› 1jrq

X-ray diffraction
2.15Å resolution

X-ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. coli Amine Oxidase

Released:
DOI: 10.2210/pdb1jrq/pdb
PDB entry 1jrq coloured by chain, front view.
PDB entry 1jrq coloured by chain, side view.
PDB entry 1jrq coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.
Murray JM, Kurtis CR, Tambyrajah W, Saysell CG, Wilmot CM, Parsons MR, Phillips SE, Knowles PF, McPherson MJ
Biochemistry 40 12808-18 (2001)
PMID: 11669617

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: 81.35 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

2 bound ligands:
Ligand CU 2 x CU
Ligand CA 4 x CA
1 modified residue:
Ligand TPQ 2 x TPQ

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P212121
Unit cell:
a: 134.54Å b: 166.45Å c: 79.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.235
Expression system: Escherichia coli

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Citations

2 review citations

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

2 mentions without citation

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