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Figure 2
Comparison of the active sites of human hexokinase IV and PvHK. (a) Crystal structure of human hexokinase IV (glucokinase) in the active closed conformation with BGC (glucose) and activator. The glucose-binding site is highlighted in the close-up view and the glucose-coordinating residues are shown (PDB entry 4dhy). (b) Cryo-EM-derived PvHK protomer in the open state. The unmodeled ligand density (mesh) at the hexose-binding site is shown along with the residues that appear to coordinate the ligand. (c) The PvHK protomer in the closed conformation with extra density present in the active site. In the close-up view, the extra density and coordinating residues are shown for a one-to-one comparison with human hexokinase. Most of the residues in human hexokinase and PvHK are conserved and are seen in a very similar conformation in PvHK to that observed in human HKs.

IUCrJ
Volume 7| Part 3| May 2020| Pages 453-461
ISSN: 2052-2525
https://doi.org/10.1107/S2052252520002456