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) |
Structure validation
Download full validation report