Inhibitors | Comment | Organism | Structure |
---|---|---|---|
6,7-dihydroxyflavone | - |
Trypanosoma brucei brucei | |
baicalein | - |
Trypanosoma brucei brucei | |
additional information | docking study, structure-function analysis, and drug design. The effects of several factors on docking accuracy, including ligand and protein flexibility, are analyzed | Leishmania major | |
additional information | docking study, structure-function analysis, and drug design. The effects of several factors on docking accuracy, including ligand and protein flexibility, are analyzed | Trypanosoma brucei brucei | |
pelargonidin | - |
Trypanosoma brucei brucei | |
pinobanksin-3-o-acetate | - |
Trypanosoma brucei brucei | |
robinetinidin | - |
Trypanosoma brucei brucei |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leishmania major | Q01782 | - |
- |
Trypanosoma brucei brucei | O76290 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
LmPTR1 | - |
Leishmania major |
More | cf. EC 1.5.1.3 | Leishmania major |
pteridine reductase 1 | - |
Leishmania major |
pteridine reductase 1 | - |
Trypanosoma brucei brucei |
PTR1 | - |
Leishmania major |
PTR1 | - |
Trypanosoma brucei brucei |
Tb-PR | - |
Leishmania major |
Tb-PR | - |
Trypanosoma brucei brucei |
TbPTR1 | - |
Trypanosoma brucei brucei |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Leishmania major | |
NADPH | - |
Trypanosoma brucei brucei |
General Information | Comment | Organism |
---|---|---|
additional information | active-site structure analysis using computational docking and virtual screening techniques. Active site structure comparisons of Tb-PR (PDB ID 3JQ9) with Leishmania major pteridine reductase (Lm-PR). The size of substrate binding cleft is reduced in TbPTR1 due to differences in specific amino acids, the presence of Trp221, adjustment of the beta6-alpha6 loop. Formation of the triad is due to the presence of Cys168, C-terminal carboxyl group and His267 in TbPTR1, detailed overview | Trypanosoma brucei brucei |
additional information | active-site structure analysis using computational docking and virtual screening techniques. Active site structure comparisons of Trypanosoma brucei pteridine reductase Tb-PR (PDB ID 3JQ9) with Lm-PR. The size of substrate binding cleft is reduced in TbPTR1 due to differences in specific amino acids, the presence of Trp221, adjustment of the beta6-alpha6 loop. Formation of the triad is due to the presence of Cys168, C-terminal carboxyl group and His267 in TbPTR1, detailed overview | Leishmania major |
physiological function | the enzyme plays a critical role in the pterin metabolic pathway that is absolutely essential for the parasite's survival in the human host | Leishmania major |
physiological function | the enzyme plays a critical role in the pterin metabolic pathway that is absolutely essential for the parasite's survival in the human host | Trypanosoma brucei brucei |