Improving Stereochemical Limitations in Protein–Ligand Complex Structure Prediction

AlphaFold3 has revolutionized biology by enabling the prediction of protein complexes with various biomolecules, including small molecular ligands. However, the ligand structures predicted by the model often contain stereochemical errors. In this study, our comprehensive evaluation of AlphaFold3 and its clone model, Boltz-1, demonstrated significant limitations in the ligand stereochemistry of their predicted structures, including chirality, bond lengths, and bond angles. To address this issue, we developed the restraint-guided inference method that applies stereochemical restraints during the reverse diffusion process. This approach perfectly reproduces the chirality specified in the input chemical structure and improves bond and angle geometries of ligands, while maintaining comparable performance in binding pose prediction. Our method provides a practical solution to the stereochemical errors in predicting protein-ligand complexes, thereby enhancing structure prediction applications in structural biology and drug discovery.

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Publication Details

Journal
ACS Omega
Published
2025-11-10
DOI
https://doi.org/10.1021/acsomega.5c07675
Citations
5
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
4.03
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article

Improving Stereochemical Limitations in Protein–Ligand Complex Structure Prediction

Ryuichiro Ishitani, Yoshitaka Moriwaki
5 citations
ACS Omega
Protein Structure and Dynamics
4.03
article

Improving Stereochemical Limitations in Protein–Ligand Complex Structure Prediction

Ryuichiro Ishitani, Yoshitaka Moriwaki
article en
5 citations

Abstract

AlphaFold3 has revolutionized biology by enabling the prediction of protein complexes with various biomolecules, including small molecular ligands. However, the ligand structures predicted by the model often contain stereochemical errors. In this study, our comprehensive evaluation of AlphaFold3 and its clone model, Boltz-1, demonstrated significant limitations in the ligand stereochemistry of their predicted structures, including chirality, bond lengths, and bond angles. To address this issue, we developed the restraint-guided inference method that applies stereochemical restraints during the reverse diffusion process. This approach perfectly reproduces the chirality specified in the input chemical structure and improves bond and angle geometries of ligands, while maintaining comparable performance in binding pose prediction. Our method provides a practical solution to the stereochemical errors in predicting protein-ligand complexes, thereby enhancing structure prediction applications in structural biology and drug discovery.

ACS OmegaVol. 10(46)
Tokyo Medical and Dental University (JP), The University of Tokyo (JP)
Openalex Percentile: Top 6%
Protein Structure and Dynamics
4.03
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Improving Stereochemical Limitations in Protein–Ligand Complex Structure Prediction — Ryuichiro Ishitani, Yoshitaka Moriwaki · ACS Omega (2025) | TGRS Research Map | TGRS