1qaf

X-ray diffraction
2.2Å resolution

THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Primary amine oxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 721 amino acids
Theoretical weight: 80.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P46883 (Residues: 36-756; Coverage: 99%)
Gene names: JW1381, b1386, maoA, tynA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P212121
Unit cell:
a: 135.2Å b: 167Å c: 79.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.176 0.244
Expression system: Escherichia coli