› 3v99

X-ray diffraction
2.25Å resolution

S663D Stable-5-LOX in complex with Arachidonic Acid

Released:
DOI: 10.2210/pdb3v99/pdb
PDB entry 3v99 coloured by chain, front view.
PDB entry 3v99 coloured by chain, side view.
PDB entry 3v99 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at Serine-663.
Gilbert NC, Rui Z, Neau DB, Waight MT, Bartlett SG, Boeglin WE, Brash AR, Newcomer ME
FASEB J 26 3222-9 (2012)
PMID: 22516296

Function and Biology Details

Reaction catalysed: 
(1a) arachidonate + O(2) = (5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyunsaturated fatty acid 5-lipoxygenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 691 amino acids
Theoretical weight: 79.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09917 (Residues: 1-674; Coverage: 100%)
Gene names: ALOX5, LOG5
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand FE2 2 x FE2
Ligand ACD 1 x ACD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 51.755Å b: 200.844Å c: 72.184Å
α: 90° β: 105.65° γ: 90°
R-values:
R R work R free
0.188 0.186 0.233
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Mammalian lipoxygenases and their biological relevance.
Kuhn et al. (2015)
3 more

51 mentions without citation

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
50 more