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Open data
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Basic information
Entry | Database: PDB / ID: 1cqz | ||||||
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Title | CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE. | ||||||
![]() | EPOXIDE HYDROLASE | ||||||
![]() | HYDROLASE / HOMODIMER / ALPHA/BETA HYDROLASE FOLD / DOMAIN-SWAPPING | ||||||
Function / homology | ![]() prostaglandin production involved in inflammatory response / Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET) / Biosynthesis of maresins / lipid-phosphate phosphatase / 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity / stilbene catabolic process / phospholipid dephosphorylation / soluble epoxide hydrolase / epoxide metabolic process / lipid phosphatase activity ...prostaglandin production involved in inflammatory response / Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET) / Biosynthesis of maresins / lipid-phosphate phosphatase / 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity / stilbene catabolic process / phospholipid dephosphorylation / soluble epoxide hydrolase / epoxide metabolic process / lipid phosphatase activity / lysophosphatidic acid phosphatase activity / Peroxisomal protein import / linoleic acid metabolic process / positive regulation of blood pressure / epoxide hydrolase activity / regulation of cholesterol metabolic process / phosphatase activity / toxic substance binding / dephosphorylation / cholesterol homeostasis / response to toxic substance / peroxisome / positive regulation of gene expression / magnesium ion binding / protein homodimerization activity / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Argiriadi, M.A. / Morisseau, C. / Hammock, B.D. / Christianson, D.W. | ||||||
![]() | ![]() Title: Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase. Authors: Argiriadi, M.A. / Morisseau, C. / Hammock, B.D. / Christianson, D.W. #1: ![]() Title: Molecular cloning and expression of murine liver soluble epoxide hydrolase Authors: Grant, D.F. / Storms, D.H. / Hammock, B.D. #2: ![]() Title: Gene evolution of epoxide hydrolases and recommended nomenclature Authors: Beetham, J.K. / Grant, D. / Arand, M. / Garbarino, J. / Kiyosue, T. / Pinot, F. / Oesch, F. / Belknap, W.R. / Shinozaki, K. / Hammock, B.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 211.5 KB | Display | ![]() |
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PDB format | ![]() | 169.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 382.2 KB | Display | ![]() |
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Full document | ![]() | 459.7 KB | Display | |
Data in XML | ![]() | 29.8 KB | Display | |
Data in CIF | ![]() | 43.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 62582.039 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.72 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6 Details: ammonium sulfate, MES, ethanol, dithiothreitol, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | |||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: OTHER / Detector: CCD / Date: Jul 29, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.908 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→50 Å / Num. all: 30555 / Num. obs: 32278 / % possible obs: 99 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 9.4 % / Biso Wilson estimate: 55.5 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 12 |
Reflection shell | Resolution: 2.8→50 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.357 / Num. unique all: 3081 / % possible all: 96.7 |
Reflection | *PLUS Num. measured all: 304577 / Rmerge(I) obs: 0.07 |
Reflection shell | *PLUS % possible obs: 96.7 % |
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Processing
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Refinement | Resolution: 2.8→20 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.8→20 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / σ(F): 2 / % reflection Rfree: 5 % / Rfactor obs: 0.214 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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