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Open data
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Basic information
| Entry | Database: PDB / ID: 8umh | |||||||||||||||||||||||||||||||||||||||||||||
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| Title | Consensus map of PICdeltaTFIIK form2 | |||||||||||||||||||||||||||||||||||||||||||||
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Keywords | TRANSCRIPTION / Transcription. POL II | |||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology information: / : / : / : / : / regulation of mitotic recombination / RNA polymerase II complex recruiting activity / transcription open complex formation at RNA polymerase II promoter / TFIIA-class transcription factor complex binding / RNA polymerase III transcription regulatory region sequence-specific DNA binding ...: / : / : / : / : / regulation of mitotic recombination / RNA polymerase II complex recruiting activity / transcription open complex formation at RNA polymerase II promoter / TFIIA-class transcription factor complex binding / RNA polymerase III transcription regulatory region sequence-specific DNA binding / : / TFIIH-class transcription factor complex binding / RNA polymerase III preinitiation complex assembly / RNA polymerase II promoter clearance / transcription factor TFIIIB complex / positive regulation of mitotic recombination / RNA polymerase I general transcription initiation factor binding / transcription factor TFIIE complex / nucleotide-excision repair factor 3 complex / nucleotide-excision repair, preincision complex assembly / DNA translocase activity / regulation of transcription by RNA polymerase III / TFIIF-class transcription factor complex binding / transcriptional start site selection at RNA polymerase II promoter / hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides / transcription factor TFIIF complex / transcription factor TFIIA complex / RNA polymerase I preinitiation complex assembly / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / DNA binding, bending / RNA Polymerase I Transcription Initiation / transcription preinitiation complex / 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 / DNA 3'-5' helicase / RNA polymerase II transcribes snRNA genes / TP53 Regulates Transcription of DNA Repair Genes / poly(A)+ mRNA export from nucleus / 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 / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / termination of RNA polymerase III transcription / RNA Polymerase II Pre-transcription Events / RNA-templated transcription / 3'-5' DNA helicase activity / 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 / RNA polymerase II complex binding / ATPase activator activity / Estrogen-dependent gene expression / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / positive regulation of translational initiation / transcription by RNA polymerase III / Dual incision in TC-NER / protein phosphatase activator activity / RNA polymerase I complex / transcription elongation by RNA polymerase I / RNA polymerase III complex / RNA polymerase II core promoter sequence-specific DNA binding / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / RNA polymerase II preinitiation complex assembly / transcription by RNA polymerase I / translation initiation factor binding / transcription-coupled nucleotide-excision repair / DNA helicase activity / TBP-class protein binding / nucleotide-excision repair / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / P-body / DNA-templated transcription initiation / positive regulation of transcription elongation by RNA polymerase II / ribonucleoside binding / DNA-directed RNA polymerase / disordered domain specific binding / DNA-directed RNA polymerase activity / ribosome biogenesis / single-stranded DNA binding / double-stranded DNA binding / transcription regulator complex / DNA-binding transcription factor binding / DNA helicase / damaged DNA binding / nucleic acid binding / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.1 Å | |||||||||||||||||||||||||||||||||||||||||||||
Authors | Yang, C. / Murakami, K. | |||||||||||||||||||||||||||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: To be publishedTitle: consensus map of PICdeltaTFIIK form2 Authors: Yang, C. / Murakami, K. | |||||||||||||||||||||||||||||||||||||||||||||
| 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 | 8umh.cif.gz | 1.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8umh.ent.gz | 1.3 MB | Display | PDB format |
| PDBx/mmJSON format | 8umh.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8umh_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 8umh_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML | 8umh_validation.xml.gz | 234.9 KB | Display | |
| Data in CIF | 8umh_validation.cif.gz | 361.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/um/8umh ftp://data.pdbj.org/pub/pdb/validation_reports/um/8umh | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 42379MC 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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Components
-Transcription ... , 8 types, 8 molecules MQPSUVWX
| #1: Protein | Mass: 38257.340 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SUA7, YPR086W, P9513.4 Production host: ![]() References: UniProt: P29055 |
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| #12: Protein | Mass: 82320.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 46684.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 34903.551 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #16: Protein | Mass: 32230.805 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: PACBIOSEQ_LOCUS5691, SCNYR20_0002031500, SCP684_0003030900 Production host: ![]() References: UniProt: A0A6A5Q2T8 |
| #17: Protein | Mass: 13473.070 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: PACBIOSEQ_LOCUS3356, PACBIOSEQ_LOCUS3547, PACBIOSEQ_LOCUS3591, PACBIOSEQ_LOCUS3602, PACBIOSEQ_LOCUS3607, PACBIOSEQ_LOCUS3639, PACBIOSEQ_LOCUS3680, PACBIOSEQ_LOCUS3892, PACBIOSEQ_LOCUS3963 Production host: ![]() References: UniProt: A0A6A5PRZ0 |
| #18: Protein | Mass: 54804.809 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 37050.434 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA-directed RNA polymerase ... , 7 types, 7 molecules ABCIKDG
| #2: Protein | Mass: 191821.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: A0A6A5Q1P2, DNA-directed RNA polymerase |
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| #3: Protein | Mass: 138937.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: A0A6A5Q4H2, DNA-directed RNA polymerase |
| #4: Protein | Mass: 35330.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 14308.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 13633.493 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 25451.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 19081.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA-directed RNA polymerases I, II, and III subunit ... , 3 types, 3 molecules EFH
| #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) ![]() |
| #7: Protein | Mass: 16525.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA-directed RNA polymerases II subunit ... , 2 types, 2 molecules JL
| #9: Protein | Mass: 8290.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #11: Protein | Mass: 7729.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 4 types, 4 molecules O162
| #15: Protein | Mass: 27042.275 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SPT15, BTF1, TBP1, YER148W Production host: ![]() References: UniProt: P13393 |
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| #23: Protein | Mass: 72993.328 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #25: Protein | Mass: 52370.035 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #27: Protein | Mass: 58602.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-General transcription and DNA repair factor IIH helicase subunit ... , 2 types, 2 molecules 07
| #22: Protein | Mass: 89899.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #26: Protein | Mass: 95461.664 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-General transcription and DNA repair factor IIH subunit ... , 2 types, 2 molecules 45
| #24: Protein | Mass: 37506.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #28: Protein | Mass: 8243.490 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA chain , 2 types, 2 molecules NT
| #29: DNA chain | Mass: 19703.676 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
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| #30: DNA chain | Mass: 19724.719 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
-Non-polymers , 3 types, 18 molecules 




| #31: Chemical | ChemComp-ZN / #32: Chemical | #33: Chemical | ChemComp-SF4 / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-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: consensus map of PICdeltaTFIIK form2 / Type: COMPLEX / Entity ID: #1-#30 / Source: NATURAL |
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| Molecular weight | Value: 1 MDa / Experimental value: YES |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.6 / Details: 20 mM HEPES PH 7.6 50 mM KOAc 5 mM DTT 2 mM MgOAc |
| Specimen | Conc.: 1 mg/ml / 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: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 1750 nm / Nominal defocus min: 750 nm / Cs: 2.7 mm / C2 aperture diameter: 100 µm |
| Image recording | Electron dose: 1.25 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: NONE | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 90136 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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FIELD EMISSION GUN