2GST
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
Summary for 2GST
Entry DOI | 10.2210/pdb2gst/pdb |
Descriptor | GLUTATHIONE S-TRANSFERASE, SULFATE ION, L-gamma-glutamyl-S-[(9S,10S)-10-hydroxy-9,10-dihydrophenanthren-9-yl]-L-cysteinylglycine, ... (4 entities in total) |
Functional Keywords | glutathione transferase |
Biological source | Rattus rattus (black rat) |
Cellular location | Cytoplasm: P04905 |
Total number of polymer chains | 2 |
Total formula weight | 52832.81 |
Authors | Ji, X.,Armstrong, R.N.,Gilliland, G.L. (deposition date: 1993-06-07, release date: 1993-10-31, Last modification date: 2023-08-30) |
Primary citation | Ji, X.,Johnson, W.W.,Sesay, M.A.,Dickert, L.,Prasad, S.M.,Ammon, H.L.,Armstrong, R.N.,Gilliland, G.L. Structure and function 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. Biochemistry, 33:1043-1052, 1994 Cited by PubMed: 8110735DOI: 10.1021/bi00171a002 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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