› 2yx9

X-ray diffraction
1.68Å resolution

Crystal structure of D298K copper amine oxidase from Arthrobacter globiformis

Released:
DOI: 10.2210/pdb2yx9/pdb
PDB entry 2yx9 coloured by chain, front view.
PDB entry 2yx9 coloured by chain, side view.
PDB entry 2yx9 coloured by chain, top view.
Source organism: Arthrobacter globiformis
Primary publication:
Trapping of a dopaquinone intermediate in the TPQ cofactor biogenesis in a copper-containing amine oxidase from Arthrobacter globiformis.
Moore RH, Spies MA, Culpepper MB, Murakawa T, Hirota S, Okajima T, Tanizawa K, Mure M
J Am Chem Soc 129 11524-34 (2007)
PMID: 17715921

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: 70.75 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 DPQ 2 x DPQ

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Unit cell:
a: 158.012Å b: 63.027Å c: 184.119Å
α: 90° β: 111.96° γ: 90°
R-values:
R R work R free
0.245 0.245 0.254
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.
Klinman et al. (2014)
5 more

5 mentions without citation

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