ADP dissociates from Kinesin-1 complex.
The intrinsic the first head domain hydrolyzes the ATP to ADP, the second head domain binds to the microtubule, and the first head releases ADP and binds ATP.
In conclusion following the consensus in Kinesin-1 motion (part of them described in the previous event):
Fifth, after the partner Kinesin?1 head has reached its forward binding site, ADP is released (leaving an empty site) and this new front head binds tightly to the microtubule, thereby leading to internal strain (perhaps communicated through the neck regions, or perhaps through the microtubule). This strain tends to suppress the premature binding of ATP to the front head until the rear head had a chance to hydrolyze its own ATP and release phosphate. Binding to the forward site may also induce additional conformations, including the possibility of motions that are not strictly parallel to the microtubule long axis (Kawaguchi 2008, Block 2007).