5alh: Difference between revisions

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 <StructureSection load='5alh' size='340' side='right'caption='[[5alh]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5alh]] 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=5ALH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ALH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5alh]] 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=5ALH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ALH FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4UA:4-[[(2-METHOXY-5-METHYL-PHENYL)SULFONYLAMINO]METHYL]-4-PHENYL-N-(P-TOLYLMETHYL)PIPERIDINE-1-CARBOXAMIDE'>4UA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4UA:4-[[(2-METHOXY-5-METHYL-PHENYL)SULFONYLAMINO]METHYL]-4-PHENYL-N-(P-TOLYLMETHYL)PIPERIDINE-1-CARBOXAMIDE'>4UA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ak3|5ak3]], [[5ak4|5ak4]], [[5ak5|5ak5]], [[5ak6|5ak6]], [[5ake|5ake]], [[5akg|5akg]], [[5akh|5akh]], [[5aki|5aki]], [[5akj|5akj]], [[5akk|5akk]], [[5akl|5akl]], [[5akx|5akx]], [[5aky|5aky]], [[5akz|5akz]], [[5ald|5ald]], [[5ale|5ale]], [[5alf|5alf]], [[5alg|5alg]], [[5ali|5ali]], [[5alj|5alj]], [[5alk|5alk]], [[5all|5all]], [[5alm|5alm]], [[5aln|5aln]], [[5alo|5alo]], [[5alp|5alp]], [[5alq|5alq]], [[5alr|5alr]], [[5als|5als]], [[5alt|5alt]], [[5alu|5alu]], [[5alv|5alv]], [[5alw|5alw]], [[5alx|5alx]], [[5aly|5aly]], [[5alz|5alz]], [[5am0|5am0]], [[5am1|5am1]], [[5am2|5am2]], [[5am3|5am3]], [[5am4|5am4]], [[5am5|5am5]]</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=5alh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5alh OCA], [https://pdbe.org/5alh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5alh RCSB], [https://www.ebi.ac.uk/pdbsum/5alh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5alh 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=5alh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5alh OCA], [http://pdbe.org/5alh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5alh RCSB], [http://www.ebi.ac.uk/pdbsum/5alh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5alh 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 ==
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 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Kack, H]]
+[[Category: Kack H]]
-[[Category: Oster, L]]
+[[Category: Oster L]]
-[[Category: Tapani, S]]
+[[Category: Tapani S]]
-[[Category: Xue, Y]]
+[[Category: Xue Y]]
-[[Category: Hydrolase]]