1PX7

A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate

Summary for 1PX7

• Entry DOI: 10.2210/pdb1px7/pdb
• Related: 1PX6
• Descriptor: Glutathione S-transferase P, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLUTATHIONE, ... (5 entities in total)
• Functional Keywords: glutathione transferase, helix capping, mutations, protein folding, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P09211
• Total number of polymer chains: 2
• Total formula weight: 47566.39

Authors

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. (deposition date: 2003-07-02, release date: 2003-07-22, 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.; The multi-functional role of a highly conserved aspartic acid residue in glutathione transferase P1-1; To be Published,

Experimental method

X-RAY DIFFRACTION (2.03 Å)