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

<table>Superimposition of subunits A (green) and C (blue) of the mTS-dUMP-Raltitrexed complex structure. Ligands and selected active site residues, which differ conformationally between subunits A and C, are shown as sticks. The Cys189 <i>γ</i>S-dUMP C6 distances of 2.48 Å (subunit A) and 2.78 Å (subunit C) are marked by dashed lines.</table>

BioMed Research International

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Figure 4: Crystal Structure of Mouse Thymidylate Synthase in Tertiary Complex with dUMP and Raltitrexed Reveals N-Terminus Architecture and Two Different Active Site Conformations 

Figure 4 | Crystal Structure of Mouse Thymidylate Synthase in Tertiary Complex with dUMP and Raltitrexed Reveals N-Terminus Architecture and Two Different Active Site Conformations 