Your privacy, your choice

We use essential cookies to make sure the site can function. We also use optional cookies for advertising, personalisation of content, usage analysis, and social media.

By accepting optional cookies, you consent to the processing of your personal data - including transfers to third parties. Some third parties are outside of the European Economic Area, with varying standards of data protection.

See our privacy policy for more information on the use of your personal data.

for further information and to change your choices.
Skip to main content
Fig. 1 | Cellular & Molecular Biology Letters

Fig. 1

From: Glucokinase (GCK) in diabetes: from molecular mechanisms to disease pathogenesis

Fig. 1

Surface representation of overall structure of glucokinase (GCK). The complex structure of glucose-bound GCK in the presence of the non-hydrolysable ATP analogue adenosine 50-(β,-γ-imino) triphosphate (AMP-PNP) and allosteric activator N-thiazol-2-yl-2-amino-4-fluoro5-(1-methylimidazol-2-yl)thiobenzamide (TAFMT) (PDBID: 3ID8). The complex comprises glucose (green, sphere), AMP-PNP (magenta, ball, and stick), and TAFMT (orange, sphere) with GCK in an active conformation. The conformational relationship of the large domain (light blue) and the small domain (salmon) exhibited a closed form

Back to article page

Cellular & Molecular Biology Letters

ISSN: 1689-1392

Contact us