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Open data
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Basic information
| Entry | Database: PDB / ID: 9r3d | ||||||||||||||||||||||||
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| Title | Cryo-EM structure of the human pre-Bact-OTS complex (whole map) | ||||||||||||||||||||||||
Components |
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Keywords | SPLICING / spliceosome | ||||||||||||||||||||||||
| Function / homology | Function and homology informationmicrofibril / regulation of retinoic acid receptor signaling pathway / cis assembly of pre-catalytic spliceosome / regulation of vitamin D receptor signaling pathway / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / embryonic brain development / nuclear retinoic acid receptor binding / U2-type catalytic step 1 spliceosome / pre-mRNA binding / positive regulation of mRNA splicing, via spliceosome ...microfibril / regulation of retinoic acid receptor signaling pathway / cis assembly of pre-catalytic spliceosome / regulation of vitamin D receptor signaling pathway / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / embryonic brain development / nuclear retinoic acid receptor binding / U2-type catalytic step 1 spliceosome / pre-mRNA binding / positive regulation of mRNA splicing, via spliceosome / RNA splicing, via transesterification reactions / mRNA 3'-end processing / host-mediated activation of viral transcription / positive regulation of vitamin D receptor signaling pathway / U2-type precatalytic spliceosome / mRNA cis splicing, via spliceosome / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / Transport of Mature mRNA derived from an Intron-Containing Transcript / RNA polymerase binding / Notch binding / RUNX3 regulates NOTCH signaling / U2-type catalytic step 2 spliceosome / U2-type spliceosomal complex / nuclear vitamin D receptor binding / NOTCH4 Intracellular Domain Regulates Transcription / transcription elongation factor activity / RNA Polymerase II Transcription Termination / NOTCH3 Intracellular Domain Regulates Transcription / : / Basigin interactions / positive regulation of neurogenesis / K63-linked polyubiquitin modification-dependent protein binding / nuclear androgen receptor binding / ubiquitin-ubiquitin ligase activity / precatalytic spliceosome / Notch-HLH transcription pathway / WW domain binding / ubiquitin-like protein conjugating enzyme binding / Formation of paraxial mesoderm / positive regulation of transforming growth factor beta receptor signaling pathway / SMAD binding / mRNA Splicing - Minor Pathway / spliceosomal tri-snRNP complex assembly / Prp19 complex / negative regulation of transcription elongation by RNA polymerase II / U5 snRNP / U5 snRNA binding / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / pre-mRNA intronic binding / U6 snRNA binding / U2 snRNA binding / Cajal body / U1 snRNA binding / U4/U6 x U5 tri-snRNP complex / retinoic acid receptor signaling pathway / cellular response to retinoic acid / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / acrosomal vesicle / positive regulation of RNA splicing / positive regulation of protein export from nucleus / nuclear receptor binding / helicase activity / protein localization to plasma membrane / spliceosomal complex / transcription coregulator activity / response to cocaine / positive regulation of transcription elongation by RNA polymerase II / sperm end piece / Downregulation of SMAD2/3:SMAD4 transcriptional activity / mRNA splicing, via spliceosome / RING-type E3 ubiquitin transferase / positive regulation of protein import into nucleus / Golgi lumen / NOTCH1 Intracellular Domain Regulates Transcription / Pre-NOTCH Transcription and Translation / cellular response to xenobiotic stimulus / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / cellular response to tumor necrosis factor / mRNA processing / nuclear matrix / protein tag activity / protein polyubiquitination / calcium-dependent protein binding / rRNA processing / osteoblast differentiation / transcription corepressor activity / ubiquitin protein ligase activity / single-stranded DNA binding / sperm principal piece / protein folding / microtubule cytoskeleton / cellular response to lipopolysaccharide / RNA polymerase II-specific DNA-binding transcription factor binding / transcription coactivator activity / RNA helicase activity / nuclear speck / cilium Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.12 Å | ||||||||||||||||||||||||
Authors | Zhang, Z. / Kumar, V. / Zhong, J. / Dybkov, O. / Kastner, B. / Urlaub, H. / Luhrmann, R. | ||||||||||||||||||||||||
| Funding support | Germany, 1items
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Citation | Journal: To Be PublishedTitle: cryo-EM structure of the human pre-Bact-OTS complex Authors: Zhang, Z. / Kumar, V. / Dybkov, O. / Zhong, J. / Kastner, B. / Henning, U. / Luehrmann, R. | ||||||||||||||||||||||||
| 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 | 9r3d.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9r3d.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9r3d.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r3/9r3d ftp://data.pdbj.org/pub/pdb/validation_reports/r3/9r3d | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 53554 M: map data used to model this data |
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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
-RNA chain , 3 types, 3 molecules 56Z
| #1: RNA chain | Mass: 24496.414 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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| #2: RNA chain | Mass: 27447.449 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
| #10: RNA chain | Mass: 9307.604 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
-Protein , 12 types, 12 molecules BCKQTXqrP7AtS1
| #3: Protein | Mass: 244823.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75643, RNA helicase |
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| #4: Protein | Mass: 109560.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15029 |
| #6: Protein | Mass: 52050.527 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P55081 |
| #7: Protein | Mass: 17032.850 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P41223 |
| #8: Protein | Mass: 124083.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O14776 |
| #9: Protein | Mass: 70098.641 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y2W2 |
| #11: Protein | Mass: 8560.945 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BZL1 |
| #12: Protein | Mass: 23664.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96NC0 |
| #13: Protein | Mass: 65612.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O60508 |
| #14: Protein | Mass: 273974.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q6P2Q9 |
| #16: Protein | Mass: 58910.379 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: Q13356, RING-type E3 ubiquitin transferase |
| #17: Protein | Mass: 60326.215 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q13573 |
-Pre-mRNA-splicing factor ... , 2 types, 2 molecules IP
| #5: Protein | Mass: 37563.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8NAV1 |
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| #15: Protein | Mass: 46959.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NW64 |
-Non-polymers , 1 types, 1 molecules 
| #18: Chemical | ChemComp-IHP / |
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-Details
| Has ligand of interest | Y |
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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: pre-Bact-OTS-complex / Type: COMPLEX / Entity ID: #1-#17 / Source: NATURAL |
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| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.9 |
| 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: 4000 nm / Nominal defocus min: 1500 nm |
| Image recording | Electron dose: 39 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.12 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 35015 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
Germany, 1items
Citation
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FIELD EMISSION GUN