› 1d6u

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE

Released:
DOI: 10.2210/pdb1d6u/pdb
PDB entry 1d6u coloured by chain, front view.
PDB entry 1d6u coloured by chain, side view.
PDB entry 1d6u coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Visualization of dioxygen bound to copper during enzyme catalysis.
Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE
Science 286 1724-8 (1999)
PMID: 10576737

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 domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155532 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Primary amine oxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 727 amino acids
Theoretical weight: 81.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P46883 (Residues: 31-757; Coverage: 100%)
Gene names: JW1381, b1386, maoA, tynA
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand CU 2 x CU
Ligand CA 4 x CA
Ligand HY1 2 x HY1
Ligand PEA 1 x PEA
Ligand GOL 2 x GOL
1 modified residue:
Ligand TYQ 2 x TYQ

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P212121
Unit cell:
a: 135.236Å b: 166.482Å c: 79.628Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.239
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Biodegradation of aromatic compounds by Escherichia coli.
Díaz et al. (2001)
9 more

5 mentions without citation

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