In the present study, the Hymenopterans wasp Vespa velutina (Asian yellow-legged hornet), Vespa affinis (Lesser banded hornet) and Vespula squamosa (Southern yellow jacket) venom protein Phospholipase A1 sequences were selected for In-silico analysis. The venom protein sequence was retrieved from the UniProtKB protein database, using those sequences their physicochemical properties were analysed from the ProtParam tool. Secondary structural elements were predicted from the SOPMA tool. The 3D model was built using the SWISS-MODEL server. The final refined model was evaluated by using the PROCHECK, and Z-score. The venom protein Phospholipase A1, the basic molecular nature, composition and their biological properties were reported. ProtParam tool result shows that the protein belongs to the lipases family. The venom protein Phospholipase A1 is hydrolyzing the phospholipid at the 2-acyl-lysophospholipid position to the fatty acid. The most abundant amino acid was found as Leucine (28 residues) in Phospholipase A1 of Lesser banded hornet V. affinis, whereas the lowest was Tryptophan. It was observed that the random coil was predominant, followed by alpha-helix and extended strand in all the three wasp venom protein Phospholipase A1.The predicted 3D structure will support the understanding of the structure of the Phospholipase A1 in wasp species.