In Silico Analysis of Size-Dependent Nucleotide Binding in the Helical Gap of Daboia russelii sPLA2 (P84674)

This study presents an in silico analysis of the interaction between adenosine nucleotides (AMP, ADP, and ATP) and a putative secondary binding site, referred to as the "helical gap," in the basic sPLA2 isoform (P84674) from Daboia russelii venom. Using a combination of AlphaFold 3 for structural modeling and AutoDock Vina for molecular docking, a size-dependent trend in ligand accommodation was identified.