compare known protein motifs with a predicted one to find differences at the catalytic site

Question

[SSL]

I tested the activity of a purified motif (SMR) against a mutant versión in one of the two likely catalytic residues. Against my expectations the mutant had a higher activity.

Now, I would like to know if comparing the predicted 3d structure against known structures could provide some insights for the observed results.

Any advice on how to proceed? Some the things that I was considering are:

• is it better to compare against one model or more (if available)
• should I compare both the native version and mutated one (at the same time)
• would the predicted model consider the mutations introduced (3 AA substitutions).

With so many options available it is a bit overwhelming to figure it out where to start thus, any advice would be welcomed.

Thanks