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Crystal structure analysis of human leukotriene C4 synthase at 1.9 ångström resolution

Analyse Crystal structure analysis of human leukotriene C4 synthase at 1.9 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PCV
Type: protein
Length: 146 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: GSH, UNL, SO4

Structure

x-ray diffraction · 1 distinct chain · 89% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Leukotriene C4 synthase (EC 4.4.1.20)	protein	146	89% helix, 0% strand	Q16873

Ligands and binding sites

GSH · Glutathione · ligand · chains A
UNL · Unknown ligand · ion · 4 copies · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
LMT · Dodecyl-beta-D-maltoside · additive · 11 copies · chains A
EDO · 1,2-ethanediol · additive · 4 copies · chains A

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

Compared structures

3PCV · Crystal structure analysis of human leukotriene C4 synthase at 1.9 angstrom resolution · 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 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q16873
Elsewhere: RCSB PDB 3PCV · PDBe 3PCV · UniProt Q16873

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