The 1.4-Å-resolution structure of the dPC chromodomain (amino acids 23–77) in complex with a histone H3 peptide (amino acids 19–33) containing K27me3 demonstrated that dPC chromodomain consists of three B-strands (B1– B3) forming a twisted antiparallel B-sheet . A helix (aA) located at the C-terminal end is packed against one edge of the B-sheet next to B1. Helices, sheets and H3K27me3 peptide are colored in magenta, lightcoral and cyan, respectively.