Sea anemones release Phospholipase A2 toxins which block human TRPV1 channel. Here four Phospholipase A2 toxins were retrieved from four Bunodosoma caisarum, Condylatic gigantea, Urticina crassicornis and Adamsia palliata. The present work represents detail in silico study of these four Phospholipase A2 toxins and their probable molecular interaction with human TRPV1 channel. To know the molecular interaction between Phospholipase A2 toxins and TRPV1 channel, Cluspro was used. Homology modeling was performed through Swissmodel. Motif and Domain prediction was performed through GenomeNet and NCBI domain search. Cleft analysis was carried out through PDBsum and energy minimization was done by Deep swiss PDB viewer. Amino acid interaction of docked model was carried out through Ligplot+. The focus of this paper is to reveal the probable molecular interaction between the sea anemone Phospholipase A2 toxins and TRPV1 channels find out the amino acid interaction between them. Cleft analysis revealed that large cleft provides increased opportunity for protein to interact with ligand. Lower energy value revealed that docked models are stable and energy minimized. Ligplot+ interaction shows that mainly hydrophobic amino acids are involved and domains are playing important role in docking. Actually PLA2c domain of Phospholipase A2 toxins and EFh domain of TRPV1 channel participate in docking. Thus this study tried to establish probable molecular interaction between Phospholipase A2 toxins with human TRPV1 channel and provides an insight for better understanding of these types of cnidarians toxins.