1MD4
A folding mutant of human class pi glutathione transferase, created by mutating glycine 146 of the wild-type protein to valine
Summary for 1MD4
Entry DOI | 10.2210/pdb1md4/pdb |
Related | 1MD3 |
Descriptor | pi glutathione transferase, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLUTATHIONE, ... (4 entities in total) |
Functional Keywords | gst, nucleation mechanism, conserved folding module, transferase |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 2 |
Total formula weight | 47582.42 |
Authors | Kong, G.K.-W.,Dragani, B.,Aceto, A.,Cocco, R.,Mannervik, B.,Stenberg, G.,McKinstry, W.J.,Polekhina, G.,Parker, M.W. (deposition date: 2002-08-06, release date: 2002-08-21, Last modification date: 2023-10-25) |
Primary citation | Kong, G.K.-W.,Polekhina, G.,McKinstry, W.J.,Parker, M.W.,Dragani, B.,Aceto, A.,Paludi, D.,Principe, D.R.,Mannervik, B.,Stenberg, G. Contribution of Glycine 146 to a Conserved Folding Module Affecting Stability and Refolding of Human Glutathione Transferase P1-1 J.Biol.Chem., 278:1291-1302, 2003 Cited by PubMed: 12414796DOI: 10.1074/jbc.M209581200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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