4ee0

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Current revision (11:03, 1 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ee0]] 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=4EE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EE0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ee0]] 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=4EE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EE0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0O4:4-(ISOQUINOLIN-1-YL)-N-[2-(MORPHOLIN-4-YL)ETHYL]BENZAMIDE'>0O4</scene>, <scene name='pdbligand=GSF:L-GAMMA-GLUTAMYL-3-SULFINO-L-ALANYLGLYCINE'>GSF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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]] 1.75&#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=0O4:4-(ISOQUINOLIN-1-YL)-N-[2-(MORPHOLIN-4-YL)ETHYL]BENZAMIDE'>0O4</scene>, <scene name='pdbligand=GSF:L-GAMMA-GLUTAMYL-3-SULFINO-L-ALANYLGLYCINE'>GSF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4ee0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ee0 OCA], [https://pdbe.org/4ee0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ee0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ee0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ee0 ProSAT]</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=4ee0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ee0 OCA], [https://pdbe.org/4ee0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ee0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ee0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ee0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/HPGDS_HUMAN HPGDS_HUMAN]] Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide.<ref>PMID:10824118</ref> <ref>PMID:11672424</ref> <ref>PMID:9425264</ref> <ref>PMID:9353279</ref> <ref>PMID:12627223</ref> <ref>PMID:15113825</ref> <ref>PMID:16547010</ref> <ref>PMID:19939518</ref>
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[https://www.uniprot.org/uniprot/HPGDS_HUMAN HPGDS_HUMAN] Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide.<ref>PMID:10824118</ref> <ref>PMID:11672424</ref> <ref>PMID:9425264</ref> <ref>PMID:9353279</ref> <ref>PMID:12627223</ref> <ref>PMID:15113825</ref> <ref>PMID:16547010</ref> <ref>PMID:19939518</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The inhibition of hH-PGDS has been proposed as a potential target for the development of anti-allergic and anti-inflammatory drugs. Herein we describe our investigation of the binding pocket of this important enzyme and our observation that two water molecules bind to our inhibitors and the enzyme. A series of compounds were prepared to the probe the importance of the water molecules in determining the binding affinity of the inhibitors to the enzyme. The study provides insight into the binding requirements for the design of potent hH-PGDS inhibitors.
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Investigation of the binding pocket of human hematopoietic prostaglandin (PG) D2 synthase (hH-PGDS): A tale of two waters.,Trujillo JI, Kiefer JR, Huang W, Day JE, Moon J, Jerome GM, Bono CP, Kornmeier CM, Williams ML, Kuhn C, Rennie GR, Wynn TA, Carron CP, Thorarensen A Bioorg Med Chem Lett. 2012 Jun 1;22(11):3795-9. Epub 2012 Apr 13. PMID:22546671<ref>PMID:22546671</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 4ee0" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==

Current revision

Crystal structure of hH-PGDS with water displacing inhibitor

PDB ID 4ee0

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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