Hemoglobin and oxygen transport

Hemoglobin carries oxygen from the lungs to every tissue, and myoglobin stores it inside muscle. Comparing the deoxy (T state) and oxy (R state) structures shows how binding oxygen at one heme makes the other hemes grab oxygen more easily, the classic example of cooperativity. The collection also includes sickle cell hemoglobin and oxygen carriers from other organisms.

Open Human deoxyhemoglobin in 3D

20 structures

• Human deoxyhemoglobin4HHB
  The classic T-state structure from Max Perutz's group, used in countless textbooks.
• Human deoxyhemoglobin at 1.25 Å2DN2
• Human oxyhemoglobin1HHO
  Compare with 4HHB to see the T to R quaternary change.
• Human oxyhemoglobin at 1.25 Å2DN1
• Human carbonmonoxy hemoglobin2DN3
  Carbon monoxide binds the same heme iron as oxygen, but far more tightly.
• Deoxyhemoglobin bound to 2,3-DPG1B86
  2,3-DPG (also called 2,3-BPG) stabilizes the T state and helps release oxygen in tissues.
• T-state hemoglobin with oxygen at all four hemes1GZX
• Sickle cell hemoglobin (deoxy HbS)2HBS
  A single Glu to Val change in the beta chain lets deoxy HbS molecules stick together into fibers.
• Horse deoxyhemoglobin2DHB
• Sperm whale myoglobin1MBN
  Myoglobin was the first protein whose 3D structure was solved, by John Kendrew's group.
• Sperm whale oxymyoglobin1MBO
• Sperm whale oxymyoglobin at atomic resolution1A6M
• Human neuroglobin1OJ6
• Human cytoglobin1V5H
• Soybean leghemoglobin from root nodules1BIN
• Horseshoe crab hemocyanin, a copper-based oxygen carrier1OXY
• Erythrocruorin, a midge larva hemoglobin1ECA
• Human hemoglobin alpha (AlphaFold)P69905 (AlphaFold)
• Human hemoglobin beta (AlphaFold)P68871 (AlphaFold)
• Human myoglobin (AlphaFold)P02144 (AlphaFold)

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