Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 9% strand (DSSP).

Ligands and binding sites

• GSH · Glutathione · ligand · 2 copies · chains A, B
• SO4 · Sulfate ion · ion · chains A, B
• MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 1321 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

• 1LBK · Crystal structure of a recombinant glutathione transferase, created by replacing the last… · the same entry in another collection · chain A against A, TM-score 1.00
• P08263 · AlphaFold monomer V2.0 prediction for glutathione S-transferase A1 (P08263) · a predicted model of the same protein · chain A against A, TM-score 0.87

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 P09211
• Every structure of UniProt P08263
• Elsewhere: RCSB PDB 1LBK · PDBe 1LBK · UniProt P09211 · UniProt P08263