Structure predictions have become invaluable tools for wet lab science by accelerating the generation of structure-based hypotheses. While AlphaFold-predicted structures are available for most proteins, viral proteins are currently absent from the EMBL/DeepMind AlphaFold database. Here, we provide proteome-wide structure predictions for all nine human herpesviruses and analyze them in depth. All predictions were scored using explicit thresholds. By clustering these predictions into groups with structural similarity, we identified new families, such as the HCMV UL112-113 cluster, that contain a unique beta-barrel conserved in all alpha- and betaherpesviruses. An exhaustive domain-level search found protein families consisting of subgroups with varying numbers of duplicated folds. Using large-scale searches, we identified viral proteins with cellular folds and potential functions, such as the HSV-1 and HSV-2 US2 proteins possessing dihydrofolate reductase folds or the EBV BMRF2 cluster of proteins that might have emerged from cellular equilibrative nucleoside transporters. Our HerpesFolds database can be accessed through an easy-to-use web interface atwww.bosse-lab.org/herpesfolds/. It displays 3D models of all protein predictions with their quality scores and structural clusters through an interactive, searchable, open-access web interface.