2GTU

LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), MONOCLINIC CRYSTAL FORM

Summary for 2GTU

Entry DOI	10.2210/pdb2gtu/pdb
Descriptor	GLUTATHIONE S-TRANSFERASE (2 entities in total)
Functional Keywords	transferase, glutathione, conjugation, detoxification, cytosolic, dimer
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm: P28161
Total number of polymer chains	2
Total formula weight	51290.91
Authors	Patskovska, L.N.,Fedorov, A.A.,Patskovsky, Y.V.,Almo, S.C.,Listowsky, I. (deposition date: 1998-05-26, release date: 1999-03-02, Last modification date: 2023-08-09)
Primary citation	Patskovsky, Y.V.,Patskovska, L.N.,Listowsky, I. The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases. J.Biol.Chem., 275:3296-3304, 2000 Cited by PubMed: 10652317 DOI: 10.1074/jbc.275.5.3296 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.55 Å)

Structure validation