The nuclear pore complex (NPC) is the conduit for bidirectional cargo traffic between the cytoplasm and the nucleus. We determined a near-complete structure of the cytoplasmic ring of the NPC from Xenopus oocytes using single-particle cryo–electron microscopy and AlphaFold prediction. Structures of nucleoporins were predicted with AlphaFold and fit into the medium-resolution map by using the prominent secondary structural density as a guide. Certain molecular interactions were further built or confirmed by complex prediction by using AlphaFold. We identified the binding modes of five copies of Nup358, the largest NPC subunit with Phe-Gly repeats for cargo transport, and predicted it to contain a coiled-coil domain that may provide avidity to assist its role as a nucleation center for NPC formation under certain conditions.