title: Crystal structure of rabbit muscle creatine kinase.
abstract: 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.
authors.affiliation: Macromolecular Structure Laboratory, NCI-Frederick Cancer Research and Development Center, ABL-Basic Research Program, Frederick, MD 21702, USA. rao@ncifcrf.gov
authors.forename: J K
authors.initials: JK
authors.lastname: Rao
authors.forename: G
authors.initials: G
authors.lastname: Bujacz
authors.forename: A
authors.initials: A
authors.lastname: Wlodawer
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology; D003402:Creatine Kinase / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009132:Muscles / Q000201:enzymology*; D011487:Protein Conformation; D011817:Rabbits; D013431:Sulfates
chemical_list: D013431:Sulfates; D003402:Creatine Kinase