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Figure 2.
Figure 2: Crystal structures of the FDTS–FAD–dUMP complex.
a, Wild-type TmFDTS (Protein Data Bank 1o26); b, S88A mutant
(Protein Data Bank 3g4a); c, S88C mutant (Protein Data Bank
3g4c). The distance between the C6 carbon of dUMP and the
reducing centre 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 wild-type FDTS, S88A and
S88C, respectively. The electron density maps are 2F[o] - F[c]
with a contour level of 1.0 sigma.
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