Non-structural protein 1, a highly conserved influenza virus protein, has been demonstrated previously to be a potential target for antiviral development.Several benzamide derivatives have been identified that inhibit NS1 function specifically and suppress virus replication.But the inhibition mechanism of these inhibitors in NS 1 is unclear.In this paper, the binding site of these inhibitors to NS 1 was explored.Potential ligand binding sites were predicted by Q-SiteFinder and blind docking of JJ3297 (a representative small molecule of benzamide derivatives) to NS1.In order to find the inhibitor binding site, JJ3297 was submitted to docking simulations, in which JJ3297 were docked into each predicted binding sites of each NS1 3-D structures that retrieved from PDB.Meanwhile, a series of benzamide derivatives were docked into five predicted binding sites used 2Z0A as NS1 3-D structure.In order to identify the key features in the interaction between NS1 and ligands, molecular dynamics simulation and MM-GBSA calculation were performed on JJ3297-NS1 complex.