The structure presented here is the human enzyme, phosphomannomutase 1, bound to its substrate, [...]mannose 1-phosphate (M1P). There are 2 isoforms of this enzyme in humans—PMM1 and PMM2, both of which catalyzes the reaction between a mannose 1-phosphate to a mannose 6-phosphate with comparable catalytic efficiency. A decrease in PMM2 activity results in a disease called Congenital Disorder of Glycosylation type 1a (CDG-1a) characterized by severe defects mainly involving the nervous system. In addition to similar kinetic properties, PMM1 and PMM2 also have similar structural features and a conversed active site, therefore, this structure of PMM1 bound to substrate M1P gives us insight to the structural basis of CDG-1a causing mutations.
This structure was solved by Nicholas R. Silvaggi