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. 2017 May 3;8:14959. doi: 10.1038/ncomms14959

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(a) Structure of apo hEXOG. Each monomer has a Core (green) and a Wing domain (grey); residues involved in domain swapping are shown in CPK. (b) Structure of Drosophila EndoG (dmEndoG) with N-terminal residues shown in CPK. (c) Electrostatic surface of apo hEXOG. (d) Sequence alignment of hEXOG, hEndoG and dmEndoG.