› 1ivx

X-ray diffraction
2.2Å resolution

Crystal structure of copper amine oxidase from Arthrobacter globiformis: Holo form generated by biogenesis in crystal.

Released:
DOI: 10.2210/pdb1ivx/pdb
PDB entry 1ivx coloured by chain, front view.
PDB entry 1ivx coloured by chain, side view.
PDB entry 1ivx coloured by chain, top view.
Source organism: Arthrobacter globiformis
Primary publication:
X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase.
Kim M, Okajima T, Kishishita S, Yoshimura M, Kawamori A, Tanizawa K, Yamaguchi H
Nat Struct Biol 9 591-6 (2002)
PMID: 12134140

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 TPQ 2 x TPQ

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Unit cell:
a: 158.076Å b: 63.39Å c: 184.018Å
α: 90° β: 111.6° γ: 90°
R-values:
R R work R free
0.22 0.217 0.292
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

4 mentions without citation

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