A double mutation of Y197C,V266H restores activity and structure similar to that of wild-type
(A) Additional mutations made in the context of V266H. Numbers in parentheses indicate change in kcat/Km values in terms of ΔΔG° (kcal/mol), as described in the text. (B) Dimer interface of caspase-3 (Y197C,V266H). (C) Interactions among Lys137, Thr140, Glu190 and Tyr195. (D) Comparison of changes in helix 3 and the active site of monomer B. For (B–D), the following colour scheme is used: Y197C,V266H (grey), V266H (yellow) and wild-type (green).