3sxx

X-ray diffraction
1.27Å resolution

Hansenula polymorpha copper amine oxidase-1 in complex with Co(II)

Released:
Source organism: Ogataea angusta
Primary publication:
The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with CuI and CoII.
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 501-10 (2012)
PMID: 22691777

Function and Biology Details

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
PDBe Complex ID:
PDB-CPX-146319 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisomal primary amine oxidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
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

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 103.887Å b: 223.364Å c: 103.969Å
α: 90° β: 95.61° γ: 90°
R-values:
R R work R free
0.109 0.108 0.138
Expression system: Escherichia coli