The antibacterial target, enoyl-acyl carrier protein (ACP) reductase, is a homotetrameric enzyme that catalyzes the last reductive step of fatty acid biosynthesis. In the present paper, Surflex docking has been carried out on a series (10 compounds) of enoyl ACP reductase inhibitors, using the SYBYL-X 2.0 package (Tripos Inc., St. Louis, USA). Surflex-docking studies revealed that the carbonyl group and pyrazole ring were significant for binding to the receptor, and it is also found that the pattern of binding of tested compounds is same as that of the 4TZK ligand, this in turn helped in understanding of specific activity of compounds.