X-ray diffraction data of human PARP15 catalytic domain in complex with benzamide adenine dinucleotide (BAD)

The catalytic domain of human PARP15 was crystallised in apo-form, and the crystals were soaked with benzamide adenine dinucleotide (BAD), a nonhydrolysable analogue of the substrate NAD⁺. This yielded a complex structure representing the binding mode of NAD⁺ in the catalytic site. This is supporting data to a broader work showing that PARP15 forms a homodimer and that the homodimer is its active form, dimerisation being required for NAD⁺ binding and thus activity.