+Open data
-Basic information
Entry | Database: PDB / ID: 4c5i | ||||||
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Title | Crystal structure of MBTD1 YY1 complex | ||||||
Components |
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Keywords | TRANSCRIPTION | ||||||
Function / homology | Function and homology information NuA4 histone acetyltransferase complex binding / response to prostaglandin F / RNA localization / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / embryonic skeletal system development / negative regulation of cell growth involved in cardiac muscle cell development / PcG protein complex / camera-type eye morphogenesis / regulation of double-strand break repair ...NuA4 histone acetyltransferase complex binding / response to prostaglandin F / RNA localization / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / embryonic skeletal system development / negative regulation of cell growth involved in cardiac muscle cell development / PcG protein complex / camera-type eye morphogenesis / regulation of double-strand break repair / Ino80 complex / chromatin silencing complex / negative regulation of interferon-beta production / response to UV-C / NuA4 histone acetyltransferase complex / anterior/posterior pattern specification / regulation of chromosome organization / DNA-binding transcription repressor activity / immunoglobulin heavy chain V-D-J recombination / positive regulation of double-strand break repair via homologous recombination / SMAD binding / regulation of DNA replication / regulation of embryonic development / regulation of DNA repair / cellular response to interleukin-1 / cis-regulatory region sequence-specific DNA binding / four-way junction DNA binding / methylated histone binding / positive regulation of DNA repair / telomere maintenance / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / B cell differentiation / negative regulation of miRNA transcription / double-strand break repair via homologous recombination / DNA Damage Recognition in GG-NER / nuclear matrix / DNA-binding transcription repressor activity, RNA polymerase II-specific / Activation of anterior HOX genes in hindbrain development during early embryogenesis / UCH proteinases / cellular response to UV / nucleosome / sequence-specific double-stranded DNA binding / site of double-strand break / chromatin organization / spermatogenesis / DNA-binding transcription activator activity, RNA polymerase II-specific / regulation of apoptotic process / DNA-binding transcription factor binding / Estrogen-dependent gene expression / transcription regulator complex / transcription cis-regulatory region binding / regulation of cell cycle / DNA-binding transcription factor activity, RNA polymerase II-specific / chromatin remodeling / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of gene expression / negative regulation of DNA-templated transcription / DNA damage response / chromatin binding / positive regulation of gene expression / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.586 Å | ||||||
Authors | Alfieri, C. / Glatt, S. / Mueller, C.W. | ||||||
Citation | Journal: Genes Dev. / Year: 2013 Title: Structural Basis for Targeting the Chromatin Repressor Sfmbt to Polycomb Response Elements Authors: Alfieri, C. / Gambetta, M.C. / Matos, R. / Glatt, S. / Sehr, P. / Fraterman, S. / Wilm, M. / Mueller, J. / Mueller, C.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4c5i.cif.gz | 181.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4c5i.ent.gz | 143.4 KB | Display | PDB format |
PDBx/mmJSON format | 4c5i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c5/4c5i ftp://data.pdbj.org/pub/pdb/validation_reports/c5/4c5i | HTTPS FTP |
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-Related structure data
Related structure data | 4c5eC 4c5gC 4c5hC 3feoS C: citing same article (ref.) S: Starting model for refinement |
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Similar 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: 49825.051 Da / Num. of mol.: 2 / Fragment: 4MBT, RESIDUES 130-566 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): GOLD / References: UniProt: Q05BQ5 #2: Protein/peptide | | Mass: 3529.880 Da / Num. of mol.: 1 / Fragment: SPACER, RESIDUES 199-228 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P25490 #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 52.4 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.93432 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Feb 3, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93432 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→2.65 Å / Num. obs: 31789 / % possible obs: 99.2 % / Observed criterion σ(I): 1.5 / Redundancy: 3.6 % / Rmerge(I) obs: 0.16 / Net I/σ(I): 8.7 |
Reflection shell | Resolution: 2.6→2.65 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.98 / Mean I/σ(I) obs: 1.5 / % possible all: 97.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3FEO Resolution: 2.586→48.807 Å / SU ML: 0.32 / σ(F): 1.35 / Phase error: 24.48 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.586→48.807 Å
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Refine LS restraints |
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LS refinement shell |
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