1HDR
THE CRYSTALLOGRAPHIC STRUCTURE OF A HUMAN DIHYDROPTERIDINE REDUCTASE NADH BINARY COMPLEX EXPRESSED IN ESCHERICHIA COLI BY A CDNA CONSTRUCTED FROM ITS RAT HOMOLOGUE
1HDR の概要
| エントリーDOI | 10.2210/pdb1hdr/pdb |
| 分子名称 | DIHYDROPTERIDINE REDUCTASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total) |
| 機能のキーワード | oxidoreductase(acting on nadh) |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 26479.90 |
| 構造登録者 | Varughese, K.I.,Su, Y.,Xuong, N.H.,Whiteley, J.M. (登録日: 1993-08-18, 公開日: 1994-08-31, 最終更新日: 2024-02-07) |
| 主引用文献 | 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 Cited by 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主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






