› 1rrl

X-ray diffraction
2.09Å resolution

Function and Biology Details

Reaction catalysed: 
Linoleate + O(2) = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140587 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Seed linoleate 9S-lipoxygenase-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 857 amino acids
Theoretical weight: 96.92 KDa
Source organism: Glycine max
UniProt:
  • Canonical: P09186 (Residues: 1-857; Coverage: 100%)
Gene names: LOX1.3, LOX3
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand FE2 2 x FE2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 106.4Å b: 133.5Å c: 60.7Å
α: 90° β: 97.3° γ: 90°
R-values:
R R work R free
0.212 0.207 0.305

Quick links

Citations

8 citation in other articles

Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data.
Choi et al. (2008)
7 more

2 mentions without citation

Fluctuations of an exposed π-helix involved in lipoxygenase substrate recognition.
Bradshaw et al. (2014)
1 more