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. Author manuscript; available in PMC: 2009 Oct 16.
Published in final edited form as: Nature. 2009 Apr 16;458(7240):919–923. doi: 10.1038/nature07973

Figure 2. Crystal structures of the FDTS-FAD-dUMP complex for: (A) Wild type tmFDTS, (B) S88A mutant, and (C) S88C mutant.

Figure 2

The distance between the C6 carbon of dUMP and the reducing center of the flavin (N5 of FAD) is 3.4 Å for all three enzymes. The distances of the side-chain of residue 88 to C6 are 4.3, 4.5, and 4.1 Å, for wtFDTS, S88A, and S88C, respectively. The electron density maps are 2Fo-Fc with a contour level of 1.0 sigma.