Fig. 4

Multiple sequence alignment of caspases from Mytilus coruscus and Homo sapiens. The catalytic dyad (blue), residues that participate in the stabilization of the carboxylate side chain of the Asp (red), the pocket physical shape of the P4-binding site of caspase-3 is partially conferred by Trp (pink), and residues that contribute to the ‘oxyanion hole’ (green) are indicated. Green boxes represent pentapeptide sites