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Yorodumi- PDB-4c06: Crystal structure of M. musculus protein arginine methyltransfera... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4c06 | ||||||
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Title | Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with MgCl2 | ||||||
Components | PROTEIN ARGININE N-METHYLTRANSFERASE 6 | ||||||
Keywords | TRANSFERASE / ARGININE METHYLTRANSFERASE / S-ADENOSYL-L-METHIONINE | ||||||
Function / homology | Function and homology information histone H2AR3 methyltransferase activity / protein-arginine omega-N monomethyltransferase activity / histone H4R3 methyltransferase activity / histone H3R2 methyltransferase activity / RMTs methylate histone arginines / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / type I protein arginine methyltransferase / protein-arginine omega-N asymmetric methyltransferase activity / histone arginine N-methyltransferase activity / protein-arginine N-methyltransferase activity ...histone H2AR3 methyltransferase activity / protein-arginine omega-N monomethyltransferase activity / histone H4R3 methyltransferase activity / histone H3R2 methyltransferase activity / RMTs methylate histone arginines / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / type I protein arginine methyltransferase / protein-arginine omega-N asymmetric methyltransferase activity / histone arginine N-methyltransferase activity / protein-arginine N-methyltransferase activity / regulation of mitochondrion organization / histone methyltransferase activity / negative regulation of ubiquitin-dependent protein catabolic process / regulation of signal transduction by p53 class mediator / protein modification process / cellular senescence / histone binding / methylation / DNA repair / negative regulation of DNA-templated transcription / chromatin binding / nucleolus / negative regulation of transcription by RNA polymerase II / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | MUS MUSCULUS (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Bonnefond, L. / Cura, V. / Troffer-Charlier, N. / Mailliot, J. / Wurtz, J.M. / Cavarelli, J. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2015 Title: Functional Insights from High Resolution Structures of Mouse Protein Arginine Methyltransferase 6. Authors: Bonnefond, L. / Stojko, J. / Mailliot, J. / Troffer-Charlier, N. / Cura, V. / Wurtz, J.M. / Cianferani, S. / Cavarelli, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4c06.cif.gz | 209 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4c06.ent.gz | 169 KB | Display | PDB format |
PDBx/mmJSON format | 4c06.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c0/4c06 ftp://data.pdbj.org/pub/pdb/validation_reports/c0/4c06 | HTTPS FTP |
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-Related structure data
Related structure data | 4c03C 4c04C 4c05C 4c07C 4c08C 2y1wS 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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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 42321.793 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) MUS MUSCULUS (house mouse) References: UniProt: Q6NZB1, Transferases; Transferring one-carbon groups; Methyltransferases, EC: 2.1.1.125 |
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#2: Chemical | ChemComp-MG / |
#3: 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: 2.63 Å3/Da / Density % sol: 53.18 % / Description: NONE |
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Crystal grow | pH: 8 / Details: pH 8.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 22, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8726 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→40.92 Å / Num. obs: 48039 / % possible obs: 98.4 % / Observed criterion σ(I): 0.9 / Redundancy: 8.2 % / Biso Wilson estimate: 20.93 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 17.29 |
Reflection shell | Resolution: 1.6→1.66 Å / Redundancy: 5.9 % / Mean I/σ(I) obs: 0.9 / % possible all: 86.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2Y1W Resolution: 1.6→40.923 Å / SU ML: 0.19 / σ(F): 1.36 / Phase error: 20.61 / 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: 1.6→40.923 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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