The nuclear localization signal of Uprosertib (GSK2141795) kanadaptin is located immediately downstream from the dsRBD. This domain architecture suggests that the nuclear protein kanadaptin might be involved in binding nucleic acids with its FHA domain serving as a regulatory module. Orthologs of kanadaptin are widely distributed in eukaryotes, from single-cell organisms such as Capsaspora owczarzaki and Monosiga brevicollis, to multicellular organisms such as Caenorhabditis elegans and humans, all of which contain a highly conserved FHA domain. To gain insights into the function of human kanadaptin, we determined the crystal structure of its FHA resolution using the JCSG high-throughput structural biology pipeline with protein expressed in the Protein Production Facility, Novo Nordisk Foundation Center for Protein Research, University of Copenhagen. The structure confirms the presence of a canonical pThr recognition site. Furthermore, a phosphopeptide mimic bound complex and a new dimer arrangement compared to other FHA dimers were observed in the crystal lattice, suggesting phosphopeptide binding dependent dimerization as a possible mechanism of kanadaptin activation. The FHA domain of kanadaptin was cloned and expressed in Escherichia coli with a TEV protease-cleavable expression and purification tag, and was purified by metal affinity and size exclusion chromatography. The purification tag was removed prior to crystallization, leaving two extra residues not present in the native protein sequence. The FHA domain of kanadaptin was crystallized using the nanodroplet vapor diffusion method with standard JCSG crystallization protocols. The structure was determined by molecular replacement in orthorhombic space group P212121 using the FHA domain of Pml1p subunit of the yeast precursor mRNA retention and Tiotropium Bromide splicing complex as a phasing model, and refined to an Rcryst of 17.6% and an Rfree of 19.8%. The final model has good geometry and compares favorably to other structures at similar resolution, with an overall MolProbity score of 1.2 that ranks in the 99% percentile.