1dhr | pdb_00001dhr

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 Buffalo rat. The August 2015 RCSB PDB Molecule of the Month feature on Tetrahydrobiopterin Biosynthesis by David Goodsell is 10.2210/rcsb_pdb/mom_2015_8. 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, PDBe, RCSB, PDBsum, ProSAT 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 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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