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. 2016 Jul 20;7:12196. doi: 10.1038/ncomms12196

Figure 1. Structural overview of ASMase.

Figure 1

(a) Domain organization of ASMase. SP, signal peptide; PL, proline-rich linker. (b) Closed and open ASMase coloured as in a. Consecutive grey spheres indicate the disordered linker between closed ASMasesap and ASMasecat in one molecule of the asymmetric unit. Boxed region magnified in c is not in the identical orientation. Glycans are omitted for clarity. Zincs are indicated as purple spheres. (c) ASMase active site. Zinc interactions are shown as dashes. Zinc–zinc distance=3.6 Å. Zinc–ligand distances range from 2.0 to 2.1 Å. Phosphate is coloured orange and red. Shown are zinc-interacting residues (beige) and residues important for leaving group protonation and substrate binding (green).