Structural highlights
Function
[KCRM_RABIT] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
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 crystal structure of rabbit muscle creatine kinase, solved at 2.35 A resolution by X-ray diffraction methods, clearly identified the active site with bound sulfates surrounded by a constellation of arginine residues. The putative binding site of creatine, which is occupied by a sulfate group in this analysis, has been tentatively identified. The dimeric interface of the enzyme is held together by a small number of hydrogen bonds.
Crystal structure of rabbit muscle creatine kinase.,Rao JK, Bujacz G, Wlodawer A FEBS Lett. 1998 Nov 13;439(1-2):133-7. PMID:9849893[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rao JK, Bujacz G, Wlodawer A. Crystal structure of rabbit muscle creatine kinase. FEBS Lett. 1998 Nov 13;439(1-2):133-7. PMID:9849893
