4y2r: Difference between revisions

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 ==Structure of soluble epoxide hydrolase in complex with 2-(piperazin-1-yl)nicotinonitrile==
-<StructureSection load='4y2r' size='340' side='right' caption='[[4y2r]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
+<StructureSection load='4y2r' size='340' side='right'caption='[[4y2r]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4y2r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y2R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y2R FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4y2r]] 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=4Y2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y2R FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=49O:2-(PIPERAZIN-1-YL)PYRIDINE-3-CARBONITRILE'>49O</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.45&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y2j|4y2j]], [[4y2p|4y2p]], [[4y2q|4y2q]], [[4y2s|4y2s]], [[4y2t|4y2t]], [[4y2u|4y2u]], [[4y2v|4y2v]], [[4y2x|4y2x]], [[4y2y|4y2y]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=49O:2-(PIPERAZIN-1-YL)PYRIDINE-3-CARBONITRILE'>49O</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Soluble_epoxide_hydrolase Soluble epoxide hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.10 3.3.2.10] </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=4y2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y2r OCA], [https://pdbe.org/4y2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y2r RCSB], [https://www.ebi.ac.uk/pdbsum/4y2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y2r 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=4y2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y2r OCA], [http://pdbe.org/4y2r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y2r RCSB], [http://www.ebi.ac.uk/pdbsum/4y2r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y2r ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HYES_HUMAN HYES_HUMAN]] Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate.<ref>PMID:12574508</ref> <ref>PMID:12574510</ref>
+[https://www.uniprot.org/uniprot/HYES_HUMAN HYES_HUMAN] Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate.<ref>PMID:12574508</ref> <ref>PMID:12574510</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 21: @@
 ==See Also==
-*[[Epoxide hydrolase|Epoxide hydrolase]]
+*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Soluble epoxide hydrolase]]
+[[Category: Homo sapiens]]
-[[Category: Amano, Y]]
+[[Category: Large Structures]]
-[[Category: Yamaguchi, T]]
+[[Category: Amano Y]]
-[[Category: Hydrolase]]
+[[Category: Yamaguchi T]]
-[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]