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Structure-based Mutation Analysis

Mapping onto crystal structure


scwrl wt energy?

Hydrogen Bonding network

The following figures show the hydrogen bonds between the wildtype residue and its environment compared to the formation of hydrogen bonds when the corresponding residue is mutated.

Figure 2: Hydrogen Bonds for methionine on pos 82 in the wild type structure
Figure 3: Hydrogen Bonds for leucine on pos 82 in the mutated type structure

Comparing the figures 2 and 3 for the wildtype and the mutated amino acid on position 82, no change in the hydrogen bonding network can be observed. This is due to the similar physiochemical properties of these two amino acids. No atom which could serve as additional hydrogen-bond donor or acceptor was introduced or removed.

Comparison Energies

foldX Energy Comparison

wildtype energy total energy of mutated protein difference
401.00 437.88 36.88


wildtype energy total energy of mutated protein difference
-2485.452755 -4253.174790 -1767.722015


Energy Average Err.Est RMSD Tot-Drift (kJ/mol)
Bond 2518.71 1700 6337.97 -10023.3
Angle 3642.41 270 638.624 -1479.34
Potential 5.16e+06 5.1e+06 7.47e+07 -3.13e+07