› 2yr6

X-ray diffraction
1.35Å resolution

Crystal structure of L-phenylalanine oxidase from Psuedomonas sp.P501

Released:
DOI: 10.2210/pdb2yr6/pdb
PDB entry 2yr6 coloured by chain, front view.
PDB entry 2yr6 coloured by chain, side view.
PDB entry 2yr6 coloured by chain, top view.
Source organism: Pseudomonas sp. P-501
Primary publication:
Structural basis of proteolytic activation of L-phenylalanine oxidase from Pseudomonas sp. P-501.
Ida K, Kurabayashi M, Suguro M, Hiruma Y, Hikima T, Yamomoto M, Suzuki H
J Biol Chem 283 16584-90 (2008)
PMID: 18417467

Function and Biology Details

Reaction catalysed: 
L-phenylalanine + O(2) = 2-phenylacetamide + CO(2) + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178472 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine 2-monooxygenase precursor Chains: A, B
Molecule details ›
Chains: A, B
Length: 721 amino acids
Theoretical weight: 77.9 KDa
Source organism: Pseudomonas sp. P-501
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5W9R9 (Residues: 2-714; Coverage: 100%)
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
3 bound ligands:
Ligand SO4 2 x SO4
Ligand BE2 2 x BE2
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 100.877Å b: 113.029Å c: 136.463Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.104 0.103 0.138
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Flavin dependent monooxygenases.
Huijbers et al. (2014)
4 more

1 mention without citation

Structure of the flavoprotein tryptophan 2-monooxygenase, a key enzyme in the formation of galls in plants.
Gaweska et al. (2013)