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Figure 8
Potential product inhibition of Nt-FDH. Comparison of the overall structure of the apo (green) and THF-complexed (blue) forms: the THF molecules are shown in ball-and-stick representation and the Tyr200 residue of the apo form and the THF complex form are shown in stick representation. In a close-up view of the active site, the additional bound THF occupies a position that interferes with Tyr200 if the orientation of the aromatic group is not altered from that in the native structure or that of the substrate (10-FDDF) complex.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 71| Part 4| April 2015| Pages 1006-1021
https://doi.org/10.1107/S1399004715002928
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