OBJECTIVE： To study the binding mode and interaction of 17 main antiviral components in Yinqiao powder with neuraminidase （NA）. METHODS： The two-dimensional structure of 17 active components as glycyrrhizin， liquiritin， chlorogenic acid， 3，3′ ，4-trimethoxy ellagic acid in Yinqiao powder and positive control zanamivir were transformed into three-dimensional structure by using CORINA，UCSF Chimera 1.3 and AutoDock Tools 1.5.4 molecular docking software. Then the grids of acceptor protein NA were set up， and the docking program was run to perform the docking operation. Using estimation inhibit constant （Ki） and binding energy （ΔGbind） as reference indexes， the difference of virtual activity of the docking moleculars were compared， and its reasons were analyzed from the docking conformation. RESULTS： In the 17 active components， Ki value for molecule docking of chlorogenic acid was 1.20 μmol/L， and ΔGbind was －8.08 kcal/mol （1 kcal＝4.184 kJ）， which was better than zanamivir （Ki 2.26 μmol/L， ΔGbind －7.70 kcal/mol）. Ki and ΔGbind of 3，3′ ，4-trimethoxy ellagic acid were 149.41 μmol/L and －5.22 kcal/mol， which were the worst among 17 compounds. Chlorogenic acid and zanamivir were more closely matched to the active sites of NA active cavity in space from the docking conformation， and occupied all the active chambers except S5， which presented a strong binding effect with NA. The docking conformation of 3，3′ ，4-trimethoxy ellagic acid was not strong as its plane structure restricted the combination with NA active sites. CONCLUSIONS： Chlorogenic acid is the strongest antiviral activity component in the Yinqiao powder， whose virtual activity is even stronger than zanamivir. The virtual activity of 3，3′ ，4-trimethoxy ellagic acid may be the weakest as its mismatching with the NA active cavity. This study may provide some theoretical guidance for the development of NA inhibitors.