Figure 1 | Scientific Reports

Figure 1

From: Structure of Chorismate Mutase-like Domain of DAHPS from Bacillus subtilis Complexed with Novel Inhibitor Reveals Conformational Plasticity of Active Site

Figure 1

Overall structure, active site and ligand interactions. Panel (A) shows the overall structure of BsCM_2 complexed with chlorogenic acid. In the zoom panel, 2F0-Fc map of chlorogenic acid at active site S1 contoured at one sigma. In panel (B), the active site is formed by residues contributing from both the chains of physiological dimer. The polar residues at the active site are highly conserved in all CM_2 or CM-like domains. However, hydrophobic acid residues are not conserved. Panel (C) shows the interaction of chlorogenic acid with the active site residues in BsCM_2-CGA structure. Panel (D) shows the interaction of citrate with the active site residues in the BsCM_2-CIT structure. Residues from different chains are colored accordingly.

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