Literature summary for 1.5.1.33 extracted from

Schuettelkopf, A.W.; Hardy, L.W.; Beverley, S.M.; Hunter, W.N.
Structures of Leishmania major pteridine reductase complexes reveal the active site features important for ligand binding and to guide inhibitor design (2005), J. Mol. Biol., 352, 105-116.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with NADPH, and with NADPH and biopterin, 5,6-dihydrobiopterin, or 5,6,7,8-tetrahydrobiopterin as well as in complex with NADPH and inhibitors CB3717 or trimethoprim. Enzyme does not undergo major conformational changes to accomplish binding and processing of substrates. Quinazoline moiety of inhibotr CB3717 binds similarly to pterin of substrate	Leishmania major

Inhibitors

Inhibitors	Comment	Organism	Structure
CB3717	-	Leishmania major
trimethoprim	-	Leishmania major

Organism

Organism	UniProt	Comment	Textmining
Leishmania major	-	-	-

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Release 2023.1 (January 2023)