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5alj

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<StructureSection load='5alj' size='340' side='right'caption='[[5alj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5alj' size='340' side='right'caption='[[5alj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5alj]] 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=5ALJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ALJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5alj]] 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=5ALJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ALJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=T5J:2-(3-FLUORO-4-METHYL-ANILINO)-4-METHYL-QUINOLIN-5-OL'>T5J</scene></td></tr>
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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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=T5J:2-(3-FLUORO-4-METHYL-ANILINO)-4-METHYL-QUINOLIN-5-OL'>T5J</scene></td></tr>
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<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]], [[5alh|5alh]], [[5ali|5ali]], [[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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5alj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5alj OCA], [https://pdbe.org/5alj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5alj RCSB], [https://www.ebi.ac.uk/pdbsum/5alj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5alj ProSAT]</span></td></tr>
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<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=5alj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5alj OCA], [http://pdbe.org/5alj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5alj RCSB], [http://www.ebi.ac.uk/pdbsum/5alj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5alj ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kack, H]]
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[[Category: Kack H]]
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[[Category: Oster, L]]
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[[Category: Oster L]]
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[[Category: Tapani, S]]
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[[Category: Tapani S]]
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[[Category: Xue, Y]]
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[[Category: Xue Y]]
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[[Category: Hydrolase]]
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Revision as of 06:13, 31 May 2023

ligand complex structure of soluble epoxide hydrolase

PDB ID 5alj

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