› 3x0v

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
L-lysine + O(2) + H(2)O = 6-amino-2-oxohexanoate + NH(3) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102234 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amine oxidase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 541 amino acids
Theoretical weight: 60.97 KDa
Source organism: Trichoderma viride
UniProt:
  • Canonical: A0A0J9X1X3 (Residues: 1-541; Coverage: 100%)
Sequence domains: Flavin containing amine oxidoreductase

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
1 bound ligand:
Ligand EPE 4 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2
Unit cell:
a: 116.975Å b: 170.012Å c: 81.046Å
α: 90° β: 132.01° γ: 90°
R-values:
R R work R free
0.16 0.159 0.188

Quick links

Citations

3 review citations

Distribution in Different Organisms of Amino Acid Oxidases with FAD or a Quinone As Cofactor and Their Role as Antimicrobial Proteins in Marine Bacteria.
Campillo-Brocal et al. (2015)
2 more

3 mentions without citation

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