› 5mef

X-ray diffraction
2.36Å resolution

Cyanothece lipoxygenase 2 (CspLOX2) variant - L304F

Released:
DOI: 10.2210/pdb5mef/pdb
PDB entry 5mef coloured by chain, front view.
PDB entry 5mef coloured by chain, side view.
PDB entry 5mef coloured by chain, top view.
Source organism: Rippkaea orientalis PCC 8801
Primary publication:
Lipoxygenase 2 from Cyanothece sp. controls dioxygen insertion by steric shielding and substrate fixation.
Newie J, Neumann P, Werner M, Mata RA, Ficner R, Feussner I
Sci Rep 7 2069 (2017)
PMID: 28522865

Function and Biology Details

Reaction catalysed: 
Arachidonate + O(2) = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110498 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipoxygenase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 569 amino acids
Theoretical weight: 64.59 KDa
Source organism: Rippkaea orientalis PCC 8801
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B7JX99 (Residues: 1-569; Coverage: 100%)
Gene name: PCC8801_3106
Sequence domains: Lipoxygenase

Ligands and Environments

4 bound ligands:
Ligand FE 2 x FE
Ligand GOL 4 x GOL
Ligand IMD 5 x IMD
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 54.4Å b: 166.26Å c: 166.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.191 0.216
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The Oxylipin Pathways: Biochemistry and Function.
Wasternack et al. (2018)
4 other articles

2 mentions without citation

Highlight selection of radiochemistry and radiopharmacy developments by editorial board.
Bernardes et al. (2022)
1 more