If the mutations were non-synonymous, resulting in different amino acids, the fact that they keep the natural function is still kinda cool. Very much a pure research result AFAICT, but worth a little something.
This is already a well known fact: protein structure (and consequently function) is much more conserved than sequence, mostly due to biophysical constraints.
If non-synonymous mutations do not change the biophysical features of the amino acid residues, then the structure is usually kept. Alternatively, it can be the case that a disruptive mutation is compensated by another one that keeps the structure/function/phenotype. This is the basis for evolutionary coupling based structure prediction methods, such as Alphafold.
It's fairly common for two proteins to have almost identical structures but different (down to 30% or lower sequence identify) and it's also possible to mess up a nice protein that folds easily with a single amino acid change.