› 5lfo

X-ray diffraction
1.66Å resolution

Crystal structure of murine N1-acetylpolyamine oxidase in complex with N1-acetylspermine

Released:
DOI: 10.2210/pdb5lfo/pdb
PDB entry 5lfo coloured by chain, front view.
PDB entry 5lfo coloured by chain, side view.
PDB entry 5lfo coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The Structure of Murine N1-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 56 458-467 (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:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183929 (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
2 bound ligands:
Ligand SP5 1 x SP5
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P61
Unit cell:
a: 122.292Å b: 122.292Å c: 54.862Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.198 0.222
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

Exploring the activity of polyamine analogues on polyamine and spermine oxidase: methoctramine, a potent and selective inhibitor of polyamine oxidase.
Di Paolo et al. (2019)
1 more