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. Author manuscript; available in PMC: 2015 Mar 1.
Published in final edited form as: FEBS J. 2014 Feb 17;281(6):1613–1628. doi: 10.1111/febs.12727

Figure 5.

Figure 5

Active site and effector binding site in LpcN-II. (A) Active site of GMP-complexed LpcN-II structure (blue) superposed with human BeF3-complexed structure (green, PDB ID 2JCM). Shown also is Motif IV in ribbon format and GMP (shown in CPK color) in the effector site of LpcN-II. BFD52 represents BeF3 covalently linked to D52 in the human structure. Dashed lines that indicate hydrogen bonds are shown only for LpcN-II except for the water-mediated hydrogen bond from Asp356 to Mg2+(green sphere) from the human cN-II structure. Water molecule is shown as red sphere. Mg2+ from the LpcN-II structure is shown as blue sphere. (B) Residues in the activator-binding site that make contact with GMP. GMP is colored in blue for carbon atoms, and residues from the two monomers are colored in green and magenta. Dashed lines indicate hydrogen bonds. (C) The electron density for GMP from omit 2Fo-Fc map seen at 1 σ.