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. 2015 Apr 1;16(4):7304–7319. doi: 10.3390/ijms16047304

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

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Active site crystal structure of the wild type (WT) ecTSase (green; PDB ID 2KCE) with 2'-deoxyuridine-5'-mono-phosphate (dUMP) (gray) and CH₂H₄folate analog, Raltitrexed (magenta). Tyr209 is shown in cyan. H-bond between 3'-OH of the dUMP and Tyr209 is shown in dashed lines. TSase chain is shown in cartoon representation (green). Residue Y209, the ligands dUMP and the cofactor analog, raltitrexed and the thio-ether bond between C-6 of dUMP and the C146 are in sticks. Color code for Y209: cyan (carbons), red (oxygen); Color code for dUMP: blue (nitrogen), grey (carbon), red (oxygen), orange (phosphorous); Color code for raltitrexed: blue (nitrogen), magenta (carbon), yellow (sulfur), red (oxygen), and the atoms in the thio-ether bond are shown in yellow.