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Yorodumi- PDB-2c46: CRYSTAL STRUCTURE OF THE HUMAN RNA guanylyltransferase and 5'- ph... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2c46 | ||||||
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Title | CRYSTAL STRUCTURE OF THE HUMAN RNA guanylyltransferase and 5'- phosphatase | ||||||
Components | MRNA CAPPING ENZYMEMRNA guanylyltransferase | ||||||
Keywords | TRANSFERASE / PHOSPHATASE / HYDROLASE / MRNA PROCESSING / MULTIFUNCTIONAL ENZYME / NUCLEOTIDYLTRANSFERASE | ||||||
Function / homology | Function and homology information RNA guanylyltransferase activity / inorganic triphosphate phosphatase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / protein tyrosine/serine/threonine phosphatase activity / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / mRNA Capping / 7-methylguanosine mRNA capping ...RNA guanylyltransferase activity / inorganic triphosphate phosphatase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / protein tyrosine/serine/threonine phosphatase activity / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / mRNA Capping / 7-methylguanosine mRNA capping / RNA processing / dephosphorylation / mRNA guanylyltransferase activity / mRNA guanylyltransferase / GTP binding / nucleoplasm / ATP binding / nucleus Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Debreczeni, J. / Johansson, C. / Longman, E. / Gileadi, O. / SavitskySmee, P. / Smee, C. / Bunkoczi, G. / Ugochukwu, E. / von Delft, F. / Sundstrom, M. ...Debreczeni, J. / Johansson, C. / Longman, E. / Gileadi, O. / SavitskySmee, P. / Smee, C. / Bunkoczi, G. / Ugochukwu, E. / von Delft, F. / Sundstrom, M. / Weigelt, J. / Arrowsmith, C. / Edwards, A. / Knapp, S. | ||||||
Citation | Journal: To be Published Title: Crystal Structure of the Human RNA Guanylyltransferase and 5'-Phosphatase Authors: Debreczeni, J. / Johansson, C. / Longman, E. / Gileadi, O. / Savitskysmee, P. / Smee, C. / Bunkoczi, G. / Ugochukwu, E. / von Delft, F. / Sundstrom, M. / Weigelt, J. / Arrowsmith, C. / Edwards, A. / Knapp, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2c46.cif.gz | 175.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2c46.ent.gz | 138.1 KB | Display | PDB format |
PDBx/mmJSON format | 2c46.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c4/2c46 ftp://data.pdbj.org/pub/pdb/validation_reports/c4/2c46 | HTTPS FTP |
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-Related structure data
Related structure data | 1i9sS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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5 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 27688.188 Da / Num. of mol.: 4 / Fragment: TPASE REGION, RESIDUES 1-219 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: O60942, mRNA guanylyltransferase #2: Water | ChemComp-HOH / | Sequence details | THE N-TERMINAL MHHHHHHSSG | |
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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: 2.2 Å3/Da / Density % sol: 44.6 % |
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Crystal grow | Details: 2 M POTASSIUM CITRATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9998 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 1, 2005 / Details: MIRRORS |
Radiation | Monochromator: SI111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9998 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→47.9 Å / Num. obs: 133485 / % possible obs: 90.4 % / Observed criterion σ(I): 3 / Redundancy: 3.79 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 10.29 |
Reflection shell | Resolution: 1.6→1.7 Å / Redundancy: 2.73 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 2.71 / % possible all: 87.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1I9S Resolution: 1.6→80.85 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.938 / SU B: 4.64 / SU ML: 0.08 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.089 / ESU R Free: 0.091 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.35 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→80.85 Å
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Refine LS restraints |
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