I recently carried out a side directed mutagenisis of protein X. I substituted catalytic His residue with Ala. After modelling the wild and the mutant type protein through bioinformatics, the mutant showed altered active site. Is it possible that a mutation of single catalytic His residue would lead to change in structure of the active site?
given that His is a large AA and Ala is small and also that His is polar and positively charged at ph7 and Ala is non polar then I would expect the shape of the molecule around each AA to be quite different
the information here about amino acids may be useful to you Shoib
http://www.public.iastate.edu/~duahn/teaching/Biomodulation%20and%20Protein/Amino%20Acids%20and%20peptide%20bond.pdf
Does your modeling technique give correct results in similar situations that are confirmed by X-ray structures?
My impression is that modern bioinformatic approaches usually don't give good predictions in such cases apart from obvious effects.
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