X-ray diffraction
2.04Å resolution

The active site base controls cofactor reactivity in Escherichia coli amine oxidase: X-ray crystallographic studies with mutational variants.


Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Primary amine oxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 727 amino acids
Theoretical weight: 81.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P46883 (Residues: 31-757; Coverage: 100%)
Gene names: JW1381, b1386, maoA, tynA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID2
Spacegroup: P212121
Unit cell:
a: 135.05Å b: 167.17Å c: 79.92Å
α: 90° β: 90° γ: 90°
R R work R free
0.185 0.185 0.237
Expression system: Escherichia coli