Human Oxymyoglobin

        In this tutorial you will learn how myoglobin binds oxygen. The mechanism of oxygen binding is similar in all myoglobins and hemoglobins. After a brief description of the tertiary structure of myoglobin, we will look at how the protein provides a pocket into which the O2 can fit. Finally, we will discuss what happens when the heme group binds oxygen.

  Toggle transparency/spacefilled models. In the transparency the N-terminus is shown in blue.
  Toggle backbone trace/transparency.

Myoglobin contains eight segments of a helix, designated by the letters A through H, counting from the N-terminus. The helices provide a rigid structural framework for the heme pocket.
  The heme is wedged into a hydrophobic pocket between the E and F helices. Five invariant residues crucial for oxygen binding are situated in the heme pocket. They are shown in green.

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