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Open data
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Basic information
Entry | Database: PDB / ID: 3g7l | ||||||
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Title | Chromodomain of Chp1 in complex with Histone H3K9me3 peptide | ||||||
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![]() | NUCLEAR PROTEIN / chromodomain / protein-peptide complex / silencing / Cell cycle / Chromosome partition / DNA-binding / Nucleus / RNA-mediated gene silencing / Acetylation / Chromosomal protein / DNA damage / DNA repair / Methylation / Nucleosome core / Phosphoprotein | ||||||
Function / homology | ![]() Assembly of the ORC complex at the origin of replication / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / nucleolar peripheral inclusion body / RITS complex / Oxidative Stress Induced Senescence / Factors involved in megakaryocyte development and platelet production / Estrogen-dependent gene expression / RNA Polymerase I Promoter Escape ...Assembly of the ORC complex at the origin of replication / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / nucleolar peripheral inclusion body / RITS complex / Oxidative Stress Induced Senescence / Factors involved in megakaryocyte development and platelet production / Estrogen-dependent gene expression / RNA Polymerase I Promoter Escape / regulatory ncRNA-mediated heterochromatin formation / Transcriptional regulation by small RNAs / mating-type region heterochromatin / heterochromatin island / heterochromatin boundary formation / mitotic sister chromatid biorientation / siRNA-mediated pericentric heterochromatin formation / chromosome, subtelomeric region / chromatin-protein adaptor activity / spindle pole body / rRNA transcription / subtelomeric heterochromatin formation / heterochromatin / pericentric heterochromatin / methylated histone binding / histone reader activity / chromosome segregation / structural constituent of chromatin / nucleosome / chromatin organization / histone binding / single-stranded RNA binding / protein heterodimerization activity / DNA damage response / chromatin binding / negative regulation of transcription by RNA polymerase II / DNA binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Schalch, T. / Joshua-Tor, L. | ||||||
![]() | ![]() Title: High-affinity binding of Chp1 chromodomain to K9 methylated histone H3 is required to establish centromeric heterochromatin Authors: Schalch, T. / Job, G. / Noffsinger, V.J. / Shanker, S. / Kuscu, C. / Joshua-Tor, L. / Partridge, J.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 54.8 KB | Display | ![]() |
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PDB format | ![]() | 39.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 448.1 KB | Display | ![]() |
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Full document | ![]() | 448.1 KB | Display | |
Data in XML | ![]() | 5.1 KB | Display | |
Data in CIF | ![]() | 6.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1kneS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 7383.179 Da / Num. of mol.: 1 / Fragment: Chromodomain (UNP residues 15 to 75) Source method: isolated from a genetically manipulated source Details: N-terminal His6-Sumo fusion Source: (gene. exp.) ![]() ![]() Gene: chp1, SPAC18G6.02c / Plasmid: pET28a-SUMO / Production host: ![]() ![]() | ||
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#2: Protein/peptide | Mass: 1771.051 Da / Num. of mol.: 1 / Fragment: UNP residues 2 to 17 / Mutation: R17Y / Source method: obtained synthetically Details: Peptide synthesis by Protein Peptide Research Ldt., Hampshire UK. References: UniProt: P09988 | ||
#3: Chemical | ChemComp-ACY / | ||
#4: Chemical | ChemComp-ZN / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.68 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 0.05 M Zinc Acetate, 20% w/v PEG 3350, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM Q315r / Detector: CCD / Date: Feb 9, 2007 |
Radiation | Monochromator: CRYOGENICALLY COOLED DOUBLE CRYSTAL MONOCHROMATOR WITH HORIZONTAL FOCUSING SAGITTAL BEND SECOND MONO CRYSTAL WITH 4:1 MAGNIFICATION RATIO AND VERTICALLY FOCUSING MIRROR Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0809 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→19.3 Å / Num. all: 7418 / Num. obs: 7255 / % possible obs: 97.93 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.4 % / Biso Wilson estimate: 44.94 Å2 / Rmerge(I) obs: 0.047 / Net I/σ(I): 14.87 |
Reflection shell | Resolution: 2.2→2.4 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.314 / Mean I/σ(I) obs: 3.46 / Num. unique all: 1683 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: Chain A of pdb code 1KNE Resolution: 2.2→19.337 Å / SU ML: 0.28 / Isotropic thermal model: Isotropic and TLS / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: CCP4 monomer library
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 56.891 Å2 / ksol: 0.41 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→19.337 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: 0.5302 Å / Origin y: -17.8348 Å / Origin z: -9.4336 Å
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Refinement TLS group | Selection details: all |