1bzr
ATOMIC RESOLUTION CRYSTAL STRUCTURE ANALYSIS OF NATIVE DEOXY AND CO MYOGLOBIN FROM SPERM WHALE AT ROOM TEMPERATURE
| |||||||
| , resolution 1.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1BZR is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
ReferenceReference
A steric mechanism for inhibition of CO binding to heme proteins., Kachalova GS, Popov AN, Bartunik HD, Science. 1999 Apr 16;284(5413):473-6. PMID:10205052
Page seeded by OCA on Thu Mar 20 10:18:00 2008