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5akl

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ligand complex structure of soluble epoxide hydrolase

Structural highlights

5akl is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
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]

Publication Abstract from PubMed

Fragment-based drug discovery relies upon structural information for efficient compound progression, yet it is often challenging to generate structures with bound fragments. A summary of recent literature reveals that a wide repertoire of experimental procedures is employed to generate ligand-bound crystal structures successfully. We share in-house experience from setting up and executing fragment crystallography in a project that resulted in 55 complex structures. The ligands span five orders of magnitude in affinity and the resulting structures are made available to be of use, for example, for development of computational methods. Analysis of the results revealed that ligand properties such as potency, ligand efficiency (LE) and, to some degree, clogP influence the success of complex structure generation.

Successful generation of structural information for fragment-based drug discovery.,Oster L, Tapani S, Xue Y, Kack H Drug Discov Today. 2015 Apr 28. pii: S1359-6446(15)00154-3. doi:, 10.1016/j.drudis.2015.04.005. PMID:25931264^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Oster L, Tapani S, Xue Y, Kack H. Successful generation of structural information for fragment-based drug discovery. Drug Discov Today. 2015 Apr 28. pii: S1359-6446(15)00154-3. doi:, 10.1016/j.drudis.2015.04.005. PMID:25931264 doi:http://dx.doi.org/10.1016/j.drudis.2015.04.005

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5akl"

@@ Line 3: / Line 3: @@
 <StructureSection load='5akl' size='340' side='right'caption='[[5akl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5akl]] 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=5AKL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AKL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5akl]] 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=5AKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AKL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6N8:N-(3,3-DIPHENYLPROPYL)PYRROLIDINE-1-CARBOXAMIDE'>6N8</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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&#8491;</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]], [[5akx|5akx]], [[5aky|5aky]], [[5akz|5akz]], [[5ald|5ald]], [[5ale|5ale]], [[5alf|5alf]], [[5alg|5alg]], [[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>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6N8:N-(3,3-DIPHENYLPROPYL)PYRROLIDINE-1-CARBOXAMIDE'>6N8</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5akl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5akl OCA], [http://pdbe.org/5akl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5akl RCSB], [http://www.ebi.ac.uk/pdbsum/5akl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5akl ProSAT]</span></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=5akl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5akl OCA], [https://pdbe.org/5akl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5akl RCSB], [https://www.ebi.ac.uk/pdbsum/5akl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5akl 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 ==
@@ Line 26: / Line 26: @@
 __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]]

5akl

From Proteopedia

Current revision

ligand complex structure of soluble epoxide hydrolase

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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