Fig. 3: AetD catalytic activity and complex structures of L-Trp with various degrees of bromination. | Nature Communications

Fig. 3: AetD catalytic activity and complex structures of L-Trp with various degrees of bromination.

From: The structural and functional investigation into an unusual nitrile synthase

Fig. 3

a The representative HPLC chromatograms of reactions containing three substrates in the presence (red traces) or absence of AetD (black traces). b The enzyme-substrate interaction networks of AetD complexes. The bound substrates, interacting residues, Fe ions, and water molecules are displayed as described in Fig. 2c. All residues that constitute the binding pocket of 1 as shown in Fig. 2c are displayed, with those distant from the bound ligands colored in gray (>5 Å, F221 and I41 in AetD/3/Fe). The dashed lines indicate distance <3.5 Å. The 2Fo-Fc and Fo-Fc maps of 1, Fe ions, and the coordinating waters and residues are shown in Supplementary Fig. 7.

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