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Yorodumi- PDB-4y2h: Crystal structure of human protein arginine methyltransferase PRM... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4y2h | ||||||
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Title | Crystal structure of human protein arginine methyltransferase PRMT6 bound to SAH and an aryl pyrazole inhibitor | ||||||
Components | Protein arginine N-methyltransferase 6 | ||||||
Keywords | TRANSFERASE | ||||||
Function / homology | Function and homology information histone H2AR3 methyltransferase activity / peptidyl-arginine methylation, to asymmetrical-dimethyl arginine / protein-arginine omega-N monomethyltransferase activity / histone H4R3 methyltransferase activity / histone H3R2 methyltransferase activity / type I protein arginine methyltransferase / protein-arginine omega-N asymmetric methyltransferase activity / regulation of megakaryocyte differentiation / histone arginine N-methyltransferase activity / protein-arginine N-methyltransferase activity ...histone H2AR3 methyltransferase activity / peptidyl-arginine methylation, to asymmetrical-dimethyl arginine / protein-arginine omega-N monomethyltransferase activity / histone H4R3 methyltransferase activity / histone H3R2 methyltransferase activity / type I protein arginine methyltransferase / protein-arginine omega-N asymmetric methyltransferase activity / regulation of megakaryocyte differentiation / histone arginine N-methyltransferase activity / protein-arginine N-methyltransferase activity / regulation of mitochondrion organization / histone H3 methyltransferase activity / histone methyltransferase activity / negative regulation of ubiquitin-dependent protein catabolic process / regulation of signal transduction by p53 class mediator / base-excision repair / protein modification process / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / RMTs methylate histone arginines / cellular senescence / histone binding / negative regulation of DNA-templated transcription / chromatin binding / nucleolus / negative regulation of transcription by RNA polymerase II / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.37 Å | ||||||
Authors | Swinger, K.K. / Boriack-Sjodin, P.A. | ||||||
Citation | Journal: Acs Med.Chem.Lett. / Year: 2015 Title: Aryl Pyrazoles as Potent Inhibitors of Arginine Methyltransferases: Identification of the First PRMT6 Tool Compound. Authors: Mitchell, L.H. / Drew, A.E. / Ribich, S.A. / Rioux, N. / Swinger, K.K. / Jacques, S.L. / Lingaraj, T. / Boriack-Sjodin, P.A. / Waters, N.J. / Wigle, T.J. / Moradei, O. / Jin, L. / Riera, T. ...Authors: Mitchell, L.H. / Drew, A.E. / Ribich, S.A. / Rioux, N. / Swinger, K.K. / Jacques, S.L. / Lingaraj, T. / Boriack-Sjodin, P.A. / Waters, N.J. / Wigle, T.J. / Moradei, O. / Jin, L. / Riera, T. / Porter-Scott, M. / Moyer, M.P. / Smith, J.J. / Chesworth, R. / Copeland, R.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4y2h.cif.gz | 156.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4y2h.ent.gz | 122.2 KB | Display | PDB format |
PDBx/mmJSON format | 4y2h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y2/4y2h ftp://data.pdbj.org/pub/pdb/validation_reports/y2/4y2h | 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
#1: Protein | Mass: 39624.992 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 27-375 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PRMT6, HRMT1L6 / Production host: Escherichia coli (E. coli) References: UniProt: Q96LA8, Transferases; Transferring one-carbon groups; Methyltransferases, EC: 2.1.1.125 #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-GOL / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.82 Å3/Da / Density % sol: 56.4 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, hanging drop / Details: MgCl, MES buffer pH 6.5, Isopropanol, PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.97856 Å | |||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 2, 2012 | |||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 | |||||||||||||||||||||||||||
Reflection | Resolution: 2.37→27.74 Å / Num. obs: 35874 / % possible obs: 99.9 % / Redundancy: 4.9 % / CC1/2: 0.991 / Rmerge(I) obs: 0.144 / Rpim(I) all: 0.073 / Net I/σ(I): 10.5 / Num. measured all: 175169 | |||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: 0
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-Processing
Software |
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Refinement | Resolution: 2.37→27.74 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.903 / SU B: 6.754 / SU ML: 0.159 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.322 / ESU R Free: 0.231 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 101.25 Å2 / Biso mean: 23.621 Å2 / Biso min: 6.95 Å2
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Refinement step | Cycle: final / Resolution: 2.37→27.74 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.37→2.431 Å / Total num. of bins used: 20
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