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Open data
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Basic information
| Entry | Database: PDB / ID: 3hoy | ||||||
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| Title | Complete RNA polymerase II elongation complex VI | ||||||
Components |
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Keywords | TRANSCRIPTION / TRANSFERASE/DNA/RNA HYBRID / RNA polymerase II / Metal-Binding / Transcription bubble / Elongation complex / DNA-RNA mismatch / RNA fraying / DNA-binding / DNA-directed RNA polymerase / Isopeptide bond / Magnesium / Nucleotidyltransferase / Nucleus / Phosphoprotein / Transferase / Ubl conjugation / Zinc / Zinc-finger / Polymorphism / Cytoplasm / DNA damage / DNA repair / mRNA processing / TRANSFERASE-DNA-RNA HYBRID 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 / 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: 3.4 Å | ||||||
Authors | Sydow, J.F. / Brueckner, F. / Cheung, A.C.M. / Damsma, G.E. / Dengl, S. / Lehmann, E. / Vassylyev, D. / Cramer, P. | ||||||
Citation | Journal: Mol.Cell / Year: 2009Title: Structural basis of transcription: mismatch-specific fidelity mechanisms and paused RNA polymerase II with frayed RNA. Authors: Sydow, J.F. / Brueckner, F. / Cheung, A.C.M. / Damsma, G.E. / Dengl, S. / Lehmann, E. / Vassylyev, D. / 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 | 3hoy.cif.gz | 826.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3hoy.ent.gz | 645.2 KB | Display | PDB format |
| PDBx/mmJSON format | 3hoy.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3hoy_validation.pdf.gz | 635.3 KB | Display | wwPDB validaton report |
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| Full document | 3hoy_full_validation.pdf.gz | 961 KB | Display | |
| Data in XML | 3hoy_validation.xml.gz | 172.7 KB | Display | |
| Data in CIF | 3hoy_validation.cif.gz | 234.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ho/3hoy ftp://data.pdbj.org/pub/pdb/validation_reports/ho/3hoy | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 3houC ![]() 3hovC ![]() 3howC ![]() 3hoxC ![]() 3hozC ![]() 1y1wS 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
-DNA-directed RNA polymerase II subunit ... , 7 types, 7 molecules ABCDGIK
| #1: Protein | Mass: 191821.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: Protein | Mass: 138937.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #3: Protein | Mass: 38677.918 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 25451.191 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 natural source / Source: (natural) ![]() |
| #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) ![]() |
-DNA-directed RNA polymerases I, II, and III subunit ... , 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) ![]() |
-DNA chain , 2 types, 2 molecules TN
| #13: DNA chain | Mass: 12561.904 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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| #14: DNA chain | Mass: 12664.168 Da / Num. of mol.: 1 / Source method: obtained synthetically |
-RNA chain , 1 types, 1 molecules P
| #15: RNA chain | Mass: 6438.927 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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-Non-polymers , 2 types, 9 molecules 


| #16: Chemical | ChemComp-ZN / #17: Chemical | ChemComp-MG / | |
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-Details
| Has protein modification | Y |
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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: 5.61 Å3/Da / Density % sol: 78.06 % |
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-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA |
| Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Jan 28, 2009 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Relative weight: 1 |
| Reflection | Resolution: 3.4→50 Å / Num. all: 168339 / Num. obs: 168339 |
| Reflection shell | Highest resolution: 3.4 Å |
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Processing
| Software | Name: CNS / Version: 1.2 / Classification: refinement | ||||||||||||||||||||
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 1Y1W Resolution: 3.4→50 Å / σ(F): 0 / σ(I): 0
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| Refinement step | Cycle: LAST / Resolution: 3.4→50 Å
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