4c4y: Difference between revisions

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 ==Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A4==
-<StructureSection load='4c4y' size='340' side='right' caption='[[4c4y]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
+<StructureSection load='4c4y' size='340' side='right'caption='[[4c4y]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4c4y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4c4y]] 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=4C4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4Y FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7WI:1-(3-CHLOROPHENYL)-3-(2-METHOXYETHYL)UREA'>7WI</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]] 2.41&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c4x|4c4x]], [[4c4z|4c4z]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7WI:1-(3-CHLOROPHENYL)-3-(2-METHOXYETHYL)UREA'>7WI</scene></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=4c4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4y OCA], [http://pdbe.org/4c4y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c4y RCSB], [http://www.ebi.ac.uk/pdbsum/4c4y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4y 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=4c4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4y OCA], [https://pdbe.org/4c4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4y RCSB], [https://www.ebi.ac.uk/pdbsum/4c4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4y 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 21: / Line 21: @@
 ==See Also==
-*[[Epoxide hydrolase|Epoxide hydrolase]]
+*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Becker, S]]
+[[Category: Homo sapiens]]
-[[Category: Elshorst, B]]
+[[Category: Large Structures]]
-[[Category: Griesinger, C]]
+[[Category: Becker S]]
-[[Category: Hessler, G]]
+[[Category: Elshorst B]]
-[[Category: Krimm, I]]
+[[Category: Griesinger C]]
-[[Category: Langer, T]]
+[[Category: Hessler G]]
-[[Category: Lee, D]]
+[[Category: Krimm I]]
-[[Category: Mazur, A]]
+[[Category: Langer T]]
-[[Category: Monecke, P]]
+[[Category: Lee D]]
-[[Category: Pilger, J]]
+[[Category: Mazur A]]
-[[Category: Schiffer, A]]
+[[Category: Monecke P]]
-[[Category: Schreuder, H]]
+[[Category: Pilger J]]
-[[Category: Wegstroth, M]]
+[[Category: Schiffer A]]
-[[Category: Wendt, K U]]
+[[Category: Schreuder H]]
-[[Category: Drug design]]
+[[Category: Wegstroth M]]
-[[Category: Hydrolase]]
+[[Category: Wendt K-U]]