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Yorodumi- PDB-1r9t: RNA POLYMERASE II STRAND SEPARATED ELONGATION COMPLEX, MISMATCHED... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1r9t | ||||||
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| Title | RNA POLYMERASE II STRAND SEPARATED ELONGATION COMPLEX, MISMATCHED NUCLEOTIDE | ||||||
Components |
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Keywords | TRANSCRIPTION/DNA-RNA HYBRID / TRANSCRIPTION / MRNA / MULTIPROTEIN COMPLEX / MOLECULAR MACHINE / DNA / TRANSCRIPTION-DNA-RNA COMPLEX / TRANSCRIPTION-DNA-RNA HYBRID complex | ||||||
| Function / homology | Function and homology informationRNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / termination of RNA polymerase II transcription / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Promoter Escape ...RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / termination of RNA polymerase II transcription / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / termination of RNA polymerase III transcription / RNA Polymerase II Pre-transcription Events / RNA-templated transcription / Formation of TC-NER Pre-Incision Complex / transcription initiation at RNA polymerase III promoter / RNA Polymerase I Promoter Escape / termination of RNA polymerase I transcription / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription initiation at RNA polymerase I promoter / nucleolar large rRNA transcription by RNA polymerase I / Estrogen-dependent gene expression / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / transcription by RNA polymerase III / Dual incision in TC-NER / translesion synthesis / RNA polymerase I complex / transcription elongation by RNA polymerase I / RNA polymerase III complex / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / transcription-coupled nucleotide-excision repair / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / ribonucleoside binding / DNA-directed RNA polymerase / cytoplasmic stress granule / DNA-directed RNA polymerase activity / peroxisome / ribosome biogenesis / nucleic acid binding / transcription by RNA polymerase II / protein dimerization activity / mRNA binding / nucleolus / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
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| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å | ||||||
Authors | Westover, K.D. / Bushnell, D.A. / Kornberg, R.D. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2004Title: Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center. Authors: Westover, K.D. / Bushnell, D.A. / Kornberg, R.D. | ||||||
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| Remark 999 | SEQUENCE Residue A 15 and residue C 16 of the chain T are not linked. Distance of O3*-P bond is 2. ...SEQUENCE Residue A 15 and residue C 16 of the chain T are not linked. Distance of O3*-P bond is 2.98. Residue T 2 and residue G 3 of the chain N are not linked. Distance of O3*-P bond is 2.67. |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1r9t.cif.gz | 897.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1r9t.ent.gz | 601.6 KB | Display | PDB format |
| PDBx/mmJSON format | 1r9t.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1r9t_validation.pdf.gz | 978.5 KB | Display | wwPDB validaton report |
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| Full document | 1r9t_full_validation.pdf.gz | 2.7 MB | Display | |
| Data in XML | 1r9t_validation.xml.gz | 353.9 KB | Display | |
| Data in CIF | 1r9t_validation.cif.gz | 437.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r9/1r9t ftp://data.pdbj.org/pub/pdb/validation_reports/r9/1r9t | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1r9sC ![]() 1twaC ![]() 1twcC ![]() 1twfC ![]() 1twgC ![]() 1twhC ![]() 1i6hS C: citing same article ( S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
-RNA chain , 1 types, 1 molecules R
| #1: RNA chain | Mass: 3264.036 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: TRANSCRIPT |
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-DNA chain , 2 types, 2 molecules TN
| #2: DNA chain | Mass: 8534.519 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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| #3: DNA chain | Mass: 4286.789 Da / Num. of mol.: 1 / Source method: obtained synthetically |
-DNA-directed RNA polymerase II ... , 5 types, 5 molecules ABCIK
| #4: Protein | Mass: 191821.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #5: Protein | Mass: 138937.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 35330.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 14308.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 13633.493 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA-directed RNA polymerases I, II, and III ... , 5 types, 5 molecules EFHJL
| #7: Protein | Mass: 25117.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #8: Protein | Mass: 17931.834 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 16525.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 8290.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 7729.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 3 types, 11 molecules 




| #14: Chemical | ChemComp-ZN / #15: Chemical | #16: Chemical | ChemComp-ATP / | |
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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: 3.67 Å3/Da / Density % sol: 66.53 % | ||||||||||||||||||||||||||||||||||||||||||||
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| Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 6000, Ammonium hydrogen phosphate, sodium dihydrogen phosphate, dioxane, DTT, pH 6.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||||
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-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.98 |
| Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 21, 2003 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
| Reflection | Resolution: 3.5→40 Å / Num. obs: 83860 / % possible obs: 94.2 % / Redundancy: 2.8 % |
| Reflection shell | Highest resolution: 3.5 Å / Rmerge(I) obs: 0.37 / % possible all: 87.3 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB entry 1I6H Resolution: 3.5→40 Å / Rfactor Rfree: 0.317 / Rfactor Rwork: 0.23 / Rfactor all: 0.239 / Rfactor obs: 0.239 | ||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.5→40 Å
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