In this work, we perform a systematic study of five different Zn(II) coordination shells, that include all histidine and/or aspartic/glutamic acid combinations. Relative stabilities of the different coordination shell arrange- ments and relative stabilities of the different coordination shell geometries, where tetrahedral and octahedral coordinations are studied, have been calculated both in the gas phase and the aqueous phase. In order to gain more insights into the contributing factors of the preferred coordination shell arrangements, we have used various state-of-the-art methods. Our results indicate that tetrahedral geometries are favored over octahedral geometries in the solvent phase, and that a mixture of histidine and aspartic/glutamic acid is preferred in the coordination shell. Multiple structures deposited in the Protein Data Bank support our findings which suggest that our trends are not exclusive to Aβ-Zn(II) systems but to all Zn(II) metalloproteins where coordination is given in these unique residue arrangements.