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Updated: Oct 25, 2026

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
Published on: June 20, 2025
How Many Crystal Structures Do You Need to Trust Your Docking Results?
Alexander Matthew Payne1,2, Benjamin Kaminow2,3, Hugo I MacDermott-Opeskin4
1Tri-Institutional Ph.D. Program in Chemical Biology, Weill Cornell Medical College, New York, New York10065, United States.
Abstract:
Structure-based drug discovery relies on the prediction of protein-bound poses of new molecule designs, the accuracy of which can impact downstream prioritization. While it is expected that crystal structures of similar molecules would provide the best template for predicting the poses of new designs, the time and cost required motivates identifying a point of diminishing returns for collecting new structures. Using 403 crystal structures of SARS-CoV-2 main protease from the open science COVID Moonshot project, we explore the tradeoff between the cost and utility of obtaining crystal structures for accurately predicting poses of designed molecules. We observe that similar reference ligands enable superior pose prediction and show that success plateaus after approximately five crystal structures per generic Bemis-Murcko scaffold, exceeding 95% for the campaign's lead series. This work provides practical recommendations for resource allocation in structure-enabled drug discovery campaigns.
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