High-Confidence Structural Modeling of ATP Binding to the Catalytic Active Site of Bangladeshi Daboia russelii Phospholipase A₂ (sPLA₂)

This dataset presents novel in-silico evidence of a stable interaction between Adenosine Triphosphate (ATP) and the secreted Phospholipase A₂ (sPLA₂) toxin from the Bangladeshi Russell's Viper (Daboia russelii). Using the AlphaFold 3 (AF3) deep learning architecture, a specific docking simulation was performed. The resulting model demonstrates: ipTM Score: 0.76, indicating a high-confidence structural interaction. pTM Score: 0.88, confirming the high quality of the overall protein folding. Binding Site: Preliminary analysis suggests ATP occupies the catalytic cleft of the sPLA₂ enzyme. Significance:While 2024 literature has identified ATP as a regulator for human calcium-independent iPLA₂, this simulation provides the first structural evidence of ATP binding to the venomous sPLA₂ variant. This suggests a potential mechanism for endogenous regulation or the development of ATP-mimetic inhibitors to neutralize Russell's Viper venom. Methodology:Data was generated on March 19, 2026. The simulation includes the primary sequence of Bangladeshi D. russelii PLA₂ and the ATP ligand. The provided ZIP file contains the raw coordinate files (.cif), Job ID metadata, and confidence plots (PAE and pLDDT).