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Figure 3 | BMC Structural Biology

Figure 3

From: Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC

Figure 3

Comparison of the MnmC2 active sites between ecMnmC and ypMnmC. Amino acid residues from ecMnmC are displayed in light green, where those from ypMnmC are in orange. Note that all displayed residues are conserved in both proteins except for Phe-24, which is disordered in the ypMnmC structure. EcMnmC bound SAM is colored as light grey (carbon), blue (nitrogen), red (oxygen), and yellow (sulfur), whereas ypMnmC bound SAM is presented in an identical color scheme except for pink (carbon). Hydrogen bonding interactions are shown as black dashes in both structures, where H-bond distances are shown in Å and labeled in blue or black for ecMnmC, or ypMnmC, respectively.

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