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. 2016 Jan 5;6:1479. doi: 10.3389/fmicb.2015.01479

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Copyright © 2016 Park, Mulelu, Sewell and Benedik.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Stereoview of the model of CynD based on the structure of the oxy-nitrilase from Synechocystis sp. PCC6803 (PDB id: 3WUY). The ribbon depicting region 1 is colored red. This region includes three residues that when mutated to cysteine, caused CynD to lose activity: E64, R67, and Y70 (colored purple). It also included seven residues that when mutated to cysteine caused the activity to drop below 50% of the “wt” activity: P55, F57, Y65, T66, F69, H71, and E72 (colored pink). The ribbon depicting region 2 is colored green. It includes two residues that when mutated to cysteine caused the activity to drop below 50% of the “wt” activity: N230 and E235 (colored pink). Residue Q228, mutation of which caused aggregation of the short spirals without loss of activity is colored brown.