1dhr

CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE

spinqualitylabelsall models 1dhr, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dhr is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAD Activity: 6,7-dihydropteridine reductase, with EC number 1.5.1.34 Resources: FirstGlance, OCA, RCSB, PDBsum 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 The structure of a binary complex of dihydropteridine reductase [DHPR; NAD(P)H:6,7-dihydropteridine oxidoreductase, EC 1.6.99.7] with its cofactor, NADH, has been solved and refined to a final R factor of 15.4% by using 2.3 A diffraction data. DHPR is an alpha/beta protein with a Rossmann-type dinucleotide fold for NADH binding. Insertion of an extra threonine residue in the human enzyme is associated with severe symptoms of a variant form of phenylketonuria and maps to a tightly linked sequence of secondary-structural elements near the dimer interface. Dimerization is mediated by a four-helix bundle motif (two helices from each protomer) having an unusual right-handed twist. DHPR is structurally and mechanistically distinct from dihydrofolate reductase, appearing to more closely resemble certain nicotinamide dinucleotide-requiring flavin-dependent enzymes, such as glutathione reductase. Crystal structure of rat liver dihydropteridine reductase.,Varughese KI, Skinner MM, Whiteley JM, Matthews DA, Xuong NH Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6080-4. PMID:1631094 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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