 Grx2 has significantly higher catalytic activity in the reduction of mixed disulphides with glutathione (GSH) compared with other glutaredoxins.The active site residues (Cys9-Pro10-Tyr11-Cys12, in "Escherichia coli" Grx2, which are found at the interface between the N- and C-terminal domains are identical to other glutaredoxins, but there is no other similarity between glutaredoxin 2 and other glutaredoxins.Grx2 is structurally similar to glutathione-S-transferases (GST), but there is no obvious sequence similarity.