InfectionwithHuman ImmunodeficiencyVirus (HIV) followed by immune deficiency is amajor threat to human.As HIV1 protease is essential for the proteolytic cleavage of precursor viral protein, it remains as an effective and more reasonable target for drug design against HIV. In the present work, we resolved a three dimensional structure of HIV 1 protease using comparative modeling technique and identified the active sites. We designed a lead candidate using hydrogen bonding potential and amino acids active site affinities. Validation was done using in silico docking techniques. The result clearly demonstrates the binding affinity of the drug candidate with the HIV 1 protease. The current study offers a new drug candidate that has promising inhibitory activity on the HIV 1 protease.