Structural highlights
Function
[MYG_PIG] 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
As part of a protein engineering study, the X-ray crystal structure of recombinant pig myoglobin, prepared and crystallized from E. coli, has been determined. Diffraction data were collected to 2.5 A spacing using a synchrotron X-ray source. The structure was solved using the molecular-replacement method and refined using least-squares minimization procedures to a crystallographic R factor of 18.5% using 14,481 reflections between 10 and 2.5 A. A preliminary comparison of the structure of pig myoglobin with other myoglobin structures is presented.
Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement.,Smerdon SJ, Oldfield TJ, Dodson EJ, Dodson GG, Hubbard RE, Wilkinson AJ Acta Crystallogr B. 1990 Jun 1;46 ( Pt 3):370-7. PMID:2383370[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Smerdon SJ, Oldfield TJ, Dodson EJ, Dodson GG, Hubbard RE, Wilkinson AJ. Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement. Acta Crystallogr B. 1990 Jun 1;46 ( Pt 3):370-7. PMID:2383370
