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; PubMed: 12414796; DOI: 10.1074/jbc.M209581200

Experimental method

X-RAY DIFFRACTION (2.1 Å)