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| | <StructureSection load='1qh5' size='340' side='right'caption='[[1qh5]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='1qh5' size='340' side='right'caption='[[1qh5]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qh5]] is a 2 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=1QH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QH5 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qh3|1qh3]]</td></tr> | + | <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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.6 3.1.2.6] </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=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> |
| - | <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=1qh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qh5 OCA], [http://pdbe.org/1qh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qh5 RCSB], [http://www.ebi.ac.uk/pdbsum/1qh5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qh5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Hydrolase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cameron, A D]] | + | [[Category: Cameron AD]] |
| - | [[Category: Mannervik, B]] | + | [[Category: Mannervik B]] |
| - | [[Category: Olin, B]] | + | [[Category: Olin B]] |
| - | [[Category: Ridderstrom, M]] | + | [[Category: Ridderstrom M]] |
| - | [[Category: Metallo-hydrolase]]
| + | |
| Structural highlights
Function
GLO2_HUMAN Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
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
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cameron AD, Ridderstrom M, Olin B, Mannervik B. Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure. 1999 Sep 15;7(9):1067-78. PMID:10508780
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