The alpha-hemolysin toxin self-assembles in lipid bilayers to form water-filled pores. In recent years, alpha-hemolysin has received great attention, mainly due to its possible usage as a sensing element. We measured the ion currents through single alpha-hemolysin channels and confirmed the presence of two different subpopulations of channels with conductance levels of 465 +/- 30 pS and 280 +/- 30 pS. Different oligomerization states could be responsible for these two conductances. In fact, a heptameric structure of the channel was revealed by x-ray crystallography, whereas atomic force microscopy revealed a hexameric structure. Due to the low resolution of atomic force microscopy the atomic details of the hexameric structure are still unknown, and are here predicted by computational methods. Several possible structures of the hexameric channel were defined, and were simulated by molecular dynamics. The conductances of these channel models were computed by a numerical method based on the Poisson-Nernst-Planck electrodiffusion theory, and the values were compared to experimental data. In this way, we identified a model of the alpha-hemolysin hexameric state with conductance characteristics consistent with the experimental data. Since the oligomerization state of the channel may affect its behavior as a molecular sensor, knowing the atomic structure of the hexameric state will be useful for biotechnological applications of alpha-hemolysin.