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. Author manuscript; available in PMC: 2016 Dec 14.
Published in final edited form as: Phys Chem Chem Phys. 2015 Dec 14;17(46):30867–30875. doi: 10.1039/c5cp01246e

Figure 5.

Figure 5

The network of H-bonds in TSase Active Site: Structure of wild-type ecTSase (PDB ID 1TLS) covalently bound to FdUMP-CH2H4folate (a mimic of the state prior to the proton abstraction) showing several relevant active site residues and water molecules. Potential H-bonds are marked by dashed line. Also marked are N5 of CH2H4folate, O4 carbonyl of dUMP, and the H-donor (C5 of dUMP). The fluorine atom is removed from C5 for clarity.