› 2wgq

X-ray diffraction
2.5Å resolution

Zinc substituted E Coli Copper Amine Oxidase, a model for the precursor for 2,4,5-trihydroxyphenylalaninequinone formation

Released:
DOI: 10.2210/pdb2wgq/pdb
PDB entry 2wgq coloured by chain, front view.
PDB entry 2wgq coloured by chain, side view.
PDB entry 2wgq coloured by chain, top view.
Source organism: Escherichia coli
Entry authors: Moody PCE, Cooper RA

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 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: 727 amino acids
Theoretical weight: 81.34 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P46883 (Residues: 31-757; Coverage: 100%)
Gene names: JW1381, b1386, maoA, tynA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX7.2
Spacegroup: P212121
Unit cell:
a: 134.68Å b: 166.21Å c: 79.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.264
Expression system: Escherichia coli

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