X-ray diffraction
1.85Å resolution

Crystal structure of murine N1-acetylpolyamine oxidase


Function and Biology Details

Reaction catalysed:
N(1)-acetylspermidine + O(2) + H(2)O = putrescine + 3-acetamidopropanal + H(2)O(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Peroxisomal N(1)-acetyl-spermine/spermidine oxidase Chain: A
Molecule details ›
Chain: A
Length: 497 amino acids
Theoretical weight: 54.63 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q8C0L6 (Residues: 4-450, 458-504; Coverage: 98%)
Gene names: Pao, Paox
Sequence domains: Flavin containing amine oxidoreductase

Ligands and Environments

Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P61
Unit cell:
a: 121.975Å b: 121.975Å c: 55.093Å
α: 90° β: 90° γ: 120°
R R work R free
0.181 0.179 0.21
Expression system: Escherichia coli BL21(DE3)