Comparison between VSP1 and P4 in active sites and dimer patterns.

(A) Residues in the catalytic site of VSP1. Magnesium ions and water molecules are colored by green and red, respectively. (B) Residues in the catalytic site of P4. Magnesium ion and water molecules are colored by green and red, respectively. (C) Hydrophobic core between two VSP1 monomers. Two VSP1 monomers are colored magenta and cyan, respectively. (D) Hydrogen bonds between two VSP1 monomers. Two VSP1 monomers are colored magenta and cyan, respectively. (E) Interaction pattern of VSP1 dimer. One monomer is coloured magenta, while the N-terminal helices of the other monomer are coloured cyan. (F) Interaction pattern of P4 dimer. One monomer is colored yellow, while the N-terminal helices of the other monomer are colored green. The magenta VSP1 monomer in (E) and the yellow P4 monomer in (F) are aligned.