› 3mph

X-ray diffraction
2.05Å resolution

The structure of human diamine oxidase complexed with an inhibitor aminoguanidine

Released:
DOI: 10.2210/pdb3mph/pdb
PDB entry 3mph coloured by chain, front view.
PDB entry 3mph coloured by chain, side view.
PDB entry 3mph coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Correlation of active site metal content in human diamine oxidase with trihydroxyphenylalanine quinone cofactor biogenesis .
McGrath AP, Caradoc-Davies T, Collyer CA, Guss JM
Biochemistry 49 8316-24 (2010)
PMID: 20722416

Function and Biology Details

Reaction catalysed: 
Histamine + H(2)O + O(2) = (imidazol-4-yl)acetaldehyde + 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-148733 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Diamine oxidase [copper-containing] Chains: A, B
Molecule details ›
Chains: A, B
Length: 731 amino acids
Theoretical weight: 83.52 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: P19801 (Residues: 21-751; Coverage: 100%)
Gene names: ABP, ABP1, AOC1, DAO
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand CU 2 x CU
Ligand CA 4 x CA
1 modified residue:
Ligand AGQ 2 x AGQ

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 92.685Å b: 94.604Å c: 196.051Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.215
Expression system: Drosophila melanogaster

Quick links

Citations

1 review citation

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

3 mentions without citation

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