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Figure 4
Crystal structure of the 14-3-3σ–Sirt3pS103 complex. (a) Content of the asymmetric unit showing a 14-3-3σ monomer with bound Sirt3 peptide. The normal physiological 14-3-3 dimer is formed by a symmetry-related molecule (see Supplementary Fig. S1). (b) Sirt3 peptide binding site with hydrogen-bonding network. (c) OMIT (by omitting Sirt3 peptide atoms) electron densities of the Sirt3 peptide contoured at 2σ (green) and at 4σ (magenta). (d, e) Structure superposition of Sirt3 peptide with (d) 14-3-3 binding mode 1 (PDB entry 1qjb) and (e) mode 2 (PDB entry 1qja) peptides by fitting the pSer residue using the Coot `superpose ligand' function. C-atom coloring: Sirt3, peptide yellow; mode 1 peptide, green; mode 2 peptide, orange.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 82| Part 1| January 2026| Pages 32-40
https://doi.org/10.1107/S2053230X25010908
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