Glial fibrillary acidic protein (GFAP) is an intermediate filament Type III protein and is containing three domains. The most conserved domain of GFAP is the rod domain. The present study has been made for in silico prediction to determine the three-dimensional structure of GFAP protein. It has been carried out through molecular modeling using MODELLER 9v5. Its active site residues has been predicted through comparative results of MODELLER 9v5. The ligands were designed using LigandScout 2.0. The designed ligand and receptor interaction studies were carried out through pharmacophore analysis followed by interaction studies using AUTODOCK4. Virtual screening of ligands has been performed by Molegro Virtual Docker. Analogues of ligands were generated through Chemsketch10.0 and ARG (258) was identified as a catalytic residue.
