› 5zp0

X-ray diffraction
1.74Å resolution

Copper amine oxidase from Arthrobacter globiformis anaerobically reduced by ethylamine at pH 8 at 288 K (2)

Released:
DOI: 10.2210/pdb5zp0/pdb
PDB entry 5zp0 coloured by chain, front view.
PDB entry 5zp0 coloured by chain, side view.
PDB entry 5zp0 coloured by chain, top view.
Source organism: Arthrobacter globiformis
Primary publication:
In crystallo thermodynamic analysis of conformational change of the topaquinone cofactor in bacterial copper amine oxidase.
Murakawa T, Baba S, Kawano Y, Hayashi H, Yano T, Kumasaka T, Yamamoto M, Tanizawa K, Okajima T
Proc Natl Acad Sci U S A 116 135-140 (2019)
PMID: 30563857

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 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: 620 amino acids
Theoretical weight: 68.91 KDa
Source organism: Arthrobacter globiformis
Expression system: Escherichia coli
UniProt:
  • Canonical: P46881 (Residues: 9-628; Coverage: 97%)
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CU 2 x CU
Ligand NA 3 x NA
Ligand EDO 2 x EDO
1 modified residue:
Ligand TYQ 2 x TYQ

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: C2
Unit cell:
a: 193.986Å b: 65.077Å c: 158.957Å
α: 90° β: 117.18° γ: 90°
R-values:
R R work R free
0.151 0.15 0.177
Expression system: Escherichia coli

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Citations

4 citation in other articles

Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing.
Murakawa et al. (2020)
3 more

1 mention without citation

In crystallo thermodynamic analysis of conformational change of the topaquinone cofactor in bacterial copper amine oxidase.
Murakawa et al. (2019)