2qxw | pdb_00002qxw
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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 NDP, LDT and CIT as ligands. Active as Aldehyde reductase, with EC number 1.1.1.21 Known structural/functional Sites: AC1, AC2, AC3 and AC4. 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
