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Yorodumi- PDB-3zp5: Crystal structure of the DNA binding ETS domain of the human prot... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3zp5 | ||||||
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Title | Crystal structure of the DNA binding ETS domain of the human protein FEV in complex with DNA | ||||||
Components |
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Keywords | TRANSCRIPTION/DNA / TRANSCRIPTION-DNA COMPLEX | ||||||
Function / homology | Function and homology information neuron fate specification / maternal behavior / neuron maturation / sequence-specific double-stranded DNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / DNA-binding transcription factor activity, RNA polymerase II-specific / nuclear speck / RNA polymerase II cis-regulatory region sequence-specific DNA binding / chromatin / positive regulation of gene expression ...neuron fate specification / maternal behavior / neuron maturation / sequence-specific double-stranded DNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / DNA-binding transcription factor activity, RNA polymerase II-specific / nuclear speck / RNA polymerase II cis-regulatory region sequence-specific DNA binding / chromatin / positive regulation of gene expression / regulation of transcription by RNA polymerase II / nucleus Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) SYNTHETIC CONSTRUCT (others) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Newman, J.A. / Cooper, C.D.O. / Krojer, T. / Shrestha, L. / Allerston, C.K. / Vollmar, M. / Arrowsmith, C.H. / Burgess-Brown, N. / Edwards, A. / von Delft, F. / Gileadi, O. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2015 Title: Structures of the Ets Domains of Transcription Factors Etv1, Etv4, Etv5 and Fev: Determinants of DNA Binding and Redox Regulation by Disulfide Bond Formation. Authors: Cooper, C.D.O. / Newman, J.A. / Aitkenhead, H. / Allerston, C.K. / Gileadi, O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3zp5.cif.gz | 78.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3zp5.ent.gz | 55.6 KB | Display | PDB format |
PDBx/mmJSON format | 3zp5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zp/3zp5 ftp://data.pdbj.org/pub/pdb/validation_reports/zp/3zp5 | HTTPS FTP |
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-Related structure data
Related structure data | 2yprSC 4avpC 4bncC 4co8C 4unoC 4uuvC S: Starting model for refinement C: citing same article (ref.) |
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Similar 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: 11813.431 Da / Num. of mol.: 1 / Fragment: ETS DOMAIN, RESIDUES 42-141 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q99581 |
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#2: DNA chain | Mass: 2995.967 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others) |
#3: DNA chain | Mass: 3094.042 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others) |
#4: Water | ChemComp-HOH / |
Sequence details | FIRST TWO RESIDUES ARE FROM PURIFICATI |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 45 % / Description: NONE |
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Crystal grow | Details: 25% PEG 3350, 0.1M BIS TRIS PH 5.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Dec 6, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2→110 Å / Num. obs: 12431 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / Redundancy: 3.9 % / Biso Wilson estimate: 38.52 Å2 / Rmerge(I) obs: 0.03 / Net I/σ(I): 23.6 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 4 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 3 / % possible all: 99.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2YPR Resolution: 2→30.976 Å / SU ML: 0.26 / σ(F): 1.34 / Phase error: 31.71 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 58.75 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→30.976 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -11.1284 Å / Origin y: -7.6218 Å / Origin z: -15.7403 Å
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Refinement TLS group | Selection details: ALL |