Crystal Structure of Mouse Thymidylate Synthase in Tertiary Complex with dUMP and Raltitrexed Reveals N-Terminus Architecture and Two Different Active Site Conformations

<table>2Fo-Fc electron density map at 1.8<i>σ</i> level showing dUMP, Raltitrexed, and catalytic Cys189 in the subunit B. Continuous electron density can be seen between Cys189 <i>γ</i>S and dUMP C6 atoms. The <i>γ</i>S-C6 distance of 2.43 Å is marked by dashed line.</table>

BioMed Research International

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Figure 3: Crystal Structure of Mouse Thymidylate Synthase in Tertiary Complex with dUMP and Raltitrexed Reveals N-Terminus Architecture and Two Different Active Site Conformations 

Figure 3 | Crystal Structure of Mouse Thymidylate Synthase in Tertiary Complex with dUMP and Raltitrexed Reveals N-Terminus Architecture and Two Different Active Site Conformations 