Figure 1 | Scientific Reports

Figure 1

From: Structure-based identification of a potential non-catalytic binding site for rational drug design in the fructose 1,6-biphosphate aldolase from Giardia lamblia

Figure 1

Structural analysis of GlFBPA according to the described method. (A) Overall view of D105; G175 and D278 on the structure of GlFBPA. Each subunit of the dimer is shown in green and blue. Selected residues are shown as space-filling models and signaled by arrows. The active site is pointed out by the presence of F1,6P, which is shown as a purple space filling model. (B) Close-up view of the interfacial salt bridge network formed by D278 and R280 of one subunit and D255 and R259 of the adjacent monomer. (C) Active site residues of GlFBPA; amino acids are shown in stick models and F1,6P as a ball and stick model (FBP), zinc ions are purple balls; key electrostatic interactions between the protein and the substrate are shown as red-dashed lines. (D) Surface model of the binding site region: residues selected by the described method are pointed by yellow arrows, whereas amino acids lining the crevice in which this are positioned are signaled by white arrows.

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