Here　a　molecular　docking　and　3D-QSAR　study　is　reported　on　a　series　of　2-(oxalic　monoamido)benzoic　acid　(OBA)　inhibitors　and　protein　tyrosine　phosphatase　1B　(PTP1B).　Firstly,　a　flexible　docking　method　(FlexX)　was　used　to　place　12　OBA　inhibitors　into　the　active　site　of　PTP1B.　The　predicted　binding　affinities　of　the　molecules　were　found　to　be　linearly　relevant　to　their　experimental　activities　(pK(i),　non-cross-validated　R-2=0.859).　After　that,　33　OBA　inhibitors　were　fixed　into　the　predicted　binding　conformation,　and　were　studied　using　CoMFA　method.　The　resulting　CoMFA　model　(cross-validated　q(2)　=　0.650)　could　predict　the　activity　of　6　molecules　in　the　test　set　within　a　mean　unsigned　error　of　0.177,　and　match　the　characters　of　our　binding　mode　perfectly.　The　discovered　binding　mode　could　provide　hints　to　further　modification　of　inhibitors.