› 1oac

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF ESCHERICHIA COLI AT 2 ANGSTROEMS RESOLUTION

Released:
DOI: 10.2210/pdb1oac/pdb
PDB entry 1oac coloured by chain, front view.
PDB entry 1oac coloured by chain, side view.
PDB entry 1oac coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.
Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF
Structure 3 1171-84 (1995)
PMID: 8591028

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
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 PX9.6
Spacegroup: P212121
Unit cell:
a: 135.732Å b: 167.775Å c: 81.904Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 not available not available

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Citations

22 review citations

Structure and function of enzymes of the Leloir pathway for galactose metabolism.
Holden et al. (2003)
21 more

13 mentions without citation

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