3wkc: Difference between revisions

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 ==Crystal structure of soluble epoxide hydrolase in complex with fragment inhibitor==
-<StructureSection load='3wkc' size='340' side='right' caption='[[3wkc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='3wkc' size='340' side='right'caption='[[3wkc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3wkc]] is a 1 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=3WKC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WKC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3wkc]] 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=3WKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WKC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=S0J:4-{2,5-DIMETHYL-1-[(2R)-TETRAHYDROFURAN-2-YLMETHYL]-1H-PYRROL-3-YL}-1,3-THIAZOL-2-AMINE'>S0J</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]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wk4|3wk4]], [[3wk5|3wk5]], [[3wk6|3wk6]], [[3wk7|3wk7]], [[3wk8|3wk8]], [[3wk9|3wk9]], [[3wka|3wka]], [[3wkb|3wkb]], [[3wkd|3wkd]], [[3wke|3wke]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=S0J:4-{2,5-DIMETHYL-1-[(2R)-TETRAHYDROFURAN-2-YLMETHYL]-1H-PYRROL-3-YL}-1,3-THIAZOL-2-AMINE'>S0J</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EPHX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3wkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wkc OCA], [https://pdbe.org/3wkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wkc RCSB], [https://www.ebi.ac.uk/pdbsum/3wkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wkc 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=3wkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wkc OCA], [http://pdbe.org/3wkc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wkc RCSB], [http://www.ebi.ac.uk/pdbsum/3wkc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wkc 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: Human]]
+[[Category: Homo sapiens]]
-[[Category: Amano, Y]]
+[[Category: Large Structures]]
-[[Category: Tanabe, E]]
+[[Category: Amano Y]]
-[[Category: Yamaguchi, T]]
+[[Category: Tanabe E]]
-[[Category: Hydrolase]]
+[[Category: Yamaguchi T]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]