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. Author manuscript; available in PMC: 2024 Apr 19.
Published in final edited form as: Arch Biochem Biophys. 2020 Dec 10;698:108716. doi: 10.1016/j.abb.2020.108716

Figure 4.

Figure 4.

Comparision of histone H3 peptides 1-RKS(PO3H2), and 4-AAS(PO3H2), (PDB file 1kx5, Python, chain; ribbon). A) Phosphoserine-10 (red/orange), creates a salt bridge with arginine-8 (blue/white). The salt-bridge is denoted by dashed lines and by the the proximity of the atoms (1.92 Å and 2.07 Å , respectively). B) In the absence of positively charged arginine-8 and lysine-9, phosphoserine-10 (red/orange), maintains or creates interactions with other atoms. These include the threonine-11 residue, other lysine residues, and backbone amide protons found both nearby and more distant to phosphoserine-10.