PWWP2A is a multivalent gene regulatory protein involved in recognition of a variety of histone code elements including histone methylation and the histone variant H2A.Z. While PWWP2A's function at the biochemical level is largely unknown, it is known to be important in cell proliferation and mitosis. Furthermore it is observed to eb found at promoter regions and transcriptional start sites around highly transcribed genes. PWWP2A not only has nucleosome binding elements, but it also forms interactions with subunits from a NuRD nucleosome remodelling complex namely MTA1 and the histone deacetylase, HDAC1. Here we characterise a previously undiscovered domain on the N-terminus of PWWP2A which were identified through alphafold 3 modelling of the protein. The domain is a 50 amino acid beta-sheet which forms a symmetric beta-barrel. Dimerisation of this domain may facilitate the interaction of PWWP2A with NuRD subunits to form a deacetylase complex. This shows another novel use of alphafold in generating hypotheses for structural biology research.