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Yorodumi- PDB-4irg: Uninhibited DNA-binding domain of the Ets transcription factor ERG -
+Open data
-Basic information
Entry | Database: PDB / ID: 4irg | ||||||
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Title | Uninhibited DNA-binding domain of the Ets transcription factor ERG | ||||||
Components | Transcriptional regulator ERGERG (gene) | ||||||
Keywords | DNA BINDING PROTEIN / winged Helix-Turn-Helix / Ets domain | ||||||
Function / homology | Function and homology information sequence-specific double-stranded DNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / DNA-binding transcription factor activity, RNA polymerase II-specific / ribonucleoprotein complex / RNA polymerase II cis-regulatory region sequence-specific DNA binding / protein phosphorylation / chromatin binding / chromatin / regulation of transcription by RNA polymerase II / signal transduction ...sequence-specific double-stranded DNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / DNA-binding transcription factor activity, RNA polymerase II-specific / ribonucleoprotein complex / RNA polymerase II cis-regulatory region sequence-specific DNA binding / protein phosphorylation / chromatin binding / chromatin / regulation of transcription by RNA polymerase II / signal transduction / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Regan, M.C. / Horanyi, P.S. / Pryor, E.E. / Sarver, J.L. / Cafiso, D.S. / Bushweller, J.H. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2013 Title: Structural and dynamic studies of the transcription factor ERG reveal DNA binding is allosterically autoinhibited. Authors: Regan, M.C. / Horanyi, P.S. / Pryor, E.E. / Sarver, J.L. / Cafiso, D.S. / Bushweller, J.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4irg.cif.gz | 53.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4irg.ent.gz | 39 KB | Display | PDB format |
PDBx/mmJSON format | 4irg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ir/4irg ftp://data.pdbj.org/pub/pdb/validation_reports/ir/4irg | 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 12562.145 Da / Num. of mol.: 1 / Fragment: Ets Domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ERG / Production host: Escherichia coli (E. coli) / References: UniProt: P11308 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.81 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, sitting drop / pH: 4.5 Details: 1.4M Sodium Citrate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Dec 1, 2012 |
Radiation | Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→35.43 Å / Num. all: 12118 / Num. obs: 11537 |
Reflection shell | Resolution: 1.7→1.73 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.7→35.43 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.93 / SU B: 4.229 / SU ML: 0.069 / Cross valid method: THROUGHOUT / ESU R: 0.106 / ESU R Free: 0.107 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.615 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→35.43 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.747 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 3.2028 Å / Origin y: 12.9128 Å / Origin z: -6.1583 Å
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