Phospholipases A2 (PLA2s) hydrolyze glycer- ophospholipids at the sn-2 position of the glycerol back- bone. These enzymes are widely distributed in nature, and 15 groups including many subgroups have been described (Schaloske and Dennis, 2006). The venoms of snakes clas- sified in the families Colubridae (sensu lato), Elapidae and Viperidae constitute rich sources of PLA2s, and at least two independent recruitment events occurred for these enzymes during snake venom evolution (Fry and Wüster, 2004). On the basis of structural features, snake venom PLA2s are classified within groups I (elapid enzymes) and II (viperid enzymes) (Fry et al., 2008). The amino acid sequences of many snake venom PLA2s and the crystal structure of a number of them have been reported. Such structural characterization has revealed a relatively high identity in many of their sequences and a conserved structural scaffold. Nevertheless, these enzymes display an