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Yorodumi- PDB-2r93: Elongation complex of RNA polymerase II with a hepatitis delta vi... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 2r93 | ||||||
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| Title | Elongation complex of RNA polymerase II with a hepatitis delta virus-derived RNA stem loop | ||||||
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Keywords | Transferase/RNA / TRANSFERASE/DNA/RNA / DNA-BINDING / PHOSPHORYLATION / RNA POLYMERASE II / METAL-BINDING / NUCLEAR PROTEIN / TRANSCRIPTION BUBBLE / ELONGATION COMPLEX / TRANSFERASE / TRANSCRIPTION / RNA-DEPENDENT / RNA-DEPENDENT RNA SYNTHESIS / RDRP / DDRP / RNA-BINDING / HEPATITIS DELTA VIRUS / HDV / DNA-directed RNA polymerase / Magnesium / Nucleotidyltransferase / Nucleus / Ubl conjugation / Zinc / Zinc-finger / Polymorphism / Cytoplasm / DNA damage / DNA repair / mRNA processing / Transferase-RNA COMPLEX | ||||||
| Function / homology | Function and homology informationRPB4-RPB7 complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / 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 ...RPB4-RPB7 complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / 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 / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / 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 / transcription initiation at RNA polymerase I promoter / nucleolar large rRNA transcription by RNA polymerase I / Gap-filling DNA repair synthesis and ligation in TC-NER / Estrogen-dependent gene expression / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / nuclear-transcribed mRNA catabolic process / transcription by RNA polymerase III / positive regulation of translational initiation / 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 / translation initiation factor binding / transcription-coupled nucleotide-excision repair / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / P-body / DNA-templated transcription initiation / ribonucleoside binding / mRNA processing / DNA-directed RNA polymerase / cytoplasmic stress granule / DNA-directed RNA polymerase activity / peroxisome / single-stranded DNA binding / ribosome biogenesis / nucleic acid binding / transcription by RNA polymerase II / single-stranded RNA binding / protein dimerization activity / nucleotide binding / mRNA binding / nucleolus / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4 Å | ||||||
Authors | Lehmann, E. / Brueckner, F. / Cramer, P. | ||||||
Citation | Journal: Nature / Year: 2007Title: Molecular basis of RNA-dependent RNA polymerase II activity. Authors: Lehmann, E. / Brueckner, F. / Cramer, P. | ||||||
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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 | 2r93.cif.gz | 816.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2r93.ent.gz | 639.7 KB | Display | PDB format |
| PDBx/mmJSON format | 2r93.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2r93_validation.pdf.gz | 594.5 KB | Display | wwPDB validaton report |
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| Full document | 2r93_full_validation.pdf.gz | 894.4 KB | Display | |
| Data in XML | 2r93_validation.xml.gz | 170.2 KB | Display | |
| Data in CIF | 2r93_validation.cif.gz | 230.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r9/2r93 ftp://data.pdbj.org/pub/pdb/validation_reports/r9/2r93 | HTTPS FTP |
-Related 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: 5671.372 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: This sequence occurs naturally in hepatitis delta virus. |
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-DNA-directed RNA polymerase II subunit ... , 7 types, 7 molecules ABCDGIK
| #2: Protein | Mass: 191821.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: Protein | Mass: 138937.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 35330.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 25451.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 19081.053 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 subunit ... , 5 types, 5 molecules EFHJL
| #6: Protein | Mass: 25117.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #7: 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 , 2 types, 9 molecules 


| #14: Chemical | ChemComp-ZN / #15: Chemical | ChemComp-MG / | |
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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: 6.025 Å3/Da / Density % sol: 79.586 % | ||||||||||||||||||||||||||||||||||||||||||||
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| Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 5% (w/v) PEG 6000, 200 mM ammonium acetate, 150 mM magnesium acetate, 50 mM Hepes pH 7.0, 5 mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K | ||||||||||||||||||||||||||||||||||||||||||||
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-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.99987 Å |
| Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: May 5, 2007 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.99987 Å / Relative weight: 1 |
| Reflection | Resolution: 4→50 Å / Num. all: 104533 / Num. obs: 104533 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.5 % / Rsym value: 0.149 / Net I/σ(I): 12.4 |
| Reflection shell | Resolution: 4→4.14 Å / Redundancy: 7.7 % / Mean I/σ(I) obs: 4.2 / Num. unique all: 10323 / Rsym value: 0.479 / % possible all: 99.9 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 4→50 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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| Refinement step | Cycle: LAST / Resolution: 4→50 Å
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| Refine LS restraints |
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