ATP binds to the A subunits and it is then hydrolyzed to power the alternation, but the exact

process by which this happens is not known. The four domains can be present in four
separate polypeptides, which occur mostly in bacteria, or present in one or two multidomain polypeptides.[1] When the polypeptides are one domain, they are can be referred to as a
full domain, and when they are two multi-domains they can be referred to as a half domain.[3] The
T domains are each built of typically 10 membrane spanning alpha helices, through which the
transported substance can cross through the plasma membrane. Also, the structure of the T
domains determines the specificity of each ABC protein. In the inward facing conformation, the
binding site on the A domain is open directly to the surrounding aqueous solutions. This allows
hydrophilic molecules to enter the binding site directly from the inner leaflet of the phospholipid
bilayer. In addition, a gap in the protein is accessible directly from the hydrophobic core of the
inner leaflet of the membrane bilayer.