5alg

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==ligand complex structure of soluble epoxide hydrolase==
==ligand complex structure of soluble epoxide hydrolase==
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<StructureSection load='5alg' size='340' side='right' caption='[[5alg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='5alg' size='340' side='right'caption='[[5alg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5alg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ALG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ALG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5alg]] 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=5ALG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ALG 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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=R4N:4-[(3-CHLOROPHENYL)METHYL]-N-[[(3S)-2,3-DIHYDRO-1,4-BENZODIOXIN-3-YL]METHYL]-3-OXIDANYLIDENE-1,4-BENZOTHIAZINE-6-CARBOXAMIDE'>R4N</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.4&#8491;</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]], [[5alh|5alh]], [[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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=R4N:4-[(3-CHLOROPHENYL)METHYL]-N-[[(3S)-2,3-DIHYDRO-1,4-BENZODIOXIN-3-YL]METHYL]-3-OXIDANYLIDENE-1,4-BENZOTHIAZINE-6-CARBOXAMIDE'>R4N</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5alg OCA], [http://pdbe.org/5alg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5alg RCSB], [http://www.ebi.ac.uk/pdbsum/5alg PDBsum]</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=5alg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5alg OCA], [https://pdbe.org/5alg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5alg RCSB], [https://www.ebi.ac.uk/pdbsum/5alg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5alg 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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==See Also==
==See Also==
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*[[Epoxide hydrolase|Epoxide hydrolase]]
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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: Kack, H]]
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[[Category: Homo sapiens]]
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[[Category: Oster, L]]
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[[Category: Large Structures]]
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[[Category: Tapani, S]]
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[[Category: Kack H]]
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[[Category: Xue, Y]]
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[[Category: Oster L]]
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[[Category: Hydrolase]]
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[[Category: Tapani S]]
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[[Category: Xue Y]]

Current revision

ligand complex structure of soluble epoxide hydrolase

PDB ID 5alg

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