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4c4y

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Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A4

Structural highlights

4c4y 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 2.41Å
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

Structure-based drug design (SBDD) is a powerful and widely used approach to optimize affinity of drug candidates. With the recently introduced INPHARMA method, the binding mode of small molecules to their protein target can be characterized even if no spectroscopic information about the protein is known. Here, we show that the combination of the spin-diffusion-based NMR methods INPHARMA, trNOE, and STD results in an accurate scoring function for docking modes and therefore determination of protein-ligand complex structures. Applications are shown on the model system protein kinase A and the drug targets glycogen phosphorylase and soluble epoxide hydrolase (sEH). Multiplexing of several ligands improves the reliability of the scoring function further. The new score allows in the case of sEH detecting two binding modes of the ligand in its binding site, which was corroborated by X-ray analysis.

A Combination of Spin Diffusion Methods for the Determination of Protein-Ligand Complex Structural Ensembles.,Pilger J, Mazur A, Monecke P, Schreuder H, Elshorst B, Bartoschek S, Langer T, Schiffer A, Krimm I, Wegstroth M, Lee D, Hessler G, Wendt KU, Becker S, Griesinger C Angew Chem Int Ed Engl. 2015 Apr 15. doi: 10.1002/anie.201500671. PMID:25877959^[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
↑ Pilger J, Mazur A, Monecke P, Schreuder H, Elshorst B, Bartoschek S, Langer T, Schiffer A, Krimm I, Wegstroth M, Lee D, Hessler G, Wendt KU, Becker S, Griesinger C. A Combination of Spin Diffusion Methods for the Determination of Protein-Ligand Complex Structural Ensembles. Angew Chem Int Ed Engl. 2015 Apr 15. doi: 10.1002/anie.201500671. PMID:25877959 doi:http://dx.doi.org/10.1002/anie.201500671

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/4c4y"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A4==
-<StructureSection load='4c4y' size='340' side='right' caption='[[4c4y]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
+<StructureSection load='4c4y' size='340' side='right'caption='[[4c4y]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4c4y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4c4y]] 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=4C4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4Y FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7WI:1-(3-CHLOROPHENYL)-3-(2-METHOXYETHYL)UREA'>7WI</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]] 2.41&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c4x|4c4x]], [[4c4z|4c4z]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7WI:1-(3-CHLOROPHENYL)-3-(2-METHOXYETHYL)UREA'>7WI</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=4c4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4y RCSB], [http://www.ebi.ac.uk/pdbsum/4c4y PDBsum]</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=4c4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4y OCA], [https://pdbe.org/4c4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4y RCSB], [https://www.ebi.ac.uk/pdbsum/4c4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4y 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 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4c4y" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Becker, S]]
+[[Category: Homo sapiens]]
-[[Category: Elshorst, B]]
+[[Category: Large Structures]]
-[[Category: Griesinger, C]]
+[[Category: Becker S]]
-[[Category: Hessler, G]]
+[[Category: Elshorst B]]
-[[Category: Krimm, I]]
+[[Category: Griesinger C]]
-[[Category: Langer, T]]
+[[Category: Hessler G]]
-[[Category: Lee, D]]
+[[Category: Krimm I]]
-[[Category: Mazur, A]]
+[[Category: Langer T]]
-[[Category: Monecke, P]]
+[[Category: Lee D]]
-[[Category: Pilger, J]]
+[[Category: Mazur A]]
-[[Category: Schiffer, A]]
+[[Category: Monecke P]]
-[[Category: Schreuder, H]]
+[[Category: Pilger J]]
-[[Category: Wegstroth, M]]
+[[Category: Schiffer A]]
-[[Category: Wendt, K U]]
+[[Category: Schreuder H]]
-[[Category: Drug design]]
+[[Category: Wegstroth M]]
-[[Category: Hydrolase]]
+[[Category: Wendt K-U]]

4c4y

From Proteopedia

Current revision

Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A4

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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