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Open data
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Basic information
| Entry | Database: PDB / ID: 1nt9 | ||||||
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| Title | Complete 12-subunit RNA polymerase II | ||||||
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Keywords | TRANSCRIPTION / TRANSFERASE / DNA-dependent RNA polymerase / cellular RNA polymerase / multisubunit complex / gene expression / mRNA / messenger RNA synthesis | ||||||
| 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 / 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 / nuclear-transcribed mRNA catabolic process / positive regulation of translational initiation / 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 / 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 / ribosome biogenesis / single-stranded DNA binding / 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: 4.2 Å | ||||||
Authors | Armache, K.-J. / Kettenberger, H. / Cramer, P. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2003Title: Architecture of initiation-competent 12-subunit RNA polymerase II Authors: Armache, K.-J. / Kettenberger, H. / Cramer, P. | ||||||
| History |
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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 | 1nt9.cif.gz | 155.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1nt9.ent.gz | 81.2 KB | Display | PDB format |
| PDBx/mmJSON format | 1nt9.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1nt9_validation.pdf.gz | 381.3 KB | Display | wwPDB validaton report |
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| Full document | 1nt9_full_validation.pdf.gz | 381.3 KB | Display | |
| Data in XML | 1nt9_validation.xml.gz | 979 B | Display | |
| Data in CIF | 1nt9_validation.cif.gz | 35 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nt/1nt9 ftp://data.pdbj.org/pub/pdb/validation_reports/nt/1nt9 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1i6hS 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
-DNA-DIRECTED RNA POLYMERASE II ... , 5 types, 5 molecules ACGIK
| #1: 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: 35330.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 19081.053 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() |
| #9: Protein | Mass: 14308.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 13633.493 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 2 types, 2 molecules BD
| #2: Protein | Mass: 138937.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #4: Protein | Mass: 25451.191 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Numbering of resiudes D10-D24 is arbitrary Source: (gene. exp.) ![]() Production host: ![]() |
-DNA-directed RNA polymerases I, II, and III ... , 5 types, 5 molecules EFHJL
| #5: Protein | Mass: 25117.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #6: Protein | Mass: 17931.834 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 16525.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 8290.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 7729.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 5.92 Å3/Da / Density % sol: 79.22 % | ||||||||||||||||||||||||||||||||||||
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 20000, ammonium sodium phosphate, sodium chloride, dioxane, DTT, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||
| Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9185 Å |
| Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 2, 2002 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9185 Å / Relative weight: 1 |
| Reflection | Resolution: 4.2→50 Å / Num. all: 83431 / Num. obs: 83431 / % possible obs: 93.8 % / Rsym value: 0.093 |
| Reflection shell | Resolution: 4.2→4.35 Å / Rmerge(I) obs: 0.363 / % possible all: 89.5 |
| Reflection | *PLUS Highest resolution: 4.2 Å / Lowest resolution: 50 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.093 |
| Reflection shell | *PLUS Highest resolution: 4.2 Å / % possible obs: 89.5 % / Num. unique obs: 7893 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRY 1I6H Resolution: 4.2→50 Å / σ(F): 0 Details: Model was fitted into electron densities, no least square minimization was performed
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| Refinement step | Cycle: LAST / Resolution: 4.2→50 Å
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| Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||
| Refinement | *PLUS | ||||||||||||
| Solvent computation | *PLUS | ||||||||||||
| Displacement parameters | *PLUS | ||||||||||||
| Refine LS restraints | *PLUS
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