Binding modes of a series of quinoline-3-carbohydrazide as protein tyrosine phosphatase 1B (PTP 1B) inhibitors have been identified by molecular modeling techniques. We have performed docking and ADME predictions of these inhibitors with PTP 1B enzyme. As per our literature, we found that PTP1B is highly hydrophobic. The results indicate that quinoline-3- carbohydrazide for addition to hydrogen bonding interactions, Arg24, Asp48, Glu115, Lys116, Lys120, Cys215, Ser216, Ala217 amino acid residues of PTP 1B are responsible for governing inhibitor potency of the compounds. ADME predictions of 6 top selected compounds were done with Qikprop 3.2 tool available in Schrödinger 9.0 ver. The information generated from the present study should be useful in the design of more potent PTP1B inhibitors as antidiabetic agents.