+Open data
-Basic information
Entry | Database: PDB / ID: 5svx | ||||||
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Title | MORC3 CW in complex with histone H3K4me3 | ||||||
Components |
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Keywords | TRANSCRIPTION / reader / histone / chromatin / methylation / methyllysine | ||||||
Function / homology | Function and homology information negative regulation of interferon-beta production / maintenance of protein location in nucleus / antiviral innate immune response / Chromatin modifying enzymes / epigenetic regulation of gene expression / negative regulation of fibroblast proliferation / methylated histone binding / telomere organization / RNA Polymerase I Promoter Opening / Interleukin-7 signaling ...negative regulation of interferon-beta production / maintenance of protein location in nucleus / antiviral innate immune response / Chromatin modifying enzymes / epigenetic regulation of gene expression / negative regulation of fibroblast proliferation / methylated histone binding / telomere organization / RNA Polymerase I Promoter Opening / Interleukin-7 signaling / Assembly of the ORC complex at the origin of replication / post-embryonic development / DNA methylation / Condensation of Prophase Chromosomes / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / Chromatin modifications during the maternal to zygotic transition (MZT) / SIRT1 negatively regulates rRNA expression / HCMV Late Events / PRC2 methylates histones and DNA / Defective pyroptosis / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / HDMs demethylate histones / PML body / PKMTs methylate histone lysines / RMTs methylate histone arginines / Meiotic recombination / Pre-NOTCH Transcription and Translation / nuclear matrix / nucleosome assembly / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / Transcriptional regulation of granulopoiesis / structural constituent of chromatin / positive regulation of cellular senescence / nucleosome / protein-macromolecule adaptor activity / RUNX1 regulates transcription of genes involved in differentiation of HSCs / gene expression / chromatin organization / Factors involved in megakaryocyte development and platelet production / HATs acetylate histones / Senescence-Associated Secretory Phenotype (SASP) / peptidyl-serine phosphorylation / Oxidative Stress Induced Senescence / Estrogen-dependent gene expression / protein stabilization / cadherin binding / protein heterodimerization activity / Amyloid fiber formation / protein phosphorylation / chromatin / negative regulation of transcription by RNA polymerase II / ATP hydrolysis activity / protein-containing complex / DNA binding / RNA binding / extracellular exosome / zinc ion binding / extracellular region / nucleoplasm / membrane / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.56 Å | ||||||
Authors | Tong, Q. / Andrews, F.H. / Kutateladze, T.G. | ||||||
Citation | Journal: Cell Rep / Year: 2016 Title: Multivalent Chromatin Engagement and Inter-domain Crosstalk Regulate MORC3 ATPase. Authors: Andrews, F.H. / Tong, Q. / Sullivan, K.D. / Cornett, E.M. / Zhang, Y. / Ali, M. / Ahn, J. / Pandey, A. / Guo, A.H. / Strahl, B.D. / Costello, J.C. / Espinosa, J.M. / Rothbart, S.B. / Kutateladze, T.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5svx.cif.gz | 25 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5svx.ent.gz | 17.4 KB | Display | PDB format |
PDBx/mmJSON format | 5svx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sv/5svx ftp://data.pdbj.org/pub/pdb/validation_reports/sv/5svx | 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/peptide | Mass: 5847.418 Da / Num. of mol.: 1 / Fragment: unp residues 407-454 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MORC3, KIAA0136, NXP2, ZCWCC3 / Production host: Escherichia coli (E. coli) / References: UniProt: Q14149 |
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#2: Protein/peptide | Mass: 1293.516 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P68431*PLUS |
#3: Chemical | ChemComp-ZN / |
#4: 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: 1.98 Å3/Da / Density % sol: 37.77 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / Details: 2.5 M (NH4)SO4, 0.1 M sodium acetate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 4.2.2 / Wavelength: 1.28 Å |
Detector | Type: DECTRIS PILATUS3 R CdTe 300K / Detector: PIXEL / Date: Sep 4, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.28 Å / Relative weight: 1 |
Reflection | Resolution: 1.56→34.32 Å / Num. obs: 15728 / % possible obs: 100 % / Redundancy: 17.6 % / Net I/σ(I): 24.3 |
Reflection shell | Resolution: 1.56→1.6 Å / Redundancy: 15 % / Rmerge(I) obs: 0.18 / % possible all: 99.7 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 1.56→34.275 Å / SU ML: 0.07 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 14.84
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.56→34.275 Å
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Refine LS restraints |
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LS refinement shell |
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