Human　immunodeficiency　virus　type　1　(HIV-1)　integrase　(IN)　is　an　essential　enzyme　in　the　lifecycle　of　this　virus　and　also　an　important　target　for　the　study　of　anti-HIV　drugs.　The　binding　modes　of　the　wild　type　IN　core　domain　and　the　W132G　mutant　with　the　hydroxycoumarin　compound　NSC158393　were　investigated　by　using　the　＂relaxed　complex＂　molecular　docking　approach　and　molecular　dynamics　(MD)　simulation.　Based　on　results　of　molecular　docking　experiment,　NSC15893　binds　the　backbone　of　the　128-136　peptide　adjacent　to　the　dimer　interface.　The　W132G　substitution　slightly　distort　the　binding　pocket　of　NSC158393,　thus　inducing　the　change　of　the　binding　mode.　From　the　comparative　analysis　of　the　MD　trajectories　of　the　wild　type　IN　and　the　IN-NSC158393　complex,　it　is　found　that　the　binding　of　NSC15893　diminishes　the　mobility　of　the　function　loop　of　IN.　All　the　above　results　are　consistent　with　experiments,　providing　us　some　helpful　information　for　understanding　the　mechanism　of　the　coumarin-based　inhibitors.