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

The multi-functional role of a highly conserved aspartic acid residue in glutathione transferase P1-1

pi Glutathione Transferase, GST class-pi, GSTP1-1

MES, PEG 8000, CALCIUM CHLORIDE, DTT(DITHIOTHREITOL), GLUTATHIONE(REDUCED), pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K

the same protein including mutation D152N

The asymmetric unit consists of a dimer, which is also the biological form of the protein.

glutathione transferase, helix capping, mutations, protein folding, TRANSFERASE