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Open data
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Basic information
| Entry | Database: PDB / ID: 9pb7 | |||||||||
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| Title | TFIIH of PIC-Med-SWI/SNF | |||||||||
Components |
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Keywords | TRANSCRIPTION/DNA / SWI/SNF / PIC / TRANSCRIPTION / TRANSCRIPTION-DNA complex | |||||||||
| Function / homology | Function and homology informationcarbon catabolite activation of transcription / NuA3b histone acetyltransferase complex / NuA3a histone acetyltransferase complex / NuA3 histone acetyltransferase complex / positive regulation of invasive growth in response to glucose limitation / regulation of mitotic recombination / transcription open complex formation at RNA polymerase II promoter / phosphatidylinositol-5-phosphate binding / RNA polymerase II promoter clearance / positive regulation of mitotic recombination ...carbon catabolite activation of transcription / NuA3b histone acetyltransferase complex / NuA3a histone acetyltransferase complex / NuA3 histone acetyltransferase complex / positive regulation of invasive growth in response to glucose limitation / regulation of mitotic recombination / transcription open complex formation at RNA polymerase II promoter / phosphatidylinositol-5-phosphate binding / RNA polymerase II promoter clearance / positive regulation of mitotic recombination / nucleotide-excision repair factor 3 complex / nucleotide-excision repair, preincision complex assembly / DNA translocase activity / transcriptional start site selection at RNA polymerase II promoter / transcription factor TFIIK complex / transcription factor TFIIF complex / phosphatidylinositol-3-phosphate binding / mediator complex / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / Ino80 complex / cyclin-dependent protein serine/threonine kinase activator activity / SWI/SNF complex / DNA 5'-3' helicase / transcription preinitiation complex / poly(A)+ mRNA export from nucleus / transcription factor TFIID complex / RNA polymerase II general transcription initiation factor activity / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / Formation of TC-NER Pre-Incision Complex / RNA Polymerase I Promoter Escape / 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 / nuclear chromosome / RNA Polymerase II Pre-transcription Events / ATPase activator activity / Gap-filling DNA repair synthesis and ligation in TC-NER / DNA 3'-5' helicase / Dual incision in TC-NER / ATP-dependent activity, acting on DNA / 3'-5' DNA helicase activity / RNA polymerase II preinitiation complex assembly / transcription by RNA polymerase I / DNA helicase activity / transcription initiation at RNA polymerase II promoter / double-strand break repair via homologous recombination / nucleotide-excision repair / transcription by RNA polymerase II / 4 iron, 4 sulfur cluster binding / ubiquitin protein ligase activity / double-stranded DNA binding / histone binding / 5'-3' DNA helicase activity / damaged DNA binding / RNA polymerase II-specific DNA-binding transcription factor binding / chromatin remodeling / DNA repair / regulation of transcription by RNA polymerase II / regulation of DNA-templated transcription / chromatin / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA-templated transcription / DNA binding / zinc ion binding / ATP binding / nucleus / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.4 Å | |||||||||
Authors | Yang, C. / Nagai, S. / Chen, D.-H. | |||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: Structure of TFIIH of PIC-Med-SWI/SNF Authors: Yang, C. / Nagai, S. / Chen, D.-H. | |||||||||
| 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 | 9pb7.cif.gz | 642.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9pb7.ent.gz | 492.6 KB | Display | PDB format |
| PDBx/mmJSON format | 9pb7.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pb/9pb7 ftp://data.pdbj.org/pub/pdb/validation_reports/pb/9pb7 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 71456MC ![]() 9pb2 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
-General transcription and DNA repair factor IIH subunit ... , 5 types, 5 molecules 54612
| #1: Protein | Mass: 8243.490 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #9: Protein | Mass: 37506.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 52370.035 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 72993.328 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: 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
| #2: Protein | Mass: 89899.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #4: Protein | Mass: 95461.664 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 3 types, 3 molecules 389
| #3: Protein | Mass: 38188.438 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #5: Protein | Mass: 102642.172 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 27473.154 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA chain , 2 types, 2 molecules NT
| #7: DNA chain | Mass: 8007.186 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
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| #8: DNA chain | Mass: 7963.193 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
-Non-polymers , 2 types, 8 molecules 


| #13: Chemical | ChemComp-SF4 / |
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| #14: Chemical | ChemComp-ZN / |
-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: TFIIH of PIC-Med-SWI/SNF / Type: COMPLEX / Entity ID: #1-#12 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.5 Details: 40 mM Hepes-KOH pH 7.5 100 mM potassium acetate 2 mM magnesium acetate 5 mM DTT |
| 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Average exposure time: 4 sec. / Electron dose: 40.8 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 433107 / Symmetry type: POINT | ||||||||||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT | ||||||||||||||||||||||||
| Refinement | Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






United States, 1items
Citation


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