Fig. 4. Structural comparison of the DNMT3A^WT–CGT and DNMT3A^R882H–CGT complexes.

a Structural superposition of the DNMT3A^WT–CGT (PDB 5YX2) and DNMT3A^R882H–CGT complexes. b Close-up view of protein–DNA interactions on the RD interface of the DNMT3A^WT–CGT and DNMT3A^R882H–CGT complexes. c Close-up view of the TRD loop and its interactions with CpG guanine (G6) and R882 in the DNMT3A^WT–CGT and DNMT3A^R882H–CGT complexes in expanded view. The hydrogen-bonding interactions are indicated by dashed lines. The conformational shifts of the DNA between the two complexes are validated by the 1.0 sigma Fo–Fo difference map (salmon) between the two complexes and indicated by arrows. d, e Close-up view of the interactions between the TRD loop and DNA in the DNMT3A^WT–CGT (PDB 5YX2) (d) and DNMT3A^R882H–CGT (e) complexes. The Fo–Fc omit map (violet) for the corresponding regions were contoured at 2.0 sigma level.