Rao J K, Bujacz G, Wlodawer A
Macromolecular Structure Laboratory, NCI-Frederick Cancer Research and Development Center, ABL-Basic Research Program, Frederick, MD 21702, USA.
FEBS Lett. 1998 Nov 13;439(1-2):133-7. doi: 10.1016/s0014-5793(98)01355-6.
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.
通过X射线衍射方法以2.35埃分辨率解析得到的兔肌肉肌酸激酶晶体结构,清晰地确定了活性位点,该位点被结合的硫酸盐所占据,周围环绕着一群精氨酸残基。在该分析中被硫酸盐基团占据的肌酸假定结合位点已被初步确定。该酶的二聚体界面通过少量氢键维系在一起。