1qh5

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[[Image:1qh5.png|left|200px]]
 
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==HUMAN GLYOXALASE II WITH S-(N-HYDROXY-N-BROMOPHENYLCARBAMOYL)GLUTATHIONE==
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The line below this paragraph, containing "STRUCTURE_1qh5", creates the "Structure Box" on the page.
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<StructureSection load='1qh5' size='340' side='right'caption='[[1qh5]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qh5]] is a 2 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=1QH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QH5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GBP:S-(N-HYDROXY-N-BROMOPHENYLCARBAMOYL)GLUTATHIONE'>GBP</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1qh5| PDB=1qh5 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qh5 OCA], [https://pdbe.org/1qh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qh5 RCSB], [https://www.ebi.ac.uk/pdbsum/1qh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qh5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLO2_HUMAN GLO2_HUMAN] Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qh/1qh5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qh5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: Glyoxalase II, the second of two enzymes in the glyoxalase system, is a thiolesterase that catalyses the hydrolysis of S-D-lactoylglutathione to form glutathione and D-lactic acid. RESULTS: The structure of human glyoxalase II was solved initially by single isomorphous replacement with anomalous scattering and refined at a resolution of 1.9 A. The enzyme consists of two domains. The first domain folds into a four-layered beta sandwich, similar to that seen in the metallo-beta-lactamases. The second domain is predominantly alpha-helical. The active site contains a binuclear zinc-binding site and a substrate-binding site extending over the domain interface. The model contains acetate and cacodylate in the active site. A second complex was derived from crystals soaked in a solution containing the slow substrate, S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione. This complex was refined at a resolution of 1.45 A. It contains the added ligand in one molecule of the asymmetric unit and glutathione in the other. CONCLUSIONS: The arrangement of ligands around the zinc ions includes a water molecule, presumably in the form of a hydroxide ion, coordinated to both metal ions. This hydroxide ion is situated 2.9 A from the carbonyl carbon of the substrate in such a position that it could act as the nucleophile during catalysis. The reaction mechanism may also have implications for the action of metallo-beta-lactamases.
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===HUMAN GLYOXALASE II WITH S-(N-HYDROXY-N-BROMOPHENYLCARBAMOYL)GLUTATHIONE===
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Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue.,Cameron AD, Ridderstrom M, Olin B, Mannervik B Structure. 1999 Sep 15;7(9):1067-78. PMID:10508780<ref>PMID:10508780</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1qh5" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10508780 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10508780}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1qh5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QH5 OCA].
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==Reference==
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<ref group="xtra">PMID:010508780</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Hydroxyacylglutathione hydrolase]]
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[[Category: Large Structures]]
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[[Category: Cameron, A D.]]
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[[Category: Cameron AD]]
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[[Category: Mannervik, B.]]
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[[Category: Mannervik B]]
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[[Category: Olin, B.]]
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[[Category: Olin B]]
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[[Category: Ridderstrom, M.]]
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[[Category: Ridderstrom M]]
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[[Category: Hydrolase]]
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[[Category: Metallo-hydrolase]]
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Current revision

HUMAN GLYOXALASE II WITH S-(N-HYDROXY-N-BROMOPHENYLCARBAMOYL)GLUTATHIONE

PDB ID 1qh5

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