Table 2 List of Hydrogen bonds between protein and substrates and conservation in MltA
From: Structure of the stationary phase survival protein YuiC from B.subtilis
Sugar Site | Ligand Atom | +NAG (4wjt) | +Anhydro (4wlk) | MltA (2pi8) | Conserved YuiC vs MltA |
|---|---|---|---|---|---|
−2 | O1 | Thr152 O via HOH A550 | None | (O4 of −1) Gln162 O | No. Thr100 YuiC is closest to MltA Gln162 |
−2 | O3 | Leu111 O | Leu111 O | None | No |
−2 | O3 | Lys102 NZ | Lys102 NZ |  | No |
−2 | O4 | HOH A430/435 | None | None |  |
−2 | O5 | Thr100 O via HOH A531 | HOH416 is too far (3.7 Å) | None |  |
−2 | O6 | Ser154 N and OG via HOH 539 | None | None |  |
−2 | O7 | Lys102 NZ | Lys102 NZ |  |  |
−2 | O7 | Gly110 N and Ala 95 O via HOH A489 | Gly110 N and Ala 95 O via HOH A428 | Ser164 OG | No. HOH 428 and Ser164 OG are close |
−2 | N2 | Asp151 OD1 and OD2 | Asp151 OD1 and OD2 | Asp297 OD2 | Yes. Asp151/297 |
−1 | O1 |  | Asp162 OD2 | (O4 of +1) none but Asp308 mutated to Ala | Yes. Asp162/308 |
−1 | O3 |  | None | None |  |
−1 | O5 |  | None | None |  |
−1 | O6 |  |  | Val298 O |  |
−1 | O7 |  | Ser 154 N and OG Ala 155 N | Gly300 N and Ala 301 N via HOH A1045 | Yes, but contact longer via water in MltA |
−1 | N2 |  | Ser99 O | Val161 O | No. Close in space but not conserved |