PDBe 1u5u

X-ray diffraction
2Å resolution

The structure of an Allene Oxide Synthase reveals a novel use for a catalase fold

Released:

Function and Biology Details

Reactions catalysed:
(9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate = (9Z,15Z)- (13S)-12,13-epoxyoctadeca-9,11,15-trienoate + H(2)O. 
Arachidonate + O(2) = (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14- tetraenoate. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Allene oxide synthase-lipoxygenase protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 374 amino acids
Theoretical weight: 42.92 KDa
Source organism: Plexaura homomalla
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O16025 (Residues: 1-374; Coverage: 35%)
Structure domains: Catalase HpII, Chain A, domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CAMD BEAMLINE GCPCC
Spacegroup: C2
Unit cell:
a: 147.94Å b: 76.679Å c: 77.761Å
α: 90° β: 109.66° γ: 90°
R-values:
R R work R free
0.209 0.196 0.239
Expression system: Escherichia coli BL21(DE3)