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. Author manuscript; available in PMC: 2016 Feb 3.
Published in final edited form as: Structure. 2015 Jan 22;23(2):332–341. doi: 10.1016/j.str.2014.10.025

Figure 6. Comparison between Substrate Recognition of NatD and NatA.

Figure 6

(A) Overlay of the peptide binding site of NatA (orange) and NatD (cyan with magenta histone substrate).

(B) Electrostatic potential surface of the NatA active site with a bound covalently linked bisubstrate inhibitor. The N-terminal serine of the substrate peptide is shown in orange, and the acetyl-CoA moiety of the bisubstrate inhibitor is in white.

(C) Electrostatic potential surface of the NatD active site. The N-terminal serine of the substrate peptide is shown in magenta, and acetyl-CoA is in orange. Waters are shown as red spheres. Acetyl-CoA was modeled into the figure by aligning the binary and ternary NatD structures.