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Yorodumi- PDB-1ta0: Three-dimensional structure of a RNA-polymerase II binding protei... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ta0 | ||||||
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Title | Three-dimensional structure of a RNA-polymerase II binding protein with associated ligand. | ||||||
Components | Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 | ||||||
Keywords | HYDROLASE / alpha-beta protein | ||||||
Function / homology | Function and homology information RNA polymerase II CTD heptapeptide repeat phosphatase activity / myosin phosphatase activity / negative regulation of G1/S transition of mitotic cell cycle / protein-serine/threonine phosphatase / negative regulation of neuron differentiation / protein dephosphorylation / negative regulation of protein phosphorylation / negative regulation of neurogenesis / regulation of transcription by RNA polymerase II / extracellular exosome ...RNA polymerase II CTD heptapeptide repeat phosphatase activity / myosin phosphatase activity / negative regulation of G1/S transition of mitotic cell cycle / protein-serine/threonine phosphatase / negative regulation of neuron differentiation / protein dephosphorylation / negative regulation of protein phosphorylation / negative regulation of neurogenesis / regulation of transcription by RNA polymerase II / extracellular exosome / nucleoplasm / metal ion binding / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Kamenski, T. / Heilmeier, S. / Meinhart, T. / Cramer, P. | ||||||
Citation | Journal: Mol.Cell / Year: 2004 Title: Structure and Mechanism of RNA Polymerase II CTD Phosphatases. Authors: Kamenski, T. / Heilmeier, S. / Meinhart, T. / Cramer, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ta0.cif.gz | 50.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ta0.ent.gz | 38.2 KB | Display | PDB format |
PDBx/mmJSON format | 1ta0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ta/1ta0 ftp://data.pdbj.org/pub/pdb/validation_reports/ta/1ta0 | 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: 22715.732 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CTDSP1, NIF3, NLIIF / Plasmid: pET21b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-RIL References: UniProt: Q9GZU7, protein-serine/threonine phosphatase |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-CIT / |
#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: 1.3 Å3/Da / Density % sol: 54 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: PEG 3300, ammonium acetate, citrate buffer, DTT , pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9919 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 22, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9919 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. all: 13642 / Num. obs: 13356 / % possible obs: 97.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.057 |
Reflection shell | Resolution: 2.1→2.2 Å / Rmerge(I) obs: 0.062 / Mean I/σ(I) obs: 16.8 / Num. unique all: 1520 / % possible all: 87.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.16 Å /
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