6hgw: Difference between revisions

Latest revision as of 08:48, 7 August 2019

Soluble epoxide hydrolase in complex with 2-(4-fluorophenyl)-N-(4-phenoxybenzyl)ethanamineSoluble epoxide hydrolase in complex with 2-(4-fluorophenyl)-N-(4-phenoxybenzyl)ethanamine

Structural highlights

6hgw is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

References

↑ Cronin A, Mowbray S, Durk H, Homburg S, Fleming I, Fisslthaler B, Oesch F, Arand M. The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1552-7. Epub 2003 Feb 6. PMID:12574508 doi:10.1073/pnas.0437829100
↑ Newman JW, Morisseau C, Harris TR, Hammock BD. The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1558-63. Epub 2003 Feb 6. PMID:12574510 doi:10.1073/pnas.0437724100

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OCA

[1] Cronin A, Mowbray S, Durk H, Homburg S, Fleming I, Fisslthaler B, Oesch F, Arand M. The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1552-7. Epub 2003 Feb 6. PMID:12574508 doi:10.1073/pnas.0437829100

[2] Newman JW, Morisseau C, Harris TR, Hammock BD. The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1558-63. Epub 2003 Feb 6. PMID:12574510 doi:10.1073/pnas.0437724100

[1]

[2]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6hgw is ON HOLD
+==Soluble epoxide hydrolase in complex with 2-(4-fluorophenyl)-N-(4-phenoxybenzyl)ethanamine==
+<StructureSection load='6hgw' size='340' side='right'caption='[[6hgw]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
-Authors: Kramer, J.S., Pogoryelov, D., Hiesinger, K., Proschak, E.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6hgw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HGW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HGW FirstGlance]. <br>
-Description: Soluble epoxide hydrolase in complex with 2-(4-fluorophenyl)-N-(4-phenoxybenzyl)ethanamine
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G3W:2-(4-fluorophenyl)-~{N}-[(4-phenoxyphenyl)methyl]ethanamine'>G3W</scene></td></tr>
-[[Category: Unreleased Structures]]
+<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=6hgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hgw OCA], [http://pdbe.org/6hgw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hgw RCSB], [http://www.ebi.ac.uk/pdbsum/6hgw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hgw ProSAT]</span></td></tr>
-[[Category: Proschak, E]]
+</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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Hiesinger, K]]
+[[Category: Kramer, J S]]
 [[Category: Pogoryelov, D]]
-[[Category: Kramer, J.S]]
+[[Category: Proschak, E]]
+[[Category: Complex]]
+[[Category: Hydrolase]]
+[[Category: Inhibitor]]
+[[Category: Seh]]

6hgw: Difference between revisions

Latest revision as of 08:48, 7 August 2019

Soluble epoxide hydrolase in complex with 2-(4-fluorophenyl)-N-(4-phenoxybenzyl)ethanamineSoluble epoxide hydrolase in complex with 2-(4-fluorophenyl)-N-(4-phenoxybenzyl)ethanamine

Structural highlights

Function

References

Contents

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6hgw: Difference between revisions

Latest revision as of 08:48, 7 August 2019

Soluble epoxide hydrolase in complex with 2-(4-fluorophenyl)-N-(4-phenoxybenzyl)ethanamineSoluble epoxide hydrolase in complex with 2-(4-fluorophenyl)-N-(4-phenoxybenzyl)ethanamine

Structural highlights

Function

References

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