The pharmacological potential of sea anemone toxins has prompted the improvement of the biochemical and structural knowledge of such toxic proteins. Cangitoxin (CGX) is a new sea anemone toxin found in Bunudosoma cangicum. Long range molecular dynamics in vacuum and also with an explicit solvent representation was used to generate a structural model of CGX. The main structural features, three S–S bridges and anti-parallel β-sheet strands that characterize all known sea anemone toxins, are observed in the final CGX model. The structural analysis of CGX clearly suggests this protein just like a type-I sea anemone toxin. Additionally, the presence of an intensive positive electrostatic field related to positive residues at the vicinity of position 35 and a salt bridge configuration obtained for the Arg14 containing-loop could be directly involved in tissue discrimination and binding affinity of CGX to the Na + channel receptor.