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Yorodumi- PDB-2e4j: Solution Structure of mouse Lipocalin-type Prostaglandin D Synthase -
+Open data
-Basic information
Entry | Database: PDB / ID: 2e4j | ||||||
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Title | Solution Structure of mouse Lipocalin-type Prostaglandin D Synthase | ||||||
Components | Prostaglandin-H2 D-isomerase | ||||||
Keywords | ISOMERASE / PGDS | ||||||
Function / homology | Function and homology information prostaglandin-D synthase / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / prostaglandin-D synthase activity / negative regulation of male germ cell proliferation / regulation of circadian sleep/wake cycle, sleep / retinoid binding / prostaglandin biosynthetic process / mast cell degranulation / response to glucocorticoid / rough endoplasmic reticulum ...prostaglandin-D synthase / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / prostaglandin-D synthase activity / negative regulation of male germ cell proliferation / regulation of circadian sleep/wake cycle, sleep / retinoid binding / prostaglandin biosynthetic process / mast cell degranulation / response to glucocorticoid / rough endoplasmic reticulum / fatty acid binding / gene expression / nuclear membrane / perinuclear region of cytoplasm / Golgi apparatus / extracellular space / extracellular region / nucleoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING, TORSION ANGLE DYNAMICS | ||||||
Authors | Shimamoto, S. / Ohkubo, T. | ||||||
Citation | Journal: to be published Title: Solution Structure of mouse Lipocalin-type Prostaglandin D Synthase Authors: Shimamoto, S. / Ohkubo, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2e4j.cif.gz | 724.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2e4j.ent.gz | 593.3 KB | Display | PDB format |
PDBx/mmJSON format | 2e4j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2e4j_validation.pdf.gz | 346.7 KB | Display | wwPDB validaton report |
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Full document | 2e4j_full_validation.pdf.gz | 491.9 KB | Display | |
Data in XML | 2e4j_validation.xml.gz | 59.1 KB | Display | |
Data in CIF | 2e4j_validation.cif.gz | 76.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e4/2e4j ftp://data.pdbj.org/pub/pdb/validation_reports/e4/2e4j | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 18585.795 Da / Num. of mol.: 1 / Mutation: C89A, C186A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pGX-2T / Production host: Escherichia coli (E. coli) / References: UniProt: O09114, prostaglandin-D synthase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 300mM NACL / pH: 6.5 / Pressure: AMBIENT / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software | Name: CNS / Version: 1.1 / Classification: refinement |
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Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING, TORSION ANGLE DYNAMICS Software ordinal: 1 |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 30 / Conformers submitted total number: 15 |