Classical zinc fingers (ZFs) are one of the most abundant and best characterized DNA-binding domains. Typically, tandem arrays of three or more ZFs bind DNA target sequences with high affinity and specificity, and the mode of DNA recognition is sufficiently well understood that tailor-made ZF-based DNA-binding proteins can be engineered. We have shown previously that a two-zinc-finger unit found in the transcriptional coregulator ZNF217 recognizes DNA but with lower affinity and specificity. To investigate the basis for these differences, we determined the structure of a ZNF217-DNA complex. We show that, although the overall position of the ZFs on the DNA closely resembles that observed for other ZFs, the sidechain interaction pattern differs substantially from the canonical model. The structure also reveals the presence of two methyl-pi interactions, each featuring a tyrosine contacting a thymine methyl group. To our knowledge, interactions of this type have not previously been observed in protein-DNA complexes. Finally, we interrogated the sequence-specificity of this two-ZF unit and discuss how ZNF217 might discriminate its target DNA sites in the cell.