The importance of dispersion corrections in geometry optimizations has been shown numerous times, including for organometallic complexes. In our previous work on enzyme benchmarking, we showed some examples of how PBEh-3c structures improved the description of dispersion-supported interactions such as hydrogen bonding and aromatic πstacking, including in the PTE model which we have also included here in the MME55 set. We see similar changes in some of the structures here, and we give two examples in fig. ; see figure caption for dispersion-uncorrected levels of theory of the original structures. For AAP Int1, the optimized structure has the substrate rotated so that the acetyl group can interact with one of the histidine residues. For Co-NHase ES, an off-center parallel π-stacking interaction between the benzonitrile substituent and tyrosine residue is only seen in the optimized structure, not the original structure.