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Open data
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Basic information
Entry | Database: PDB / ID: 5o85 | ||||||||||||||||||
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Title | p34-p44 complex | ||||||||||||||||||
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![]() | TRANSCRIPTION / DNA repair / TFIIH / TFIIH interaction network / p34-p44 complex | ||||||||||||||||||
Function / homology | ![]() core TFIIH complex portion of holo TFIIH complex / G protein-coupled receptor internalization / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / transcription preinitiation complex / RNA Polymerase I Transcription Termination / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / transcription factor TFIID complex / Formation of the Early Elongation Complex ...core TFIIH complex portion of holo TFIIH complex / G protein-coupled receptor internalization / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / transcription preinitiation complex / RNA Polymerase I Transcription Termination / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / transcription factor TFIID complex / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / RNA polymerase II general transcription initiation factor activity / mRNA Capping / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / 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 I Transcription Initiation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / response to UV / RNA Polymerase II Pre-transcription Events / nucleotide-excision repair / transcription initiation at RNA polymerase II promoter / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase I Promoter Escape / NoRC negatively regulates rRNA expression / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / Dual Incision in GG-NER / Formation of Incision Complex in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription by RNA polymerase II / nuclear speck / DNA repair / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleus / metal ion binding Similarity search - Function | ||||||||||||||||||
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Method | ![]() ![]() ![]() | ||||||||||||||||||
![]() | Radu, L. / Poterszman, A. | ||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: The intricate network between the p34 and p44 subunits is central to the activity of the transcription/DNA repair factor TFIIH. Authors: Radu, L. / Schoenwetter, E. / Braun, C. / Marcoux, J. / Koelmel, W. / Schmitt, D.R. / Kuper, J. / Cianferani, S. / Egly, J.M. / Poterszman, A. / Kisker, C. | ||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 123.9 KB | Display | ![]() |
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PDB format | ![]() | 88 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5nusC ![]() 5obzC ![]() 4pn7S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 34416.008 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 44465.934 Da / Num. of mol.: 2 / Mutation: C381S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-ZN / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.82 Å3/Da / Density % sol: 56.41 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 0.1 mM Tris-HCl or Hepes (pH 7.0 to 8.5) and 20-40% PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 13, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.28236 Å / Relative weight: 1 |
Reflection | Resolution: 3.19→46.55 Å / Num. obs: 141682 / % possible obs: 99.4 % / Redundancy: 13.1 % / CC1/2: 0.995 / Rmerge(I) obs: 0.149 / Rpim(I) all: 0.061 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 3.19→3.39 Å / Redundancy: 12.8 % / Rmerge(I) obs: 3.092 / Mean I/σ(I) obs: 1 / Num. unique all: 19316 / CC1/2: 0.593 / Rpim(I) all: 1.272 / % possible all: 96.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4pn7 Resolution: 3.4→40.7 Å / SU ML: 0.51 / Cross valid method: FREE R-VALUE / σ(F): 1.91 / Phase error: 38.54
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.4→40.7 Å
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Refine LS restraints |
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LS refinement shell |
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