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 three-dimensional structure of sperm whale myoglobin His64(E7)-->Val,Thr67(E10)-->Arg double mutant has been studied by X-ray crystallography at 1.6 A resolution, and refined to a crystallographic R-factor of 0.197. The Arg67(E10) side chain is extended in the direction of the ligand binding site, and its NH1 atom is at a distance of 3.11 A from the NH1 atom of Arg45(CD3), which is also pointing towards the distal site. Both are kept in this position by hydrogen bonding and electrostatic interactions with a solvent sulfate ion, located amongst the two, on the protein surface. No liganded water molecule is present at the sixth coordination position of the Fe(III) heme.
Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution.,Rizzi M, Bolognesi M, Coda A, Cutruzzola F, Allocatelli CT, Brancaccio A, Brunori M FEBS Lett. 1993 Mar 29;320(1):13-6. PMID:8462669[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rizzi M, Bolognesi M, Coda A, Cutruzzola F, Allocatelli CT, Brancaccio A, Brunori M. Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution. FEBS Lett. 1993 Mar 29;320(1):13-6. PMID:8462669
