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Yorodumi- PDB-1y5r: The crystal structure of murine 11b-hydroxysteroid dehydrogenase ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1y5r | ||||||
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Title | The crystal structure of murine 11b-hydroxysteroid dehydrogenase complexed with corticosterone | ||||||
Components | Corticosteroid 11-beta-dehydrogenase, isozyme 1 | ||||||
Keywords | OXIDOREDUCTASE / corticosterone bound | ||||||
Function / homology | Function and homology information mineralocorticoid metabolic process / Glucocorticoid biosynthesis / glucocorticoid catabolic process / regulation of pentose-phosphate shunt / glucocorticoid biosynthetic process / 11beta-hydroxysteroid dehydrogenase / 11-beta-hydroxysteroid dehydrogenase (NADP+) activity / cortisol dehydrogenase activity / 7beta-hydroxysteroid dehydrogenase (NADP+) / 7-beta-hydroxysteroid dehydrogenase (NADP+) activity ...mineralocorticoid metabolic process / Glucocorticoid biosynthesis / glucocorticoid catabolic process / regulation of pentose-phosphate shunt / glucocorticoid biosynthetic process / 11beta-hydroxysteroid dehydrogenase / 11-beta-hydroxysteroid dehydrogenase (NADP+) activity / cortisol dehydrogenase activity / 7beta-hydroxysteroid dehydrogenase (NADP+) / 7-beta-hydroxysteroid dehydrogenase (NADP+) activity / Prednisone ADME / steroid catabolic process / steroid binding / lung development / apical part of cell / NADP binding / nuclear membrane / intracellular membrane-bounded organelle / endoplasmic reticulum membrane / protein homodimerization activity Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 3 Å | ||||||
Authors | Zhang, J. / Osslund, T.D. / Plant, M.H. / Clogston, C.L. / Nybo, R.E. / Xiong, F. / Delaney, J.M. / Jordan, S. | ||||||
Citation | Journal: Biochemistry / Year: 2005 Title: Crystal Structure of Murine 11-Hydroxysteroid Dehydrogenase 1: An Important Therapeutic Target for Diabetes Authors: Zhang, J. / Osslund, T.D. / Plant, M.H. / Clogston, C.L. / Nybo, R.E. / Xiong, F. / Delaney, J.M. / Jordan, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1y5r.cif.gz | 116.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1y5r.ent.gz | 92 KB | Display | PDB format |
PDBx/mmJSON format | 1y5r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y5/1y5r ftp://data.pdbj.org/pub/pdb/validation_reports/y5/1y5r | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 30585.680 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Hsd11b1 / Plasmid: pAMG21 / Production host: Escherichia coli (E. coli) / Strain (production host): GM221 References: UniProt: P50172, 11beta-hydroxysteroid dehydrogenase #2: Chemical | #3: Chemical | |
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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: 2.24 Å3/Da / Density % sol: 44.67 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 7.5 Details: 1.8M Li2SO4, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Sep 25, 2003 / Details: monochromator |
Radiation | Monochromator: Double-crystal, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3→40 Å / Num. all: 21330 / Num. obs: 21330 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.068 |
Reflection shell | Resolution: 3→3.11 Å / Rmerge(I) obs: 0.25 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: SIRAS / Resolution: 3→40 Å / Isotropic thermal model: anisotropic / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 3→40 Å
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Refine LS restraints |
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Xplor file |
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