AlphaFold Protein Structure Database and 3D-Beacons: New Data and Capabilities

Jennifer Fleming, Paulyna Magaña, Sreenath Sasidharan Nair, Maxim I. Tsenkov, Damian Bertoni, Ivanna Pidruchna, Marcelo Querino Lima Afonso, Adam Midlik, Urmila Paramval, Augustin Žídek, Agata Laydon, Oleg V. Kovalevskiy, Elisa Wong, Joshua Pan, Jun Cheng, Žiga Avsec, Clare Bycroft, Lai Hong Won, Meera Last, Milot Mirdita, Martin Steinegger, Mihály Váradi, Pushmeet Kohli, Sameer Velnankar

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Abstract

The AlphaFold Protein Structure Database (https://alphafold.ebi.ac.uk/) has made significant strides in enhancing its utility and accessibility for the life science research community. The recent integration of AlphaMissense predictions enables access to the pathogenicity of human protein missense variants, with an innovative and interactive heatmap and 3D visualisation that display variant data at the residue level. Users can now toggle between structure model quality (pLDDT) and average pathogenicity scores, providing insights into the implications of specific residue changes. The Foldseek integration offers a rapid and accurate method for protein structure searches and comparisons. Bulk data download options further facilitate comprehensive data analysis and integration with other computational tools. The 3D-Beacons framework (https://www.ebi.ac.uk/pdbe/pdbe-kb/3dbeacons/) has also been enhanced with detailed annotation endpoints (such as AlphaMissense data) and integrates LevyLab’s dataset of homomeric AlphaFold 2 models. These advancements, plus the release of the training module "AlphaFold: A Practical Guide", significantly improve the functionality and accessibility of these resources, enabling discoveries using structure data.

Abstract of "AlphaFold Protein Structure Database and 3D-Beacons: New Data and Capabilities" by Jennifer Fleming, Paulyna Magaña, Sreenath Sasidharan Nair et al., https://doi.org/10.1016/j.jmb.2025.168967, used under its Creative Commons Attribution license (CC-BY); markup removed, otherwise unmodified.

Record

Archive ID
doi:10.1016/j.jmb.2025.168967
Published
Jan 29, 2025
Venue
Journal of Molecular Biology
DOI
10.1016/j.jmb.2025.168967
PubMed
40133787
Categories
Protein Structure and Dynamics
License
cc-by
Provenance
openalex+europepmc

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