› 1ekm

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1ekm/pdb
PDB entry 1ekm coloured by chain, front view.
PDB entry 1ekm coloured by chain, side view.
PDB entry 1ekm coloured by chain, top view.
Source organism: Ogataea angusta
Primary publication:
Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli.
Chen Z, Schwartz B, Williams NK, Li R, Klinman JP, Mathews FS
Biochemistry 39 9709-17 (2000)
PMID: 10933787

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

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: 656 amino acids
Theoretical weight: 73.73 KDa
Source organism: Ogataea angusta
Expression system: Escherichia coli
UniProt:
  • Canonical: P12807 (Residues: 17-672; Coverage: 95%)
Gene name: AMO
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 139.227Å b: 153.515Å c: 223.407Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.208
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

2 mentions without citation

The role of protein crystallography in defining the mechanisms of biogenesis and catalysis in copper amine oxidase.
Klema et al. (2012)
1 more