Figure 3 | Scientific Reports

Figure 3

From: Structural and Mechanistic Analysis of Drosophila melanogaster Agmatine N-Acetyltransferase, an Enzyme that Catalyzes the Formation of N-Acetylagmatine

Figure 3

Comparison of the surface electrostatic potential of D. melanogaster AgmNAT to that of D. melanogaster AANATA and human SSAT. (A) AgmNAT (PDB code 5K9N). (B) D. melanogaster AANATA (PDB code 3TE4). (C) Human SSAT (PDB code 2JEV). (D) Close up of AgmNAT active site oriented to show the entry point for acetyl-CoA. (E) Close up of D. melanogaster AANATA active site with acetyl-CoA bound and oriented to show the entry point for acetyl-CoA. (F) Close up of the human SSAT active site with the bisubstrate inhibitor N 1-spermine-acetyl-CoA bound and oriented to show the entry point for acetyl-CoA. Blue is for positive charges and red is for negative charges. Surface electrostatic potentials reveal that the amine binding pocket for AgmNAT and SSAT are more negatively charged than the arylalkylamine binding pocket of AANATA.

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