Reverse transcriptase of the human immunodeficiency virus reads the sequence of viral RNA nucleic acids that have entered the host cell and transcribes the sequence into complementary DNA sequence. Reverse transcriptase protein structure was retrieved from NCBI and the similarity searches were made by using BLAST PDB Database, and further the protein structure is modeled using Modeler 9v1. Structural visualization of reverse transcriptase was done by Accerlys Discovery Studio. Using Q-Site Finder, prediction of ligand binding site was done. The three dimensional structure of inhibitots viz., 3,6-Pyridazinedione, 1,2-dihydro-4-methyl, 4-H-pyran-4 one, 2,3 dihydro-3,5-dihydroxy-6-methyl-, 1H-inden-1-one,2,3,dihydro, d-Mannose, 1,6-an hydro-a-D-gluco pyranose (Levoglucosan), m-toluic acid, allyl ester, Erythrocentaurin,1H-indole-2,3-dione,1 methyl ,3-hydrazone 2H-Pyra-2-one,5,6-dihydro-4-(2-methyl-2-propen-3yl)-, were obtained from GC-MS analysis and further the structure is drawn in ACD CHEM SKETCH software. Docking studies of 3,6-Pyridazinedione, 1,2-dihydro-4-methyl, 4-H-pyran-4 one , 2,3 dihydro-3,5-dihydroxy-6-methyl-, 1H-inden-1-one,2,3,dihydro, d-Mannose, 1,6-an hydro-a-D-gluco pyranose (Levoglucosan), m-toluic acid, allyl ester, Erythrocentaurin,1H-indole-2,3-dione, 1 methyl, 3-hydrazone 2H-Pyra-2-one,5,6-dihydro-4-(2-methyl-2-propen-3yl)-, against reverse transcriptase was undertaken to gain insight in to the binding mode of the investigated compounds at the active site of reverse transcriptase.1-6-An hydro-a-D-glucopyranose compound were found to be active againse reverse transcriptase as indicated by docking results; the best being 1-6-An hydro-a-D-glucopyranose. Results suggest that 1-6-An hydro-a-D-glucopyranose should be evaluated further for therapeutic use in combination of HIV/AIDS drugs. Further, this may be confirmed by drug trial to find out the effeciency in inhibiting reverse transcriptase activity to treat HIV/AIDS complications.
