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. 2007 Nov 30;374(3):749–763. doi: 10.1016/j.jmb.2007.09.055

Fig. 4.

Fig. 4

The UDP-binding pockets are shown for (a) His6-WbmF, soaked with UDP and (b) the His6-WbmG, UDP co-crystal. Spheres represent atoms within 3.5 Å of the bound UDP; NAD indicates the nicotinamide ring of the NAD cofactor. (c) dTDP-glucose bound in the active site of a D128N, E129Q mutant of dTDP-glucose 4,6-dehydratase DesIV from S. venezuelae (PDB ID 1R6D).23 The substrate-binding pockets are all shown from the same angle to enable comparison of the relative positions of the UDP diphosphates in (a) and (b) with the phosphates in dTDP-glucose in (c).