1BZ6
ATOMIC RESOLUTION CRYSTAL STRUCTURE AQUOMET-MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE
Summary for 1BZ6
Entry DOI | 10.2210/pdb1bz6/pdb |
Descriptor | PROTEIN (MYOGLOBIN), SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
Functional Keywords | oxygen transport, respiratory protein, heme, atomic resolution, oxygen storage |
Biological source | Physeter catodon (sperm whale) |
Total number of polymer chains | 1 |
Total formula weight | 18235.69 |
Authors | Popov, A.N.,Kachalova, G.S.,Bartunik, H.D. (deposition date: 1998-11-05, release date: 1999-05-10, Last modification date: 2023-08-09) |
Primary citation | Kachalova, G.S.,Popov, A.N.,Bartunik, H.D. A steric mechanism for inhibition of CO binding to heme proteins. Science, 284:473-476, 1999 Cited by PubMed Abstract: The crystal structures of myoglobin in the deoxy- and carbon monoxide-ligated states at a resolution of 1.15 angstroms show that carbon monoxide binding at ambient temperatures requires concerted motions of the heme, the iron, and helices E and F for relief of steric inhibition. These steps constitute the main mechanism by which heme proteins lower the affinity of the heme group for the toxic ligand carbon monoxide. PubMed: 10205052DOI: 10.1126/science.284.5413.473 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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