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| | <StructureSection load='2j8t' size='340' side='right'caption='[[2j8t]], [[Resolution|resolution]] 0.82Å' scene=''> | | <StructureSection load='2j8t' size='340' side='right'caption='[[2j8t]], [[Resolution|resolution]] 0.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2j8t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J8T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2j8t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J8T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.82Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fzb|2fzb]], [[2fzd|2fzd]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8t OCA], [https://pdbe.org/2j8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j8t RCSB], [https://www.ebi.ac.uk/pdbsum/2j8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8t ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8t OCA], [http://pdbe.org/2j8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j8t RCSB], [http://www.ebi.ac.uk/pdbsum/2j8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. | + | [https://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2j8t" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2j8t" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[Aldo-keto reductase 3D structures|Aldo-keto reductase 3D structures]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aldehyde reductase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Biadene, M]] | + | [[Category: Biadene M]] |
| - | [[Category: Cousido, A]] | + | [[Category: Cousido A]] |
| - | [[Category: Ginell, S]] | + | [[Category: Ginell S]] |
| - | [[Category: Hazemann, I]] | + | [[Category: Hazemann I]] |
| - | [[Category: Podjarny, A]] | + | [[Category: Podjarny A]] |
| - | [[Category: Schneider, T R]] | + | [[Category: Schneider TR]] |
| - | [[Category: Sheldrick, G M]] | + | [[Category: Sheldrick GM]] |
| - | [[Category: Citrate]]
| + | |
| - | [[Category: Nadp]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
ALDR_HUMAN Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of human aldose reductase in complex with citrate has been determined to a resolution of 0.82 A. The difference electron density for H atoms unequivocally shows that the cofactor is in the oxidized state corresponding to the situation after the catalytic event has occurred. A citrate molecule bound to the active site has been modelled in two different conformations. These two conformations correlate with a fully closed and a partially open conformation of the so-called safety-belt loop (Gly213-Ser226). The open conformation is observed for the first time with the cofactor bound to the protein and may be related to the initial phase of the opening of the safety belt. The structure suggests that after the catalytic event, a rearrangement of a bound ligand can trigger the opening of the safety-belt loop, thus initiating the release of the oxidized cofactor.
The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop.,Biadene M, Hazemann I, Cousido A, Ginell S, Joachimiak A, Sheldrick GM, Podjarny A, Schneider TR Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):665-72. Epub 2007, May 15. PMID:17505104[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Biadene M, Hazemann I, Cousido A, Ginell S, Joachimiak A, Sheldrick GM, Podjarny A, Schneider TR. The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop. Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):665-72. Epub 2007, May 15. PMID:17505104 doi:10.1107/S0907444907011997
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