3GTU
LIGAND-FREE HETERODIMERIC HUMAN GLUTATHIONE S-TRANSFERASE M2-3 (EC 2.5.1.18), MONOCLINIC CRYSTAL FORM
Summary for 3GTU
Entry DOI | 10.2210/pdb3gtu/pdb |
Descriptor | GLUTATHIONE S-TRANSFERASE (3 entities in total) |
Functional Keywords | transferase, glutathione, conjugation, detoxification, cytosolic, heterodimer |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm: P28161 P21266 |
Total number of polymer chains | 4 |
Total formula weight | 104211.73 |
Authors | Patskovsky, Y.V.,Patskovska, L.N.,Listowsky, I. (deposition date: 1998-07-29, release date: 1999-07-29, Last modification date: 2024-05-22) |
Primary citation | Patskovsky, Y.V.,Patskovska, L.N.,Listowsky, I. An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases. Biochemistry, 38:16187-16194, 1999 Cited by PubMed: 10587441DOI: 10.1021/bi991714t PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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