Structure of the xenobiotic substrate binding site of a glutathione S- transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9, 10-dihydrophenanthrene

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 9% strand (DSSP).

Ligands and binding sites

• GPR · (9R,10R)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene · ligand · 2 copies · chains A, B
• SO4 · Sulfate ion · ion · 7 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1391 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

• 3GST · Structure of the xenobiotic substrate binding site of a glutathione S-transferase as… · the same entry in another collection · chain A against A, TM-score 1.00
• P04905 · AlphaFold monomer V2.0 prediction for glutathione S-transferase mu 1 (P04905) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P04905
• Elsewhere: RCSB PDB 3GST · PDBe 3GST · UniProt P04905