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. 2024 Jan 2;21(2):279–289. doi: 10.1038/s41592-023-02130-4

Fig. 4. The structural modeling results of DMFold on 5,042 difficult targets from the human proteome.

Fig. 4

a, Distributions of pLDDTs for DMFold models versus AlphaFold2 DB models for the subset of 5,042 AlphaFold2 DB models with pLDDT < 0.70. The red dashed line marks the threshold pLDDT = 0.70 for considering a target to be confidently predicted, where DMFold models have a pLDDT ≥ 0.7 in 1,934 cases. b, Head-to-head comparison of the residue-level pLDDTs obtained by DMFold and AlphaFold2 DB for the 1,934 confidently DMFold-modeled proteins, which involve in total 878,094 residues. c, Structural models generated for a putative uncharacterized protein FLJ45035 (Q6ZQT0) by AlphaFold2 DB (yellow) and DMFold (blue), respectively. d, Residue-level pLDDT curves of AlphaFold2 DB (yellow) and DMFold (blue) for Q6ZQT0. e, Structural models generated for a putative diacylglycerol O-acyltransferase 2-like protein (Q6IED9) by AlphaFold2 DB (yellow) and DMFold (blue), respectively, where two better-formed β-sheet secondary structures created by DMFold are highlighted by red. f, Residue-level pLDDT curves of AlphaFold2 DB (yellow) and DMFold (blue) for Q6IED9, where the pLDDTs associated with the four β-strands are highlighted with red backgrounds.

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