Table 1. Distance between phosphosites and ATP γ-phosphate in the ternary complexes.
| System | Sp0-Oγ…Pγ-ATP Distance(Å) | B-factor (Sp0-Oγ) (Å2) |
|---|---|---|
| Akt2/GSK3-pept · ANP/MN (crystal structure: 1O6K) | 3.57 | 14.8 |
| Akt2/GSK3-pept · ATP/MG | 3.35 | 13.6 |
| Akt2/LBR-S78 · ATP/MG | 3.65 | 65.8 |
| Akt2/LBR-S80 · ATP/MG | 3.44 | 36.5 |
| Akt2/LBR-S82 · ATP/MG | 3.59 | 44.9 |
| Akt2/LBR-S84 · ATP/MG | 6.63 | 67.9 |
Distance between the hydroxyl oxygen of the corresponding serine residues at p-0 peptide positions (Sp0-Oγ) and the γ-phosphorus atom of ATP (Pγ-ATP), and calculated B-factor values (see “Materials & Methods”) of the Sp0-Oγ atoms, in the final 3D-models of the ATP/MG-bound Akt2/peptide complexes simulated in this study (shown in Fig 7). The equivalent, S9-Oγ…Pγ-ANP distance and crystallographic B-factor in the template crystal structure, are also given for comparison.