5ai4

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==ligand complex structure of soluble epoxide hydrolase==
==ligand complex structure of soluble epoxide hydrolase==
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<StructureSection load='5ai4' size='340' side='right' caption='[[5ai4]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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<StructureSection load='5ai4' size='340' side='right'caption='[[5ai4]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ai4]] 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=5AI4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AI4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ai4]] 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=5AI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AI4 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=4VY:2-[(5-BROMO-2-PYRIDYL)-METHYL-AMINO]ETHANOL'>4VY</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ahx|5ahx]], [[5ai0|5ai0]], [[5ai5|5ai5]], [[5ai6|5ai6]], [[5ai8|5ai8]], [[5ai9|5ai9]], [[5aia|5aia]], [[5aib|5aib]], [[5aic|5aic]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4VY:2-[(5-BROMO-2-PYRIDYL)-METHYL-AMINO]ETHANOL'>4VY</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ai4 OCA], [http://pdbe.org/5ai4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ai4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ai4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ai4 ProSAT]</span></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=5ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ai4 OCA], [https://pdbe.org/5ai4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ai4 RCSB], [https://www.ebi.ac.uk/pdbsum/5ai4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ai4 ProSAT]</span></td></tr>
</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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</div>
</div>
<div class="pdbe-citations 5ai4" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5ai4" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Kack, H]]
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[[Category: Large Structures]]
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[[Category: Oster, L]]
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[[Category: Kack H]]
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[[Category: Tapani, S]]
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[[Category: Oster L]]
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[[Category: Xue, Y]]
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[[Category: Tapani S]]
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[[Category: Hydrolase]]
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[[Category: Xue Y]]

Current revision

ligand complex structure of soluble epoxide hydrolase

PDB ID 5ai4

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