2QXW

Perdeuterated alr2 in complex with idd594

Summary for 2QXW

• Entry DOI: 10.2210/pdb2qxw/pdb
• Related: 1US0
• Descriptor: Aldose reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, IDD594, ... (5 entities in total)
• Functional Keywords: oxidoreductase, nadp, idd594, cataract
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P15121
• Total number of polymer chains: 1
• Total formula weight: 37444.25

Authors

Blakeley, M.P.,Ruiz, F.,Cachau, R.,Hazemann, I.,Meilleur, F.,Mitschler, A.,Ginell, S.,Afonine, P.,Ventura, O.,Cousido-Siah, A.,Joachimiak, A.,Myles, D.,Podjarny, A. (deposition date: 2007-08-13, release date: 2008-01-22, Last modification date: 2023-08-30)

Primary citation

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 a 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

Experimental method

X-RAY DIFFRACTION (0.8 Å)