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

Figure 6

Superimposition of the crystal structures of mTS-dUMP (green) and mTS-dUMP-Raltitrexed (violet) complexes. Side chains of selected, mostly hydrophobic, amino acid residues located between the N-terminus and active site are shown as sticks and ligands, dUMP and Raltitrexed, as ball and sticks. N-terminal amino acids in the tertiary complex have no equivalents in the binary complex, as this part was disordered in the latter structure.