Table 5.
Hydrogen bond distances (Å) between protein and ligands (dUMP, CB3717) in complexes of wild-type TS and the Tyr-261 variants Met, Phe, Ala, and Trp
| DUMP atom | Protein atoma | Wt Lc | M | F | A | W | Wt Ec | Ec W |
|---|---|---|---|---|---|---|---|---|
| O1P | R218Nη2 | 2.9 | 3.0 | 2.8 | 2.8 | 2.7 | 2.8 | 2.7 |
| R179Nε | 2.9 | 2.8 | 2.9 | 2.8 | 2.9 | 2.9 | 2.9 | |
| R179Nη2 | 3.0 | 2.9 | 3.1 | 2.9 | 2.9 | 2.8 | 2.9 | |
| O2P | S219Oγ | 2.8 | 3.1 | 2.7 | 3.0 | 3.0 | 2.7 | 2.7 |
| R218Nη1 | 2.8 | 2.7 | 3.1 | 3.1 | 2.8 | 2.8 | 2.8 | |
| R178Nε | 3.3 | 3.4 | 3.3 | 3.3 | 3.2 | 2.9 | 2.9 | |
| O3P | R23Nε | 3.0 | 2.6 | 2.8 | 3.4 | 2.7 | 2.8 | 2.7 |
| R178Nη2 | 3.0 | 3.1 | 3.3 | — | 3.3 | 2.9 | 2.9 | |
| Wat8 | 2.9 | 2.4 | 2.5 | 2.5 | — | 2.8 | 2.8 | |
| O5′ | R23Nη2 | 3.0 | 3.1 | 2.9 | 2.9 | 2.8 | 2.9 | 3.1 |
| R178Nη2 | 3.2 | 3.4 | 3.5 | 3.6 | 3.2 | 3.4 | 3.5 | |
| O3′ | H259Nε2 | 2. 9 | 2.6 | 2.7 | 3.1 | 2.7 | 2.7 | 2.8 |
| Y261Oη | 2.8 | — | — | — | — | 2.7 | — | |
| W261Nε1 | — | — | — | — | — | — | 3.2 | |
| O4 | N229Nδ2 | 2.9 | 2.9 | 2.5 | 2.5 | 2.6 | 3.0 | 3.0 |
| WAT1 | 3.2 | 3.1 | 3.1 | 3.7 | 3.2 | 3.0 | 3.0 | |
| H199Cδ2 | 3.0 | 2.8 | 3.3 | 3.3 | 3.2 | 3.2 | 3.2 | |
| O2 | D221N | 2.8 | 2.8 | 2.6 | 2.6 | 2.5 | 3.0 | 3.0 |
| N3 | N229Oδ1 | 3.1 | 2.9 | 2.9 | 3.0 | 2.9 | 3.0 | 3.0 |
| CB3717 | ||||||||
| N1 | WAT2 | 2.9 | 2.9 | |||||
| NA2 | A315O | 3.0 | 3.0 | |||||
| NA2 | WAT3 | 3.1 | 3.3 | |||||
| N3 | D221Oδ2 | 2.7 | 2.7 | |||||
a
LcTS numbering; LcTS residue numbers, m, can be converted to EcTS residue numbers, n, by n=m-2, for m less than or equal to 89, and n=m-52 for m greater than 89.