[HTML][HTML] Crystal structure of rabbit muscle creatine kinase
JKM Rao, G Bujacz, A Wlodawer - FEBS letters, 1998 - Elsevier
JKM Rao, G Bujacz, A Wlodawer
FEBS letters, 1998•ElsevierThe crystal structure of rabbit muscle creatine kinase, solved at 2.35 Å 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.
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.
The crystal structure of rabbit muscle creatine kinase, solved at 2.35 Å 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.
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