1AGS
A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL
Summary for 1AGS
Entry DOI | 10.2210/pdb1ags/pdb |
Descriptor | GLUTATHIONE S-TRANSFERASE ALPHA, S-HEXYLGLUTATHIONE (2 entities in total) |
Functional Keywords | transferase (glutathione) |
Biological source | synthetic construct |
Cellular location | Cytoplasm: P09210 |
Total number of polymer chains | 2 |
Total formula weight | 52159.02 |
Authors | Zeng, K.,Rose, J.P.,Wang, B.C. (deposition date: 1995-01-23, release date: 1995-07-10, Last modification date: 2024-02-07) |
Primary citation | Zeng, K.,Rose, J.P.,Chen, H.C.,Strickland, C.L.,Tu, C.P.,Wang, B.C. A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal. Proteins, 20:259-263, 1994 Cited by PubMed: 7892174DOI: 10.1002/prot.340200306 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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