› 3sx1

X-ray diffraction
1.73Å resolution

Hansenula polymorpha copper amine oxidase-1 in its apo form

Released:
DOI: 10.2210/pdb3sx1/pdb
PDB entry 3sx1 coloured by chain, front view.
PDB entry 3sx1 coloured by chain, side view.
PDB entry 3sx1 coloured by chain, top view.
Source organism: Ogataea angusta
Primary publication:
The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with CuI and CoII.
Klema VJ, Johnson BJ, Klinman JP, Wilmot CM
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 501-10 (2012)
PMID: 22691777

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

Assemblies composition:
homo dimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-146319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisomal primary amine oxidase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 692 amino acids
Theoretical weight: 77.63 KDa
Source organism: Ogataea angusta
Expression system: Escherichia coli
UniProt:
  • Canonical: P12807 (Residues: 1-692; Coverage: 100%)
Gene name: AMO
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 14 x GOL
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 139.617Å b: 153.636Å c: 223.562Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.134 0.132 0.163
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Oxygen Activation Switch in the Copper Amine Oxidase of Escherichia coli.
Gaule et al. (2018)

3 mentions without citation

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