Table 3 Effect of Mutations on Protein Stability and Interactions with Ligand, Nucleic acid and Other Protein Subunits.
From: Structural Implications of Mutations Conferring Rifampin Resistance in Mycobacterium leprae
Impact of Mutations on Protein Stability and Ligand Interaction (ΔΔG in kcal/mol) * | ||||
|---|---|---|---|---|
Prediction Tools | D441Y | D441V | S437L | H476R |
mCSM | 0.042 | 1.513 | −0.031 | −0.933 |
mCSM-lig | −0.147 | −0.204 | −0.268 | −0.516 |
mCSM-NA | 5.990 | 0.345 | −3.55 | −1.008 |
mCSM-PPI | −0.294 | 0.155 | −0.555 | −1.171 |
DUET | 0.002 | 1.597 | 0.190 | −0.956 |
SDM2 | −0.710 | 0.330 | 1.280 | −1.870 |
ENCoM & FoldX4** | 2.020 | 1.210 | 1.880 | 2.110 |
Interface Residue | No | No | No | Yes |
Distance from the Interface | 7.080 Å | 7.080 Å | 7.090 Å | 3.550 Å |
Distance from the Ligand | 3.435 Å | 3.435 Å | 4.000 Å | 16.745 Å |
Distance from the Nucleic Acids | 7.082 Å | 7.082 Å | 12.344 Å | 8.624 Å |
