1DIR

CRYSTAL STRUCTURE OF A MONOCLINIC FORM OF DIHYDROPTERIDINE REDUCTASE FROM RAT LIVER

Summary for 1DIR

• Entry DOI: 10.2210/pdb1dir/pdb
• Descriptor: DIHYDROPTERIDINE REDUCTASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase(acting on nadh or nadph)
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 4
• Total formula weight: 104970.40

Authors

Varughese, K.I.,Su, Y.,Skinner, M.M.,Matthews, D.A.,Whitely, J.M.,Xuong, N.H. (deposition date: 1994-04-18, release date: 1994-07-31, Last modification date: 2024-02-07)

Primary citation

Su, Y.,Skinner, M.M.,Xuong, N.H.,Matthews, D.A.,Whiteley, J.M.,Varughese, K.I.
Crystal structure of a monoclinic form of dihydropteridine reductase from rat liver.
Acta Crystallogr.,Sect.D, 50:884-888, 1994

PubMed Abstract: 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.

PubMed: 15299357
DOI: 10.1107/S0907444994005718

Experimental method

X-RAY DIFFRACTION (2.6 Å)