+Open data
-Basic information
Entry | Database: PDB / ID: 3otq | ||||||
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Title | Soluble Epoxide Hydrolase in complex with pyrazole antagonist | ||||||
Components | Epoxide hydrolase 2 | ||||||
Keywords | HYDROLASE / epoxide hydrolase | ||||||
Function / homology | Function and homology information lipid-phosphate phosphatase / 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity / stilbene catabolic process / phospholipid dephosphorylation / lipid phosphatase activity / epoxide metabolic process / Biosynthesis of maresins / soluble epoxide hydrolase / lysophosphatidic acid phosphatase activity / Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET) ...lipid-phosphate phosphatase / 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity / stilbene catabolic process / phospholipid dephosphorylation / lipid phosphatase activity / epoxide metabolic process / Biosynthesis of maresins / soluble epoxide hydrolase / lysophosphatidic acid phosphatase activity / Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET) / epoxide hydrolase activity / regulation of cholesterol metabolic process / phosphatase activity / peroxisomal matrix / toxic substance binding / dephosphorylation / cholesterol homeostasis / Peroxisomal protein import / response to toxic substance / peroxisome / positive regulation of gene expression / magnesium ion binding / protein homodimerization activity / extracellular exosome / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Farrow, N.A. | ||||||
Citation | Journal: Bioorg.Med.Chem.Lett. / Year: 2010 Title: Substituted pyrazoles as novel sEH antagonist: investigation of key binding interactions within the catalytic domain. Authors: Lo, H.Y. / Man, C.C. / Fleck, R.W. / Farrow, N.A. / Ingraham, R.H. / Kukulka, A. / Proudfoot, J.R. / Betageri, R. / Kirrane, T. / Patel, U. / Sharma, R. / Hoermann, M.A. / Kabcenell, A. / Lombaert, S.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3otq.cif.gz | 109.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3otq.ent.gz | 87.2 KB | Display | PDB format |
PDBx/mmJSON format | 3otq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ot/3otq ftp://data.pdbj.org/pub/pdb/validation_reports/ot/3otq | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 62685.617 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EPHX2 / Production host: Escherichia coli (E. coli) / References: UniProt: P34913, soluble epoxide hydrolase |
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#2: Chemical | ChemComp-MZL / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.43 Å3/Da / Density % sol: 49.29 % |
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-Data collection
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH3R |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 3→50 Å / Num. obs: 12861 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3→50 Å
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Refinement step | Cycle: LAST / Resolution: 3→50 Å
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