1BZR
ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE
Summary for 1BZR
| Entry DOI | 10.2210/pdb1bzr/pdb |
| Descriptor | PROTEIN (MYOGLOBIN), SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
| Functional Keywords | carbonmonoxy myoglobin, atomic resolution, oxygen storage |
| Biological source | Physeter catodon (sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18071.57 |
| Authors | Kachalova, G.S.,Popov, A.N.,Bartunik, H.D. (deposition date: 1998-11-03, 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 (1.15 Å) |
Structure validation
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