4kyh: Difference between revisions

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<StructureSection load='4kyh' size='340' side='right'caption='[[4kyh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='4kyh' size='340' side='right'caption='[[4kyh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4kyh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KYH FirstGlance]. <br>
<table><tr><td colspan='2'>[[4kyh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KYH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZST:3,4-DIHYDRO-4-OXO-3-((5-TRIFLUOROMETHYL-2-BENZOTHIAZOLYL)METHYL)-1-PHTHALAZINE+ACETIC+ACID'>ZST</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZST:3,4-DIHYDRO-4-OXO-3-((5-TRIFLUOROMETHYL-2-BENZOTHIAZOLYL)METHYL)-1-PHTHALAZINE+ACETIC+ACID'>ZST</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2za0|2za0]], [[4kyk|4kyk]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2za0|2za0]], [[4kyk|4kyk]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Glo1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5] </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=4kyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kyh OCA], [https://pdbe.org/4kyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kyh RCSB], [https://www.ebi.ac.uk/pdbsum/4kyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kyh 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=4kyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kyh OCA], [http://pdbe.org/4kyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kyh RCSB], [http://www.ebi.ac.uk/pdbsum/4kyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kyh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/LGUL_MOUSE LGUL_MOUSE]] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (By similarity).  
[[https://www.uniprot.org/uniprot/LGUL_MOUSE LGUL_MOUSE]] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (By similarity).  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Lactoylglutathione lyase]]
[[Category: Lactoylglutathione lyase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Chen, S]]
[[Category: Chen, S]]
[[Category: Chen, Y]]
[[Category: Chen, Y]]

Revision as of 08:03, 25 August 2022

Crystal structure of mouse glyoxalase I complexed with zopolrestatCrystal structure of mouse glyoxalase I complexed with zopolrestat

Structural highlights

4kyh is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Lactoylglutathione lyase, with EC number 4.4.1.5
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LGUL_MOUSE] Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (By similarity).

Publication Abstract from PubMed

Old drugs new tricks: Zopolrestat, an aldose reductase inhibitor developed by Pfizer for the treatment of diabetic complications, is a potent competition inhibitor of human glyoxalase I (GLOI) in vitro. Crystal structures of GLOI in complex with zopolrestat and indomethacin, a nonsteroidal anti-inflammatory drug and moderate inhibitor of GLOI, provide a structural basis for the development of novel GLOI inhibitors with excellent pharmacokinetics profiles.

Zopolrestat as a Human Glyoxalase I Inhibitor and Its Structural Basis.,Zhai J, Zhang H, Zhang L, Zhao Y, Chen S, Chen Y, Peng X, Li Q, Yuan M, Hu X ChemMedChem. 2013 Jul 15. doi: 10.1002/cmdc.201300243. PMID:23857942[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Zhai J, Zhang H, Zhang L, Zhao Y, Chen S, Chen Y, Peng X, Li Q, Yuan M, Hu X. Zopolrestat as a Human Glyoxalase I Inhibitor and Its Structural Basis. ChemMedChem. 2013 Jul 15. doi: 10.1002/cmdc.201300243. PMID:23857942 doi:10.1002/cmdc.201300243

4kyh, resolution 2.50Å

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