1HDR

THE CRYSTALLOGRAPHIC STRUCTURE OF A HUMAN DIHYDROPTERIDINE REDUCTASE NADH BINARY COMPLEX EXPRESSED IN ESCHERICHIA COLI BY A CDNA CONSTRUCTED FROM ITS RAT HOMOLOGUE

Summary for 1HDR

• Entry DOI: 10.2210/pdb1hdr/pdb
• Descriptor: DIHYDROPTERIDINE REDUCTASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase(acting on nadh)
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 26479.90

Authors

Varughese, K.I.,Su, Y.,Xuong, N.H.,Whiteley, J.M. (deposition date: 1993-08-18, release date: 1994-08-31, Last modification date: 2024-02-07)

Primary citation

Su, Y.,Varughese, K.I.,Xuong, N.H.,Bray, T.L.,Roche, D.J.,Whiteley, J.M.
The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue.
J.Biol.Chem., 268:26836-26841, 1993

PubMed Abstract: A human dihydropteridine reductase (EC 1.6.99.10) has been created from a rat cDNA clone by a single five-oligonucleotide mutagenesis reaction and expressed in good yield in Escherichia coli. The enzyme has been purified to homogeneity, and kinetic identity to the naturally occurring enzyme has been proven. Crystallization has also been achieved, and the crystal structure was solved using 2.5 A data that was refined to an R value of 16.9%. The structure described in this report represents the first complete structural characterization of this important human enzyme.

PubMed: 8262916

Experimental method

X-RAY DIFFRACTION (2.5 Å)