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Germin like proteins (GLPs) is a heterogeneous group of proteins that are part of Cupin superfamily. Various GLPs of Grapevine (VvGLP3) have been identified and characterized at molecular but not at the structural level. This study analyzes the structure of VvGLP3 to elucidate its role in defense against powdery mildew disease caused by Erysiphe necator. Physiochemical analysis through the high aliphatic index (AI), low instability index and grand average of hydropathy (GRAVY) reveal that VvGLP3 is heat stable hydrophobic protein. InterProScan was used to check the similarity of VvGLP3 to other GLPs and TMHMM indicates that VvGLP3 is a transmembrane protein. Secondary structure of VvGLP3 reveals that it consists of random coils followed by extended ?-helix and ?-trends and I-TASSER was employed to construct a 3-D structure of VvGLP3. A molecular docking approach was applied to study molecular interaction and binding pattern by Auto Dock Vina. I-TASSER and SOPMA were used to determine the functionally important residues and their role. In the present study, molecular docking binding affinity energy is from -1.5 to -1.3 of germin like protein with manganese (Mn+2) co-factor which depict its role in defense against powdery mildew disease.