Fig. 5

Structural analysis of Ami1_Di and Ami2_Di showing zinc binding and active site motifs. (A) Cartoon representation of Ami1_Di, colored based on secondary structure (helix, sheet, and loop are shown in red, yellow, and green, respectively). (B) Close-up on the conserved active site motif of Ami1_Di. The motifs are represented as sticks, where nitrogen and oxygen are shown in blue and red, respectively. (C) Close-up on the equivalent residue for zinc binding sites of Ami1_Di. The zinc and surrounding helix and sheets are shown in green and bright orange, respectively. The chelating residues are represented as sticks (nitrogen and oxygen are shown in blue and red, respectively). (D) Cartoon representation of Ami2_Di, colored based on secondary structure (helix, sheet, and loop are shown in red, yellow, and green, respectively). (E) Close-up on the conserved active site motif of Ami2_Di. The motifs are represented as sticks, where nitrogen and oxygen are shown in blue and red, respectively. (F) Close-up on the equivalent residue for zinc binding sites of Ami2_Di. The zinc and surrounding helix and sheets are shown in green and bright orange, respectively. The chelating residues are represented as sticks (nitrogen and oxygen are shown in blue and red, respectively)