› 5lae

X-ray diffraction
1.85Å resolution

Crystal structure of murine N1-acetylpolyamine oxidase

Released:
DOI: 10.2210/pdb5lae/pdb
PDB 5lae coloured by chain and viewed from the front.
PDB 5lae coloured by chain and viewed from the side.
PDB 5lae coloured by chain and viewed from the top.
Source organism: Mus musculus
Primary publication:
The Structure of Murine N(1)-Acetylspermine Oxidase Reveals Molecular Details of Vertebrate Polyamine Catabolism.
Sjögren T, Wassvik CM, Snijder A, Aagaard A, Kumanomidou T, Barlind L, Kaminski TP, Kashima A, Yokota T, Fjellström O
Biochemistry (2017)
PMID: 28029774

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • 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:
Ligand GOL 2 x GOL
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-values:
R R work R free
0.181 0.179 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Polyamines in cancer: integrating organismal metabolism and antitumour immunity.
Holbert et al. (2022)
2 more

2 mentions without citation

Bioinformatic Analysis of the Flavin-Dependent Amine Oxidase Superfamily: Adaptations for Substrate Specificity and Catalytic Diversity.
Tararina et al. (2020)
1 more