Fig. 2: Crystal structures. | Nature Communications

Fig. 2: Crystal structures.

From: Distal mutations enhance catalysis in designed enzymes by facilitating substrate binding and product release

Fig. 2

a The active sites of HG3-Core, HG3-Shell and KE70-Core do not change substantially upon binding of the 6-nitrobenzotriazole transition-state analogue (6NBT, ball-and-stick). In 1A53-Core, a 2-(N-morpholino)ethanesulfonic acid molecule (MES, ball-and-stick) from the crystallization buffer occupies the 6NBT binding site, inducing a conformational change in W110. The 1A53-2.5 crystal structure (PDB ID: 6NW4)27 was used for comparison with 1A53-Core, as 1A53-Evolved was unavailable. We re-refined the KE70-Evolved crystal structure with bound 6NBT (PDB ID: 3Q2D)3 to model missing residues (22–25 in chain A and 3–25 in chain B) into the available density and to flip 6NBT into a productive binding pose. In all cases, only the major conformer of each first-shell active-site residue is shown. b Core variants display active-site configurations in the presence of 6NBT that are nearly identical to those of their Evolved counterparts, while HG3-Shell displays a configuration similar to HG3-Designed.

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