We therefore envision that novel small molecules that achieve higher affinity to stabilize these non‐productive conformations might serve as chemical inhibitors for A3B, especially given the remarkable conformational plasticity of the A3B active site as demonstrated by MD simulations here, as well as in our prior studies.28, 29 In this regard, the A3B‐GL7 structures presented may contribute to the future development of potent A3B inhibitors, which we hypothesize will help to control tumor evolution and other mutational processes relevant to human diseases. This evidence concerns the gene APOBEC3B and neoplasm.