Patch clamp investigations of single ion channels give insight into the function of these proteins on the molecular level. Utilizing this technique, we performed detailed investigations of the human P2X7 receptor, which is a ligand gated ion channel opened by binding of ATP, like the other P2X receptor subtypes. P2X7 receptors become activated under pathological conditions of ATP release like hypoxia or cell destruction. They are involved in inflammatory and nociceptive reactions of the organism to these pathological events. Knowledge about the function of the P2X7 receptor might lead to a deeper insight into the signaling within these pathophysiological processes and to reveal targets of anti-inflammatory and anti-nociceptive therapies. We found that hP2X7 receptors become activated by ATP within a few milliseconds and are permeable only to cations. Their ion channel conductance remains constant across minutes of activation, which argues against dilation of the ion channel pore. Substitution of Na+ or Cl- ions not only influences the ion channel current amplitude but also the channel gating. Polar residues of the second transmembrane domains of the three protein subunits are important for ion conduction, with S342 constituting the ion selectivity filter and the gate of the channel. The specific long C-terminal domains are important for hP2X7 receptor ion channel function, as their loss strongly decreases ion channel currents.