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Open data
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Basic information
| Entry | Database: PDB / ID: 3i4n | ||||||
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| Title | 8-oxoguanine containing RNA polymerase II elongation complex E | ||||||
Components |
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Keywords | TRANSCRIPTION / TRANSFERASE/DNA-RNA HYBRID / RNA POLYMERASE II / METAL-BINDING / TRANSCRIPTION BUBBLE / ELONGATION COMPLEX / 8-OXOGUANINE / DNA DAMAGE / OXIDATIVE DAMAGE / DNA-binding / DNA-directed RNA polymerase / Isopeptide bond / Magnesium / Nucleotidyltransferase / Nucleus / Phosphoprotein / Transferase / Zinc-finger / 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 / nucleolar large rRNA transcription by RNA polymerase I / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription initiation at RNA polymerase I promoter / 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 / 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: 3.9 Å | ||||||
Authors | Damsma, G.E. / Cramer, P. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2009Title: Molecular basis of transcriptional mutagenesis at 8-oxoguanine Authors: Damsma, G.E. / 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 | 3i4n.cif.gz | 838.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3i4n.ent.gz | 654 KB | Display | PDB format |
| PDBx/mmJSON format | 3i4n.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3i4n_validation.pdf.gz | 621.3 KB | Display | wwPDB validaton report |
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| Full document | 3i4n_full_validation.pdf.gz | 1 MB | Display | |
| Data in XML | 3i4n_validation.xml.gz | 190.4 KB | Display | |
| Data in CIF | 3i4n_validation.cif.gz | 257.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i4/3i4n ftp://data.pdbj.org/pub/pdb/validation_reports/i4/3i4n | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 3i4mC ![]() 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: 36159.328 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: 8059.021 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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| #14: DNA chain | Mass: 3677.415 Da / Num. of mol.: 1 / Source method: obtained synthetically |
-RNA chain , 1 types, 1 molecules P
| #15: RNA chain | Mass: 5035.015 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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-Non-polymers , 2 types, 9 molecules 


| #16: Chemical | ChemComp-MG / |
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| #17: Chemical | ChemComp-ZN / |
-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: 5.785691 Å3/Da / Density % sol: 78.740654 % / Description: The file contains Friedel pairs. |
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| Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 5%(w/v) PEG 6000, 200mM ammonium acetate, 300mM sodium acetate, 50mM Hepes, 5mM TCEP , pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9186 Å |
| Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Feb 8, 2008 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9186 Å / Relative weight: 1 |
| Reflection | Resolution: 3.9→50 Å / Num. all: 216612 / Num. obs: 216612 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Rsym value: 0.078 / Net I/σ(I): 13.4 |
| Reflection shell | Resolution: 3.9→4 Å / Redundancy: 4 % / Mean I/σ(I) obs: 2.6 / Num. unique all: 15791 / Rsym value: 0.863 / % possible all: 99.8 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 1Y1W without nucleic acids Resolution: 3.9→50 Å / σ(F): 0 / σ(I): 0 / Details: The file contains Friedel pairs.
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| Refinement step | Cycle: LAST / Resolution: 3.9→50 Å
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| Refine LS restraints |
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