A quantifiable fraction of human proteins have experimentally solved 3D structures.
A quantifiable fraction of human proteins possess experimentally solved 3D structures, forming a substantial baseline of structural coverage that has recently been complemented by high-accuracy computational predictions.
The claim states that a quantifiable fraction of human proteins have experimentally solved 3D structures. This is specific, empirical, and verifiable. The retrieved literature clearly supports this, noting that historical experimental and template-based methods covered a significant portion of the human proteome (e.g., around 48% as a baseline before AlphaFold) and thousands of experimental structures are actively curated in the Protein Data Bank. Therefore, the claim is supported.
Sirawit Ittisoponpisan, S. Islam, Tarun Khanna, Eman Alhuzimi, A. David, M. Sternberg. Can Predicted Protein 3D Structures Provide Reliable Insights into whether Missense Variants Are Disease Associated?. 2019. https://doi.org/10.1016/j.jmb.2019.04.009
Paper 0 notes that baseline experimental structural coverage accounts for a substantial fraction of the human proteome before adding homology predictions.
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Eduard Porta-Pardo, Victoria Ruiz-Serra, Samuel Valentini, Alfonso Valencia. The structural coverage of the human proteome before and after AlphaFold. 2021. https://doi.org/10.1101/2021.08.03.454980
Paper 5 reports that the baseline structural coverage of the human proteome from experimentally derived or template-based models was already at 48% prior to the inclusion of AlphaFold predictions.
Yuhe Liang, Christine Zardecki. RCSB Protein Data Bank (PDB): Driving Research and Education Using Experimentally-Determined Structures and Computed Structure Models from Artificial Intelligence/Machine Learning. 2025. https://doi.org/10.1063/4.0000914
Paper 7 details how the RCSB Protein Data Bank houses hundreds of thousands of experimentally determined 3D macromolecular structures alongside computed models.
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