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Crystal structure of human leukotriene C4 synthase in complex with substrate glutathione

Analyse Crystal structure of human leukotriene C4 synthase in complex with substrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2UUH
Type
protein
Length
150 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Leukotriene C4 synthase
EC
4.4.1.20
UniProt
Q16873
Ligands
PLM, LMU, GSH, PAM, NI, SO4

Structure

x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALeukotriene C4 synthase (EC 4.4.1.20)protein15085% helix, 0% strandQ16873

Ligands and binding sites

  • PLM · Palmitic acid · ligand · 5 copies · chains A
  • LMU · Dodecyl-alpha-D-maltoside · ligand · chains A
  • GSH · Glutathione · ligand · chains A
  • PAM · Palmitoleic acid · ligand · chains A
  • NI · Nickel (II) ion · metal · 2 copies · chains A
  • SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 2UUH · Crystal structure of Human Leukotriene C4 Synthase in complex with substrate glutathione · the same entry in another collection · chain A against A, TM-score 1.00
  • Q16873 · AlphaFold monomer V2.0 prediction for leukotriene C4 synthase (Q16873) · a predicted model of the same protein · chain A against A, TM-score 0.96

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