› 2sbl

X-ray diffraction
2.6Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE

Released:
DOI: 10.2210/pdb2sbl/pdb
PDB entry 2sbl coloured by chain, front view.
PDB entry 2sbl coloured by chain, side view.
PDB entry 2sbl coloured by chain, top view.
Source organism: Glycine max
Primary publication:
The three-dimensional structure of an arachidonic acid 15-lipoxygenase.
Boyington JC, Gaffney BJ, Amzel LM
Science 260 1482-6 (1993)
PMID: 8502991

Function and Biology Details

Reaction catalysed: 
Alpha-linolenate + O(2) = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139953 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Seed linoleate 13S-lipoxygenase-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 839 amino acids
Theoretical weight: 94.48 KDa
Source organism: Glycine max
Expression system: Not provided
UniProt:
  • Canonical: P08170 (Residues: 1-839; Coverage: 100%)
Gene names: LOX1, LOX1.1
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 184.5Å b: 125.6Å c: 94.7Å
α: 90° β: 102.9° γ: 90°
R-values:
R R work R free
0.173 0.173 not available
Expression system: Not provided

Quick links

Citations

38 review citations

Lipoxygenase and leukotriene pathways: biochemistry, biology, and roles in disease.
Haeggström et al. (2011)
37 more

5 mentions without citation

The structural basis for specificity in lipoxygenase catalysis.
Newcomer et al. (2015)
4 more