2qxw | pdb_00002qxw
Perdeuterated alr2 in complex with idd594
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| 2qxw, resolution 0.80Å | |||||||||||||
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| Sites: | AC1, AC2, AC3 and AC4 | ||||||||||||
| Ligands: | CIT, LDT, NDP | ||||||||||||
| Activity: | Aldehyde reductase, with EC number 1.1.1.21 | ||||||||||||
| Related: | 1US0
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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 Mon Mar 31 04:54:37 2008
