+Open data
-Basic information
Entry | Database: PDB / ID: 5ego | ||||||
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Title | HOXB13-MEIS1 heterodimer bound to methylated DNA | ||||||
Components |
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Keywords | TRANSCRIPTION / transcription factor / heterodimer / complex / bound to DNA | ||||||
Function / homology | Function and homology information epithelial cell maturation involved in prostate gland development / cell growth involved in cardiac muscle cell development / negative regulation of myeloid cell differentiation / lens morphogenesis in camera-type eye / eye development / embryonic pattern specification / methyl-CpG binding / definitive hemopoiesis / regulation of growth / megakaryocyte development ...epithelial cell maturation involved in prostate gland development / cell growth involved in cardiac muscle cell development / negative regulation of myeloid cell differentiation / lens morphogenesis in camera-type eye / eye development / embryonic pattern specification / methyl-CpG binding / definitive hemopoiesis / regulation of growth / megakaryocyte development / response to testosterone / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / hemopoiesis / negative regulation of neuron differentiation / epidermis development / locomotory behavior / animal organ morphogenesis / brain development / DNA-binding transcription repressor activity, RNA polymerase II-specific / response to wounding / Activation of anterior HOX genes in hindbrain development during early embryogenesis / sequence-specific double-stranded DNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / angiogenesis / transcription regulator complex / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / chromatin binding / positive regulation of cell population proliferation / chromatin / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) synthetic construct (others) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.54 Å | ||||||
Authors | Morgunova, E. / Yin, Y. / Jolma, A. / Popov, A. / Taipale, J. | ||||||
Citation | Journal: Science / Year: 2017 Title: Impact of cytosine methylation on DNA binding specificities of human transcription factors. Authors: Yin, Y. / Morgunova, E. / Jolma, A. / Kaasinen, E. / Sahu, B. / Khund-Sayeed, S. / Das, P.K. / Kivioja, T. / Dave, K. / Zhong, F. / Nitta, K.R. / Taipale, M. / Popov, A. / Ginno, P.A. / ...Authors: Yin, Y. / Morgunova, E. / Jolma, A. / Kaasinen, E. / Sahu, B. / Khund-Sayeed, S. / Das, P.K. / Kivioja, T. / Dave, K. / Zhong, F. / Nitta, K.R. / Taipale, M. / Popov, A. / Ginno, P.A. / Domcke, S. / Yan, J. / Schubeler, D. / Vinson, C. / Taipale, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ego.cif.gz | 61.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ego.ent.gz | 40.9 KB | Display | PDB format |
PDBx/mmJSON format | 5ego.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eg/5ego ftp://data.pdbj.org/pub/pdb/validation_reports/eg/5ego | HTTPS FTP |
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-Related structure data
Related structure data | 5ef6C 5hodC 5ltyC 5luxC 4xrmS 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: 6756.834 Da / Num. of mol.: 1 / Fragment: UNP residues 279-333 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MEIS1 / Plasmid: pETG20A / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta / References: UniProt: O00470 |
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#2: DNA chain | Mass: 5600.653 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
#3: DNA chain | Mass: 5458.584 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
#4: Protein | Mass: 7640.061 Da / Num. of mol.: 1 / Fragment: UNP residues 217-277 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HOXB13 / Plasmid: pETG20A / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta / References: UniProt: Q92826 |
#5: 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: 2.35 Å3/Da / Density % sol: 47.72 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8 Details: PEG 5000, potassium chloride, magnesium chloride, Tris, PEG 400 PH range: 8 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.984 Å |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: May 25, 2015 |
Radiation | Monochromator: Si(111) and Si (311) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.984 Å / Relative weight: 1 |
Reflection | Resolution: 2.54→40 Å / Num. obs: 8290 / % possible obs: 98.7 % / Redundancy: 4.2 % / Rmerge(I) obs: 0.048 / Net I/σ(I): 15.5 |
Reflection shell | Resolution: 2.54→2.63 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.761 / Mean I/σ(I) obs: 1.6 / % possible all: 98.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4XRM Resolution: 2.54→38.544 Å / SU ML: 0.51 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 35.45 / 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 max: 164.57 Å2 / Biso mean: 70.1019 Å2 / Biso min: 49.36 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.54→38.544 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5401→2.9076 Å
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