› 2y73

X-ray diffraction
2.6Å resolution

THE NATIVE STRUCTURES OF SOLUBLE HUMAN PRIMARY AMINE OXIDASE AOC3

Released:
DOI: 10.2210/pdb2y73/pdb
PDB entry 2y73 coloured by chain, front view.
PDB entry 2y73 coloured by chain, side view.
PDB entry 2y73 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Identification of two imidazole binding sites and key residues for substrate specificity in human primary amine oxidase AOC3.
Elovaara H, Kidron H, Parkash V, Nymalm Y, Bligt E, Ollikka P, Smith DJ, Pihlavisto M, Salmi M, Jalkanen S, Salminen TA
Biochemistry 50 5507-20 (2011)
PMID: 21585208

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Amine oxidase [copper-containing] 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 763 amino acids
Theoretical weight: 84.73 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q16853 (Residues: 1-763; Coverage: 100%)
Gene names: AOC3, VAP1
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
5 bound ligands:
Ligand CU 2 x CU
Ligand CA 4 x CA
Ligand IMD 8 x IMD
Ligand NAG 4 x NAG
Ligand FMT 2 x FMT
1 modified residue:
Ligand TPQ 2 x TPQ

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P6522
Unit cell:
a: 225.755Å b: 225.755Å c: 216.985Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.175 0.213

Quick links

Citations

3 review citations

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

6 mentions without citation

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