› 4kvl

X-ray diffraction
1.96Å resolution

Crystal structure of Oryza sativa fatty acid alpha-dioxygenase Y379F with palmitic acid

Released:
DOI: 10.2210/pdb4kvl/pdb
PDB entry 4kvl coloured by chain, front view.
PDB entry 4kvl coloured by chain, side view.
PDB entry 4kvl coloured by chain, top view.
Source organism: Oryza sativa
Primary publication:
Crystal structures of α-dioxygenase from Oryza sativa: insights into substrate binding and activation by hydrogen peroxide.
Zhu G, Koszelak-Rosenblum M, Malkowski MG
Protein Sci 22 1432-8 (2013)
PMID: 23934749

Function and Biology Details

Reaction catalysed: 
A fatty acid + O(2) = a (2R)-2-hydroperoxyfatty acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173886 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-dioxygenase PIOX Chain: A
Molecule details ›
Chain: A
Length: 621 amino acids
Theoretical weight: 70.95 KDa
Source organism: Oryza sativa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2QRV3 (Residues: 10-618; Coverage: 99%)
Gene names: LOC_Os12g26290, Os12g0448900, PIOX
Sequence domains: Animal haem peroxidase
Structure domains: Haem peroxidase domain superfamily, animal type

Ligands and Environments

9 bound ligands:
Ligand HEM 1 x HEM
Ligand PLM 2 x PLM
Ligand CA 1 x CA
Ligand IMD 1 x IMD
Ligand BOG 2 x BOG
Ligand 1PE 1 x 1PE
Ligand PGE 6 x PGE
Ligand PG4 1 x PG4
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: I222
Unit cell:
a: 72.887Å b: 130.202Å c: 188.173Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.157 0.186
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biosynthesis and analysis of plant oxylipins.
Griffiths G. (2015)
1 more

1 mention without citation

Crystal structures of α-dioxygenase from Oryza sativa: insights into substrate binding and activation by hydrogen peroxide.
Zhu et al. (2013)