NextTopDocker: A Large-Scale Docking-Power Benchmark Reveals Limitations of Current End-to-End Machine-Learning Docking and the Strength of Hybrid Rescoring
Open accessPublished version of a preprint
Abstract
Predicting three-dimensional binding orientations of drug-like molecules remains challenging in structure-based drug design. Despite methodological advances, docking performance is often assessed on small and outdated benchmarks. We present “NextTopDocker,” a large, up-to-date, open-access data set for docking-power assessment comprising 14,038 training and 5201 test entries across 3173 unique protein targets, constructed from the Protein Data Bank. Developed with open-source tools, it includes crystallographic structures, Smina-generated docking poses, and ligand-similarity-aware training subsets. We benchmarked four state-of-the-art machine-learning (ML) docking frameworks (DeepDock, Interformer, SurfDock, and Uni-Mol Docking v.2) against classical (Smina) and hybrid baselines (GNINA 1.3 and logistic regression using Smina and GNINA 1.3 scores). Interformer alone matched the docking power of logistic regression on Smina poses, while the others showed dependence on downstream physics-based correction. Most raw ML-generated poses displayed steric clashes and/or implausible geometries, highlighting the need for physics-informed constraints in autonomous docking. “NextTopDocker” is available at https://github.com/caominhtr/NextTopDocker and https://zenodo.org/records/17492994.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Accurate structure prediction of biomolecular interactions with AlphaFold 3
Abramson, J., Adler, J., Dunger, J., Evans, R., Green, T., Pritzel, A., Ronneberger, O., Willmore, L., Ballard, A. J., Bambrick, J., et al. (2024) · Nature · doi:10.1038/s41586-024-07487-w · Cited by 15,861 · see citing works
Larian Studios Dev Team (2024) · doi:10.1145/3292500.3330701 · Cited by 8,618 · see citing works
Evolutionary-scale prediction of atomic level protein structure with a language model
Lin, Z., Akin, H., Rao, R., Hie, B., Zhu, Z., Lu, W., Smetanin, N., Verkuil, R., Kabeli, O., Shmueli, Y., et al. (2022) · doi:10.1101/2022.07.20.500902 · Cited by 5,523 · see citing works
Shortcut learning in deep neural networks
Geirhos, R., Jacobsen, J.-H., Michaelis, C., Zemel, R., Brendel, W., Bethge, M., & Wichmann, F. A. (2020) · Nature Machine Intelligence · doi:10.1038/s42256-020-00257-z · Cited by 2,224 · see citing works
Performance of machine-learning scoring functions in structure-based virtual screening.
Wójcikowski, M., Ballester, P. J., & Siedlecki, P. (2017) · Scientific Reports · doi:10.1038/srep46710 · Cited by 364 · see citing works
Self-citation
Flagged first, then by citations
- Authors
- Truong, C.-M., Ballester, P. J., Taboureau, O., & Tran-Nguyen, V.-K.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Imperial College London (GB)
- Université Paris Cité, CNRS UMR 8251, INSERM ERL 1133 , ,
- Corresponding author
- Taboureau, Olivier
- Venue
- Journal of Medicinal Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2026-08-06
- Volume
- 69
- Issue
- 16
- Pages
- 19808-19821
- ISSN
- 0022-2623 (ISSN-L)
- 1520-4804
- PMC
- PMC13699998
- OpenAlex
- W7197002560
- Cited by
- 2
- References
- 6
- Citations by year
- 2026: 2
- FWCI
- 7.26
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Medicinal Chemistry (publishedVersion, cc-by)
- ChemRxiv (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion, cc-by)
- HAL (submittedVersion, cc-by)
- Funders
- Agence Nationale de la Recherche (ANR-25-CE45-0171)
- Topics
- Physical Sciences › Computer Science › Computational Theory and Mathematics › Computational Drug Discovery Methods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- structure-based drug design, GNINA, steric clashes, physics-informed constraints
- MeSH terms
- Machine Learning, Ligands, Proteins, Drug Design, Databases, Protein, Molecular Docking Simulation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review