Fig. 3: Detailed view of the active site area.
From: Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site
Panels a–f correspond to the highest resolution (1.29 Å) structure OP, while (g) shows structure MP2. a 2Fo-Fc electron density (contour level 1.50σ) at the Zn coordination sphere. b Hydrogen bonds (black dashed lines) involving residues participating in Zn coordination (thick dotted blue lines); alternative conformations of D187 were visible only in the OP structure. c Overall structure of the ReAV protomer with residues creating the active site in stick representation. d Surface electrostatic potential with the strongest positive charge (blue) visible in the active site area. e 2Fo-Fc electron density (contour level 1.50σ) around Ser48 and the water triad w2-w3-w4. f A detailed map of the most important hydrogen bonds in the active site. g Ser48 observed in two conformations (circled A and B) in structure MP2, where the water triad is absent.
