› 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:
DOI: 10.2210/pdb1qaf/pdb
PDB entry 1qaf coloured by chain, front view.
PDB entry 1qaf coloured by chain, side view.
PDB entry 1qaf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants.
Murray JM, Saysell CG, Wilmot CM, Tambyrajah WS, Jaeger J, Knowles PF, Phillips SE, McPherson MJ
Biochemistry 38 8217-27 (1999)
PMID: 10387067

Function and Biology Details

Reaction catalysed: 
RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155532 (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:
Ligand CU 2 x CU
Ligand CA 4 x CA
Ligand GOL 1 x GOL
1 modified residue:
Ligand TPQ 2 x TPQ

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

Quick links

Citations

9 review citations

Biodegradation of aromatic compounds by Escherichia coli.
Díaz et al. (2001)
8 more

2 mentions without citation

Copper active sites in biology.
Solomon et al. (2014)
1 more