› 2wo0

X-ray diffraction
2.6Å resolution

EDTA treated E. coli copper amine oxidase

Released:
DOI: 10.2210/pdb2wo0/pdb
PDB entry 2wo0 coloured by chain, front view.
PDB entry 2wo0 coloured by chain, side view.
PDB entry 2wo0 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Exploring the roles of the metal ions in Escherichia coli copper amine oxidase.
Smith MA, Pirrat P, Pearson AR, Kurtis CR, Trinh CH, Gaule TG, Knowles PF, Phillips SE, McPherson MJ
Biochemistry 49 1268-80 (2010)
PMID: 20052994

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: 81.37 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 CU 2 x CU
Ligand NA 4 x NA
1 modified residue:
Ligand TPQ 2 x TPQ

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 134.676Å b: 166.619Å c: 79.834Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.248
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.
Klinman et al. (2014)
1 more

3 mentions without citation

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