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Both PLA<jats:sub>2<\/jats:sub>s present close molecular weights of 13,534 and 13,430\u2009Da and Isoectric pH\u00a0(pI) 7.38 and 7.86 respectively, for Cc<jats:sub>1<\/jats:sub>\u2010PLA<jats:sub>2<\/jats:sub> and Cc<jats:sub>2<\/jats:sub>\u2010PLA<jats:sub>2<\/jats:sub>. These Ca<jats:sup>2+<\/jats:sup>\u2010dependent enzymes showed a high catalytic activity upon phospholipids, inducing indirect hemolysis, since they conserve the catalytic domain of PLA<jats:sub>2<\/jats:sub>s <jats:sup>26<\/jats:sup>CYCGWGGKG<jats:sup>34<\/jats:sup>. They exhibited dual inhibition of platelet aggregation by targeting P<jats:sub>2<\/jats:sub>Y<jats:sub>12<\/jats:sub> and TP\u03b1 receptors preventing Adenosine diphosphate\/arachidonate binding and blood clotting. These effects are due to the interaction of Cc<jats:sub>1<\/jats:sub>\u2010PLA<jats:sub>2<\/jats:sub>s\/Cc<jats:sub>2<\/jats:sub>\u2010PLA<jats:sub>2<\/jats:sub>s with factor FXa through a noncatalytic PL\u2010independent mechanism leading to nonreleased thrombin. Both proteins consist of 120 amino acid residues and share similar three\u2010dimensional structures close to other SV\u2010PLA<jats:sub>2<\/jats:sub>s. Structural data of PLA<jats:sub>2<\/jats:sub>s allowed the relevant residues involved in binding to FXa and platelet receptors. 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