› 2cwu

X-ray diffraction
1.85Å resolution

Substrate schiff-base intermediate of copper amine oxidase from arthrobacter globiformis

Released:
DOI: 10.2210/pdb2cwu/pdb
PDB entry 2cwu coloured by chain, front view.
PDB entry 2cwu coloured by chain, side view.
PDB entry 2cwu coloured by chain, top view.
Source organism: Arthrobacter globiformis
Primary publication:
Kinetic and structural studies on the catalytic role of the aspartic acid residue conserved in copper amine oxidase.
Chiu YC, Okajima T, Murakawa T, Uchida M, Taki M, Hirota S, Kim M, Yamaguchi H, Kawano Y, Kamiya N, Kuroda S, Hayashi H, Yamamoto Y, Tanizawa K
Biochemistry 45 4105-20 (2006)
PMID: 16566584

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:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155528 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylethylamine oxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 638 amino acids
Theoretical weight: 70.81 KDa
Source organism: Arthrobacter globiformis
Expression system: Escherichia coli
UniProt:
  • Canonical: P46881 (Residues: 1-638; Coverage: 100%)
Sequence domains: Copper amine oxidase, enzyme domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CU 2 x CU
1 modified residue:
Ligand 1TY 2 x 1TY

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Unit cell:
a: 157.84Å b: 62.73Å c: 183.89Å
α: 90° β: 112.31° γ: 90°
R-values:
R R work R free
0.178 0.176 0.204
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Human copper-dependent amine oxidases.
Finney et al. (2014)
1 more

1 mention without citation

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