Sandbox 201: Difference between revisions
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* <scene name='Sandbox_201/Atp_binding_site/1'>ATP binding site</scene> | * <scene name='Sandbox_201/Atp_binding_site/1'>ATP binding site</scene> | ||
:The N- and C-terminal domains are both able to form interactions with ATP and ATP analogues. But the ß-strands of the core region in the N-terminal domain contain most of the residues involved in binding ATP. <scene name='Sandbox_201/Atp_binding_site_lys75/1'>Lys75</scene>, <scene name='Sandbox_201/Atp_binding_site_lys99/1'>Lys99</scene> (motif I), Lys119 (motif Ia), Lys240 (motif V), and Lys242 (motif V) interact with the phosphate groups of ATP and ATP analogues. | :The N- and C-terminal domains are both able to form interactions with ATP and ATP analogues. But the ß-strands of the core region in the N-terminal domain contain most of the residues involved in binding ATP. <scene name='Sandbox_201/Atp_binding_site_lys75/1'>Lys75</scene>, <scene name='Sandbox_201/Atp_binding_site_lys99/1'>Lys99</scene> (motif I), <scene name='Sandbox_201/Atp_binding_site_lys119/1'>Lys119</scene> (motif Ia), Lys240 (motif V), and Lys242 (motif V) interact with the phosphate groups of ATP and ATP analogues. | ||
* Divalent cation binding sites | * Divalent cation binding sites | ||
