As you stated, you have multiple protomers in the asymmetric unit, where they
are free from
crystallographic symmetry constraints. Generally that means different local
environment for
each protomer. Inspecting the sites in the different protomers (frequently
related by various
Hey,
That is a good question, and there could be multiple reasons. One
possibility could be the crystal contacts. I have experience with the
pentameric vial surface protein (PMID: 24648448), and I could see the
carbohydrate ligand only in a subset of protein chains in ASU.
Another reason could
Perhaps the subunits have different conformational states that are differently
able to bind the ligand. There are definitely oligomers where the subunits do
that e.g. mGluR1 binding domain dimer is usually 1 open subunit and 1 closed in
the active state without cations at the interface. This is
Hello all,
In homo-dimeric or homo-oligomeric protein crystal structures, what would be
the reason for having a ligand (chemical compound or fragment) binds to one
molecule and not all molecules in the asymmetric unit?
I have soaked a fragment that has an affinity of 200 uM to a viral protein