EC Number   |
Title |
Organism |
|---|
    2.7.6.3 | A network of conformational transitions revealed by molecular dynamics simulations of the binary complex of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase with MgATP |
Escherichia coli |
| 2.7.6.3 | Bisubstrate inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase Transition state analogs for high affinity binding |
Escherichia coli |
| 2.7.6.3 | Exploration of multistate conformational dynamics upon ligand binding of a monomeric enzyme involved in pyrophosphoryl transfer |
Escherichia coli |
| 2.7.6.3 | Probing the binding mechanism of mercaptoguanine derivatives as inhibitors of HPPK by docking and molecular dynamics simulations |
Staphylococcus aureus |
| 2.7.6.3 | Structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium vivax sheds light on drug resistance |
Plasmodium vivax |
| 2.7.6.3 | Structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium vivax sheds light on drug resistance |
Plasmodium vivax Salvador 1 |
| 2.7.6.3 | Structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium vivax sheds light on drug resistance |
Plasmodium vivax Salvador I |
| 2.7.6.3 | The structure of Plasmodium falciparum hydroxymethyldihydropterin pyrophosphokinase-dihydropteroate synthase reveals the basis of sulfa resistance |
Plasmodium falciparum |
| 2.7.6.3 | 7,8-Dihydropteroate-synthesizing enzyme from Plasmodium chabaudi |
Plasmodium chabaudi |
| 2.7.6.3 | A rapid assay for dihydropteroate synthase activity suitable for identification of inhibitors |
Saccharomyces cerevisiae |
