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Literature summary for 2.7.1.1 extracted from

  • Ermakova, E.
    Structural insight into the glucokinase-ligands interactions. Molecular docking study (2016), Comput. Biol. Chem., 64, 281-296.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular docking of glucose and synthetic ligands (allosteric activators). Predicted position of glucose coincides with its position in the crystallographic complex. Glucose interacts with the residues of large (Ile225, Gly229, Cys230, Asn231, Glu256, Gln287, Glu290) and small (Ser151, Phe152, Pro153, Thr168, Lys169) domains and with the residues of connecting region Asn204, Asp205. Hydrogen bonds with Asp205, Glu256 and Glu290 stabilize this complex. The allosteric site formed by the small and large domains and two loops connecting them is located approximately 20 A away from the glucose binding site. There are two stable positions of glucokinase activators and approximately five sites of ligand binding with less favorable interaction energy. Predicted position of glucose coincides with its position in the crystallographic complex Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P35557
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Synonyms

Synonyms Comment Organism
GCK
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Homo sapiens