It is important to mention that challenges like the prediction of the relative positions of protein domains and their changes when an external stimulus is applied remain partially unsolved. Additionally, the transition from disordered to ordered domain states cannot be elucidated using AlphaFold, and it is limited to structures with less than 2700 amino acids . Nevertheless, the high impact of its accurate protein structure predictions is indisputable . For example, the predicted structural information about nucleoporins has been combined with cryo-electron tomography (cryo-ET) to generate a model that precisely explains 90% of the scaffold of the human nuclear pore complex (NPC) . Another example is the identification of tens of thousands of unknown potential binding sites for iron-sulfur clusters and zinc ions in more than 360,000 proteins .