› 3leo

X-ray diffraction
2.1Å resolution

Structure of human Leukotriene C4 synthase mutant R31Q in complex with glutathione

Released:
DOI: 10.2210/pdb3leo/pdb
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Source organism: Homo sapiens
Primary publication:
Arginine 104 is a key catalytic residue in leukotriene C4 synthase.
Rinaldo-Matthis A, Wetterholm A, Martinez Molina D, Holm J, Niegowski D, Ohlson E, Nordlund P, Morgenstern R, Haeggström JZ
OpenAccess logo J Biol Chem 285 40771-6 (2010)
PMID: 20980252

Function and Biology Details

Reaction catalysed: 
Leukotriene C(4) = leukotriene A(4) + glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dodecamer
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leukotriene C4 synthase Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.25 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q16873 (Residues: 2-150; Coverage: 99%)
Gene name: LTC4S
Sequence domains: MAPEG family
Structure domains: Membrane associated eicosanoid/glutathione metabolism-like domain

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
6 bound ligands:
Ligand PAM 2 x PAM
Ligand PLM 6 x PLM
Ligand SO4 2 x SO4
Ligand NI 2 x NI
Ligand LMT 1 x LMT
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: F23
Unit cell:
a: 169.54Å b: 169.54Å c: 169.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.172 0.196
Expression system: Komagataella pastoris

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Citations

8 review citations

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

2 mentions without citation

Arginine 104 is a key catalytic residue in leukotriene C4 synthase.
Rinaldo-Matthis et al. (2010)
1 more

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