2R24

Human Aldose Reductase structure

2R24 の概要

• エントリーDOI: 10.2210/pdb2r24/pdb
• 分子名称: Aldose reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, IDD594, ... (4 entities in total)
• 機能のキーワード: beta/alpha-8 tim barrel, cataract, nadp, oxidoreductase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm: P15121
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37057.98

構造登録者

Blakeley, M.P.,Ruiz, F.,Cachau, R.,Hazemann, I.,Meilleur, F.,Mitschler, A.,Ginell, S.,Afonine, P.,Ventura, O.N.,Cousido-Siah, A.,Haertlein, M.,Joachimiak, A.,Myles, D.,Podjarny, A. (登録日: 2007-08-24, 公開日: 2008-12-23, 最終更新日: 2024-02-21)

主引用文献

Blakeley, M.P.,Ruiz, F.,Cachau, R.,Hazemann, I.,Meilleur, F.,Mitschler, A.,Ginell, S.,Afonine, P.,Ventura, O.N.,Cousido-Siah, A.,Haertlein, M.,Joachimiak, A.,Myles, D.,Podjarny, A.
Quantum model of catalysis based on mobile proton revealed by subatomic X-Ray and neutron diffraction studies of h-Aldose Reductase
Proc.Natl.Acad.Sci.USA, 105:1844-1848, 2008

PubMed Abstract: We present results of combined studies of the enzyme human aldose reductase (h-AR, 36 kDa) using single-crystal x-ray data (0.66 A, 100K; 0.80 A, 15K; 1.75 A, 293K), neutron Laue data (2.2 A, 293K), and quantum mechanical modeling. These complementary techniques unveil the internal organization and mobility of the hydrogen bond network that defines the properties of the catalytic engine, explaining how this promiscuous enzyme overcomes the simultaneous requirements of efficiency and promiscuity offering a general mechanistic view for this class of enzymes.

PubMed: 18250329
DOI: 10.1073/pnas.0711659105

実験手法

NEUTRON DIFFRACTION (2.194 Å)
X-RAY DIFFRACTION (1.752 Å)