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- PDB-1i9s: CRYSTAL STRUCTURE OF THE RNA TRIPHOSPHATASE DOMAIN OF MOUSE MRNA ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1i9s | ||||||
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Title | CRYSTAL STRUCTURE OF THE RNA TRIPHOSPHATASE DOMAIN OF MOUSE MRNA CAPPING ENZYME | ||||||
![]() | MRNA CAPPING ENZYME | ||||||
![]() | HYDROLASE / RNA triphosphatase domain / mRNA capping enzyme | ||||||
Function / homology | ![]() RNA Pol II CTD phosphorylation and interaction with CE / mRNA Capping / inorganic triphosphate phosphatase activity / protein tyrosine/serine/threonine phosphatase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / 7-methylguanosine mRNA capping / dephosphorylation / mRNA guanylyltransferase activity ...RNA Pol II CTD phosphorylation and interaction with CE / mRNA Capping / inorganic triphosphate phosphatase activity / protein tyrosine/serine/threonine phosphatase activity / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / 7-methylguanosine mRNA capping / dephosphorylation / mRNA guanylyltransferase activity / mRNA guanylyltransferase / GTP binding / ATP binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Changela, A. / Ho, C.K. / Martins, A. / Shuman, S. / Mondragon, A. | ||||||
![]() | ![]() Title: Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme. Authors: Changela, A. / Ho, C.K. / Martins, A. / Shuman, S. / Mondragon, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 59.1 KB | Display | ![]() |
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PDB format | ![]() | 41.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 444 KB | Display | ![]() |
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Full document | ![]() | 444.7 KB | Display | |
Data in XML | ![]() | 12.1 KB | Display | |
Data in CIF | ![]() | 17.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 24319.631 Da / Num. of mol.: 1 / Fragment: TPASE DOMAIN (RESIDUES 1-210) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 221 molecules ![](data/chem/img/SO4.gif)
![](data/chem/img/CAC.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/IPA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CAC.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/IPA.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-SO4 / | ||
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#3: Chemical | ChemComp-CAC / | ||
#4: Chemical | ChemComp-MG / | ||
#5: Chemical | #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.8 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 15% isopropanol, 50mM sodium cacodylate (pH 6.5), 25mM magnesium chloride, 25mM ammonium sulfate , VAPOR DIFFUSION, HANGING DROP, temperature 283K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 10 ℃ | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 15, 2000 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→27 Å / Num. all: 143292 / Num. obs: 26506 / % possible obs: 99.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.4 % / Biso Wilson estimate: 16.2 Å2 / Rmerge(I) obs: 0.093 / Rsym value: 8.4 / Net I/σ(I): 5.2 |
Reflection shell | Resolution: 1.65→1.69 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.282 / Mean I/σ(I) obs: 2.9 / Num. unique all: 1916 / Rsym value: 25.1 / % possible all: 98.6 |
Reflection | *PLUS Num. measured all: 143292 |
Reflection shell | *PLUS % possible obs: 98.6 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 1.65→27 Å
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LS refinement shell | Resolution: 1.65→1.74 Å
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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