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. 2014 Dec 18;9(12):e115409. doi: 10.1371/journal.pone.0115409

Figure 5. Molecular Docking and Isothermal calorimetry experiments.

Figure 5

(A) Docking modes of l-serine with MtSerB2. l-serine was docked against the binding sites predicted in the ACTI and ACTII domains respectively. Interactions of l-serine with ACTI (top) and ACTII (bottom) domains are shown here. Key interacting residues are labeled in black and shown in stick representation while the rest of the site is shown in cartoon representation. l-serine is depicted in ball- and-stick representation. (B) ITC experiments involving interactions of l-serine with MtSerB2. Titration of l-serine (300 µM) into MtSerB2 solution (30 µM). The experiments were performed in 50 mM sodium phosphate buffer, pH 7.4, and 50 mM NaCl and 2 mM β mercaptoethanol at 25°C. The cell volume was 1.43 ml while the injection volume was 6 µl.