Assessing interaction recovery of predicted protein-ligand poses

The field of protein-ligand pose prediction has seen significant advances in recent years, with machine learning-based methods now being commonly used in lieu of classical docking methods or even to predict all-atom protein-ligand complex structures. Most contemporary studies focus on the accuracy and physical plausibility of ligand placement to determine pose quality, often neglecting a direct assessment of the interactions observed with the protein. In this work, we demonstrate that ignoring protein-ligand interaction fingerprints can lead to overestimation of model performance, most notably in recent protein-ligand cofolding models which often fail to recapitulate key interactions.Scientific Contribution The interaction analysis used in this study is provided as a python package at https://github.com/Exscientia/plif_validity .

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Publication Details

Journal
Journal of Cheminformatics
Published
2025-05-19
DOI
https://doi.org/10.1186/s13321-025-01011-6
Citations
15
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
12.09
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article

Assessing interaction recovery of predicted protein-ligand poses

Frédéric A. Dreyer, Cédric Bouysset, David Errington, Constantin Schneider
15 citations
Journal of Cheminformatics
Protein Structure and Dynamics
12.09
article

Assessing interaction recovery of predicted protein-ligand poses

Frédéric A. Dreyer, Cédric Bouysset, David Errington, Constantin Schneider
article en
15 citations

Abstract

The field of protein-ligand pose prediction has seen significant advances in recent years, with machine learning-based methods now being commonly used in lieu of classical docking methods or even to predict all-atom protein-ligand complex structures. Most contemporary studies focus on the accuracy and physical plausibility of ligand placement to determine pose quality, often neglecting a direct assessment of the interactions observed with the protein. In this work, we demonstrate that ignoring protein-ligand interaction fingerprints can lead to overestimation of model performance, most notably in recent protein-ligand cofolding models which often fail to recapitulate key interactions.Scientific Contribution The interaction analysis used in this study is provided as a python package at https://github.com/Exscientia/plif_validity .

Journal of CheminformaticsVol. 17(1)
Recursion (United States) (US)
Zero hunger
Openalex Percentile: Top 1%
Protein Structure and Dynamics
12.09
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