2qxw

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|PDB= 2qxw |SIZE=350|CAPTION= <scene name='initialview01'>2qxw</scene>, resolution 0.80&Aring;
|PDB= 2qxw |SIZE=350|CAPTION= <scene name='initialview01'>2qxw</scene>, resolution 0.80&Aring;
|SITE= <scene name='pdbsite=AC1:Ndp+Binding+Site+For+Residue+A+318'>AC1</scene>, <scene name='pdbsite=AC2:Ldt+Binding+Site+For+Residue+A+320'>AC2</scene>, <scene name='pdbsite=AC3:Cit+Binding+Site+For+Residue+A+400'>AC3</scene> and <scene name='pdbsite=AC4:Cit+Binding+Site+For+Residue+A+450'>AC4</scene>
|SITE= <scene name='pdbsite=AC1:Ndp+Binding+Site+For+Residue+A+318'>AC1</scene>, <scene name='pdbsite=AC2:Ldt+Binding+Site+For+Residue+A+320'>AC2</scene>, <scene name='pdbsite=AC3:Cit+Binding+Site+For+Residue+A+400'>AC3</scene> and <scene name='pdbsite=AC4:Cit+Binding+Site+For+Residue+A+450'>AC4</scene>
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|LIGAND= <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=LDT:IDD594'>LDT</scene> and <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene>
+
|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=LDT:IDD594'>LDT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </span>
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1us0|1US0]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qxw OCA], [http://www.ebi.ac.uk/pdbsum/2qxw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qxw RCSB]</span>
}}
}}
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[[Category: Ruiz, F.]]
[[Category: Ruiz, F.]]
[[Category: Ventura, O.]]
[[Category: Ventura, O.]]
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[[Category: CIT]]
 
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[[Category: LDT]]
 
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[[Category: NDP]]
 
[[Category: acetylation]]
[[Category: acetylation]]
[[Category: cataract]]
[[Category: cataract]]
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[[Category: polymorphism]]
[[Category: polymorphism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:30:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:54:37 2008''

Revision as of 01:54, 31 March 2008

Image:2qxw.jpg


PDB ID 2qxw

Drag the structure with the mouse to rotate
, resolution 0.80Å
Sites: , , and
Ligands: , ,
Activity: Aldehyde reductase, with EC number 1.1.1.21
Related: 1US0


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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