Structural highlights
Function
[DHPR_RAT] The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A binary complex of dihydropteridine reductase and NADH crystallizes in the space group C2, with a = 222.2, b = 46.5, c = 95.3 A and beta = 101.1 degrees. There are two dimers in the asymmetric unit. The structure was solved by molecular-replacement techniques and refined with 2.6 A data to a crystallographic R factor of 16.8%. Each dimer has twofold non-crystallographic symmetry and the four individual monomers in the asymmetric unit have the same overall molecular conformation.
Crystal structure of a monoclinic form of dihydropteridine reductase from rat liver.,Su Y, Skinner MM, Xuong NH, Matthews DA, Whiteley JM, Varughese KI Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):884-8. PMID:15299357[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Su Y, Skinner MM, Xuong NH, Matthews DA, Whiteley JM, Varughese KI. Crystal structure of a monoclinic form of dihydropteridine reductase from rat liver. Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):884-8. PMID:15299357 doi:10.1107/S0907444994005718
