Hi All,

I am working on a bifunctional enzyme with these two hypothesized features:

- it is first autocatalytically cleaved to form a heterodimer;

- it then forms a homotetramer of heterodimers.

These two events would lead to a protein assembly with 2 active sites for catalytic activity A and 1 active site for catalytic activity B.

I have two questions:

1. I have modelled the initial heterodimer by "cleaving" the preprotein at the predicted autocatalytic cleavage site and feeding the resulting two aa sequences to the AlphaFold Server. Is there a better way to predict heterodimerization of such proteins using AlphaFold?

2. Is there a way to tetramerize the resulting AlphaFold heterodimer from 1. in ChimeraX?

Jernej