Table 4.
Summary of docking poses for NAD+ binding to ALDH isozymes.
| ALDH2 | ALDH1B1*1 | ALDH1B1*2 | ALDH1B1*3 | ALDH1B1*5 | |
|---|---|---|---|---|---|
| Interaction Energy (kcal / mol) | |||||
| Total | −201.0 | −189.9 | −182.5 | −210.7 | −234.2 |
| Electrical | −156.1 | −132.5 | −129.7 | −160.2 | −189.8 |
| Van der Waals | −44.9 | −57.4 | −52.8 | −50.5 | −44.4 |
| Dist to substrate1 (Å) | 5.4 | 4.4 | 16.9 | 4.1 | 12.0 |
| H-bonds2 | 5(8) | 5(5) | 4(4) | 5(6) | 5(6) |
| LEU286 | LEU286 | LEU286 | |||
| GLU416 | GLU416x3 | GLU416 | GLU416 | GLU416 | |
| TRP185 | TRP185 | TRP185 | TRP185 | ||
| SER263 | SER263x2 | SER263 | SER263x2 | SER263 | |
| GLU212 | GLU212 | GLU212 | GLU212 | GLU212 | GLU212x2 |
| LYS209 | LYS209 | LYS209 | LYS209 | ||
| ILE183 | ILE183 | ILE183 | ILE183 | ||
1
Distance between the carbonyl oxygen of the docked propionaldehyde and the nicotinamide ring of NAD+
2
Number of unique hydrogen bonds to each amino acid with total hydrogen bonds in parentheses. Only interactions described for ALDH2 in Steinmetz et al. 1997 are shown. Where multiple interactions to the same amino acid was measured, ×2 or ×3 is indicated.