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Open data
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Basic information
| Entry | Database: PDB / ID: 8b3f | ||||||||||||||||||||||||||||||||||||
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| Title | Pol II-CSB-CSA-DDB1-ELOF1 | ||||||||||||||||||||||||||||||||||||
Components |
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Keywords | TRANSCRIPTION / DNA repair / ubiquitin / cryo-EM | ||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationregulation of transcription-coupled nucleotide-excision repair / negative regulation of double-strand break repair via nonhomologous end joining / nucleotide-excision repair complex / response to auditory stimulus / regulation of transcription elongation by RNA polymerase II / B-WICH complex / DNA protection / single strand break repair / positive regulation by virus of viral protein levels in host cell / Formation of RNA Pol II elongation complex ...regulation of transcription-coupled nucleotide-excision repair / negative regulation of double-strand break repair via nonhomologous end joining / nucleotide-excision repair complex / response to auditory stimulus / regulation of transcription elongation by RNA polymerase II / B-WICH complex / DNA protection / single strand break repair / positive regulation by virus of viral protein levels in host cell / Formation of RNA Pol II elongation complex / Formation of the Early Elongation Complex / Transcriptional regulation by small RNAs / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / FGFR2 alternative splicing / RNA polymerase II transcribes snRNA genes / mRNA Capping / mRNA Splicing - Minor Pathway / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Elongation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Pol II CTD phosphorylation and interaction with CE / Estrogen-dependent gene expression / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / mRNA Splicing - Major Pathway / response to superoxide / double-strand break repair via classical nonhomologous end joining / photoreceptor cell maintenance / chromatin-protein adaptor activity / ATP-dependent chromatin remodeler activity / spindle assembly involved in female meiosis / nuclear lumen / epigenetic programming in the zygotic pronuclei / UV-damage excision repair / RNA polymerase binding / response to UV-B / positive regulation of DNA-templated transcription, elongation / biological process involved in interaction with symbiont / positive regulation of transcription by RNA polymerase III / regulation of mitotic cell cycle phase transition / WD40-repeat domain binding / Cul4A-RING E3 ubiquitin ligase complex / Cul4-RING E3 ubiquitin ligase complex / ATP-dependent DNA damage sensor activity / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / positive regulation of transcription by RNA polymerase I / negative regulation of reproductive process / negative regulation of developmental process / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / cullin family protein binding / protein tyrosine kinase activator activity / viral release from host cell / RNA Polymerase I Transcription Initiation / site of DNA damage / pyrimidine dimer repair / response to X-ray / positive regulation of transcription initiation by RNA polymerase II / ATP-dependent activity, acting on DNA / ectopic germ cell programmed cell death / translation elongation factor activity / RNA polymerase I complex / positive regulation of viral genome replication / transcription elongation by RNA polymerase I / RNA polymerase III complex / ubiquitin-like ligase-substrate adaptor activity / response to UV / RNA polymerase II, core complex / proteasomal protein catabolic process / tRNA transcription by RNA polymerase III / positive regulation of double-strand break repair via homologous recombination / protein autoubiquitination / transcription by RNA polymerase I / translation initiation factor binding / JNK cascade / neurogenesis / transcription-coupled nucleotide-excision repair / positive regulation of gluconeogenesis / DNA-directed RNA polymerase complex / positive regulation of DNA repair / DNA damage checkpoint signaling / regulation of DNA-templated transcription elongation / transcription elongation factor complex / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / response to gamma radiation / nucleotide-excision repair / transcription initiation at RNA polymerase II promoter / Recognition of DNA damage by PCNA-containing replication complex / helicase activity / base-excision repair / regulation of circadian rhythm / DNA Damage Recognition in GG-NER / B-WICH complex positively regulates rRNA expression / Dual Incision in GG-NER / response to toxic substance Similarity search - Function | ||||||||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human)![]() | ||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||||||||||||||||||||||||||
Authors | Kokic, G. / Cramer, P. | ||||||||||||||||||||||||||||||||||||
| Funding support | Germany, European Union, 2items
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Citation | Journal: To Be PublishedTitle: Pol II-CSB-CSA-DDB1-ELOF1 structure. Authors: Kokic, G. / 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 | 8b3f.cif.gz | 1.9 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8b3f.ent.gz | 1.6 MB | Display | PDB format |
| PDBx/mmJSON format | 8b3f.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8b3f_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 8b3f_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | 8b3f_validation.xml.gz | 158.3 KB | Display | |
| Data in CIF | 8b3f_validation.cif.gz | 248.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b3/8b3f ftp://data.pdbj.org/pub/pdb/validation_reports/b3/8b3f | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 15826MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-DNA-directed RNA polymerase ... , 7 types, 7 molecules ABCEFGI
| #1: Protein | Mass: 217450.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: A0A7M4DUC2, DNA-directed RNA polymerase |
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| #2: Protein | Mass: 133201.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: A0A0B8RVL1, DNA-directed RNA polymerase |
| #3: Protein | Mass: 31439.074 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 24644.318 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 14477.001 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 19314.283 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 14541.221 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-RNA polymerase II subunit ... , 2 types, 2 molecules DL
| #4: Protein | Mass: 16331.255 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #12: Protein | Mass: 7018.244 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA-directed RNA polymerases I, II, and III subunit ... , 2 types, 2 molecules HJ
| #8: Protein | Mass: 17162.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #10: Protein | Mass: 7655.123 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 3 types, 3 molecules KMd
| #11: Protein | Mass: 13310.284 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #13: Protein | Mass: 9475.881 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOF1, hCG_29982 / Production host: ![]() |
| #19: Protein | Mass: 127097.469 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DDB1, XAP1 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q16531 |
-DNA chain , 2 types, 2 molecules NT
| #14: DNA chain | Mass: 16027.309 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
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| #16: DNA chain | Mass: 15824.121 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
-RNA chain , 1 types, 1 molecules P
| #15: RNA chain | Mass: 3264.036 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
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-DNA excision repair protein ERCC- ... , 2 types, 2 molecules ab
| #17: Protein | Mass: 44107.160 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ERCC8, CKN1, CSA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q13216 |
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| #18: Protein | Mass: 168945.797 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ERCC6, CSB / Production host: Trichoplusia ni (cabbage looper)References: UniProt: Q03468, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
-Non-polymers , 2 types, 10 molecules 


| #20: Chemical | ChemComp-ZN / #21: Chemical | ChemComp-MG / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Pol II-CSB-CSA-DDB1-ELOF1 complex. / Type: COMPLEX / Entity ID: #1-#19 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 140 nm |
| Image recording | Electron dose: 42 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.18.2_3874: / Classification: refinement | ||||||||||||||||||||||||
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| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 220655 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)

Germany, European Union, 2items
Citation
PDBj









































gel filtration
Trichoplusia ni (cabbage looper)
