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Figure 3
Structural comparison between the ternary complexes of T4dCH and EcTS. (a) Structural superposition of T4dCH (white) and EcTS (cyan). (b) Differences in the THF ligand geometries in the active sites of T4dCH and EcTS. This orientation was obtained from the optimal superposition of T4dCH and EcTS protein as shown in (a). Carbon atoms of THF bound to T4dCH and EcTS are colored white and cyan, respectively. (c) Schematic plot of the interaction between T4dCH and THF. (d) Schematic plot of the interaction between EcTS and THF. The dotted lines and numbers indicate the hydrogen bonds and their distances in Å, respectively. The starburst indicates the hydrophobic interactions. Water molecules are labeled as `w' for clarity. Nitrogen and oxygen atoms are colored blue and red, respectively, for all panels.

IUCrJ
Volume 6| Part 2| March 2019| Pages 206-217
ISSN: 2052-2525
https://doi.org/10.1107/S2052252518018274