigatus ornithine hydroxylase (SidA) bound to NADP and ornithine

Released:

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)
PDBe Complex ID:
PDB-CPX-123229 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ornithine N(5)-monooxygenase Chain: A
Molecule details ›
Chain: A
Length: 501 amino acids
Theoretical weight: 56.96 KDa
Source organism: Aspergillus fumigatus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: E9QYP0 (Residues: 1-501; Coverage: 100%)
Gene names: Afu2g07680, sidA
Sequence domains: L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD

Cofactor: Ligand NAP 1 x NAP
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: I222
Unit cell:
a: 77.806Å b: 84.424Å c: 145.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.229
Expression system: Escherichia coli BL21