structural analysis of mvdac1's structure showed a barrel-like channel composed of 19 amphipathic β-strands, with the n-terminus and c-terminus both facing towards the inter membrane space of the mitochondrion. β-strands are connected via loops and are arranged in an anti-parallel pattern with the exception of β-strands 1 and 19 which are parallel. the pore has a height of 40 ẳ, spans a distance of 27 ẳ by 20 ẳ at the openings and tapers down to 20 ẳ by 14 ẳ at the n-terminal α-helix segment in the open state. the closed state conformation has yet to be isolated and determined. additionally, the n-terminus has an alpha helical segment that is held to the inside wall of the pore by hydrophobic interactions with residues on β-sheets 8-18. this n-terminus can serve as a scaffold for the movement of ions or attachment of proteins. one such example is seen as it is the docking site for hk1 binding. a significant residue to point out is the glutamate located at the 73rd residue on the amino acid chain (e73). this residue is found in vdac1 and vdac2 but not vdac3. the side chain of this charged residue points into the phospholipid bilayer which would normally cause repulsive forces to occur. e73 however, has been implicated in vdac1 function and interaction.