Extended Data Fig. 7: Structure of human OMPDC in complex with transition-state analog BMP. | Nature Catalysis

Extended Data Fig. 7: Structure of human OMPDC in complex with transition-state analog BMP.

From: Ground-state destabilization by electrostatic repulsion is not a driving force in orotidine-5′-monophosphate decarboxylase catalysis

Extended Data Fig. 7

Structure of human OMPDC in complex with transition-state analog BMP. Close-up of the active site showing the local interactions of residue Asp317’. The structural model is superposed with the corresponding 2mFo-DFc electron density map (blue, contour level 5.3σ). Peaks in the H-omit mFo-DFc difference electron density map (magenta, contour level 3σ) indicate the positions of hydrogen atoms of the analog and interacting protein groups. The structural data suggest that the side chain Asp317’ is ionized and interacts with Lys314 (-NH3+), the backbone amide of Ile318’ and the 2’-OH group of BMP. Crystallographic statistics are provided in Supplementary Table 1. Abbreviations: OMPDC, orotidine-5’-monophosphate decarboxylase; BMP, 6-hydroxy-UMP.

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