Metal3D: a general deep learning framework for accurate metal ion location prediction in proteins
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Abstract
Metal ions are essential cofactors for many proteins and play a crucial role in many applications such as enzyme design or design of protein-protein interactions because they are biologically abundant, tether to the protein using strong interactions, and have favorable catalytic properties. Computational design of metalloproteins is however hampered by the complex electronic structure of many biologically relevant metals such as zinc . In this work, we develop two tools - Metal3D (based on 3D convolutional neural networks) and Metal1D (solely based on geometric criteria) to improve the location prediction of zinc ions in protein structures. Comparison with other currently available tools shows that Metal3D is the most accurate zinc ion location predictor to date with predictions within 0.70 ± 0.64 Å of experimental locations. Metal3D outputs a confidence metric for each predicted site and works on proteins with few homologes in the protein data bank. Metal3D predicts a global zinc density that can be used for annotation of computationally predicted structures and a per residue zinc density that can be used in protein design workflows. Currently trained on zinc, the framework of Metal3D is readily extensible to other metals by modifying the training data.
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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
SciPy 1.0: fundamental algorithms for scientific computing in Python
Virtanen, P., Gommers, R., Oliphant, T. E., Haberland, M., Reddy, T., Cournapeau, D., Burovski, E., Peterson, P., Weckesser, W., Bright, J., et al. (2020) · Nature Methods · doi:10.1038/s41592-019-0686-2 · Cited by 38,430 · see citing works
Highly accurate protein structure prediction for the human proteome
Tunyasuvunakool, K., Adler, J., Wu, Z., Green, T., Zielinski, M., Žídek, A., Bridgland, A., Cowie, A., Meyer, C., Laydon, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03828-1 · Cited by 3,025 · cited 3× · see citing works
“For human palmitoyltransferase ZDHHC23 (Uniprot Q8IYP9) a high con fi dence AlphaFold2 prediction exists but AlphaFill cannotplacethezincionsbecausethesequenceidentity is24%tothe closest PDB structure (PDB 6BMS 47 ), i.e. below the 25% cutoff.”
Metal ions in biological catalysis: from enzyme databases to general principles
Andreini, C., Bertini, I., Cavallaro, G., Holliday, G. L., & Thornton, J. M. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0404-5 · Cited by 1,150 · see citing works
3D deep convolutional neural networks for amino acid environment similarity analysis
Torng, W., & Altman, R. B. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1702-0 · Cited by 142 · see citing works
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- Authors
- Dürr, S. L., Levy, A., & Rothlisberger, U.
- Affiliations
- École Polytechnique Fédérale de Lausanne (CH)
- Venue
- Nature Communications
- Published
- 2023-05-11
- Volume
- 14
- Issue
- 1
- Pages
- 2713-2713
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC10175565
- OpenAlex
- W4376225285
- Cited by
- 88
- References
- 5
- Citations by year
- 2026: 35 · 2025: 30 · 2024: 19 · 2023: 4
- FWCI
- 7.84
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (200020-185092)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- zinc ions, metalloproteins, protein structure, 3D convolutional neural networks, geometric criterion, protein design, cofactors
- MeSH terms
- Deep Learning, Binding Sites, Ions, Metalloproteins, Metals, Zinc
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