The reduction of dehydroascorbate(DHA)to ascorbic acid(AA)is a vital cellular function.The omega-class glutathione transferases(GSTs)catalyze several reductive reactions in cellular biochemistry,including DHA reduction.In humans,GSTO1-1 and GSTO2-2 are proved to be significant DHA reductase(DHAR)activity1.The structure of a human GSTO1-1(PDB ID: 3VLN)has been determined at 1.7(A)resolution in complex with the reaction product AA,which unexpectedly binds in the G-site,where the glutamyl moiety of GSH binds.In this work,molecular docking and molecular dynamics simulations were carried out to obtain the complex of GSTO-GSH-DHA and explore the conformational change of this complex.AutoDock4.2 software package2 was used to dock DHA into the active site of GSTO1-1.Then 40ns MD simulation was carried out by employing AMBER113.ff99SB force field4 was used here.Root mean square deviation(RMSD)was shown in Figure 1.By using clustering analysis in AmberTools1.5,the representative structure was obtained and was shown in Figure 2.This complex can be used as the starting structure of the reaction of reduction of dehydroascorbate(DHA)to ascorbic acid(AA).