+Open data
-Basic information
Entry | Database: PDB / ID: 1cqz | ||||||
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Title | CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE. | ||||||
Components | EPOXIDE HYDROLASE | ||||||
Keywords | HYDROLASE / HOMODIMER / ALPHA/BETA HYDROLASE FOLD / DOMAIN-SWAPPING | ||||||
Function / homology | Function and homology information 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 / lipid phosphatase activity / epoxide metabolic process / soluble epoxide hydrolase ...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 / lipid phosphatase activity / epoxide metabolic process / soluble epoxide hydrolase / lysophosphatidic acid phosphatase activity / Peroxisomal protein import / positive regulation of blood pressure / linoleic acid metabolic process / 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 | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.8 Å | ||||||
Authors | Argiriadi, M.A. / Morisseau, C. / Hammock, B.D. / Christianson, D.W. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1999 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: Journal: J.Biol.Chem. / Year: 1993 Title: Molecular cloning and expression of murine liver soluble epoxide hydrolase Authors: Grant, D.F. / Storms, D.H. / Hammock, B.D. #2: Journal: DNA Cell Biol. / Year: 1995 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cqz.cif.gz | 211.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cqz.ent.gz | 169.7 KB | Display | PDB format |
PDBx/mmJSON format | 1cqz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cq/1cqz ftp://data.pdbj.org/pub/pdb/validation_reports/cq/1cqz | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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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.) Mus musculus (house mouse) / Organ: LIVER / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P34914, epoxide hydrolase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.908 |
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 % |
-Processing
Software |
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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: X-PLOR / Version: 3.851 / Classification: refinement | |||||||||||||||||||||||||
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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