2qxw

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spinqualitylabelsall models 2qxw, resolution 0.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Perdeuterated alr2 in complex with idd594

Overview

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.

About this Structure

2QXW is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Aldehyde reductase, with EC number 1.1.1.21 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.

Reference

Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase., Blakeley MP, Ruiz F, Cachau R, Hazemann I, Meilleur F, Mitschler A, Ginell S, Afonine P, Ventura ON, Cousido-Siah A, Haertlein M, Joachimiak A, Myles D, Podjarny A, Proc Natl Acad Sci U S A. 2008 Feb 12;105(6):1844-8. Epub 2008 Feb 4. PMID:18250329

Page seeded by OCA on Fri Mar 14 09:43:12 2008