Structural highlights
Function
[MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The X-ray crystal structure of the ferric sperm whale (Physeter catodon) myoglobin:imidazole complex has been refined at 2.0 A resolution, to a final R-factor of 14.8%. The overall conformation of the protein is little affected by binding of the ligand. Imidazole is co-ordinated to the heme iron at the distal site, and forces distinguishable local changes in the surrounding protein residues. His64(E7) swings out of the distal pocket and becomes substantially exposed to the solvent: nevertheless, it stabilizes the exogenous ligand by hydrogen bonding. The side-chains of residues Arg45(CD3) and Asp60(E3) are also affected by imidazole association.
X-ray crystal structure of the ferric sperm whale myoglobin: imidazole complex at 2.0 A resolution.,Lionetti C, Guanziroli MG, Frigerio F, Ascenzi P, Bolognesi M J Mol Biol. 1991 Feb 5;217(3):409-12. PMID:1994031[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lionetti C, Guanziroli MG, Frigerio F, Ascenzi P, Bolognesi M. X-ray crystal structure of the ferric sperm whale myoglobin: imidazole complex at 2.0 A resolution. J Mol Biol. 1991 Feb 5;217(3):409-12. PMID:1994031
