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Open data
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Basic information
| Entry | Database: PDB / ID: 10dq | |||||||||||||||||||||
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| Title | Cbf1-CCAN-CEN complex | |||||||||||||||||||||
Components |
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Keywords | CELL CYCLE / kinetochore / centromere / DNA binding | |||||||||||||||||||||
| Function / homology | Function and homology informationCbf1-Met4-Met28 complex / positive regulation of sulfate assimilation / regulation of sulfur metabolic process / negative regulation of kinetochore assembly / positive regulation of inositol biosynthetic process / negative regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination / COMA complex / maintenance of meiotic sister chromatid cohesion / negative regulation of ceramide biosynthetic process / meiotic sister chromatid segregation ...Cbf1-Met4-Met28 complex / positive regulation of sulfate assimilation / regulation of sulfur metabolic process / negative regulation of kinetochore assembly / positive regulation of inositol biosynthetic process / negative regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination / COMA complex / maintenance of meiotic sister chromatid cohesion / negative regulation of ceramide biosynthetic process / meiotic sister chromatid segregation / Mis6-Sim4 complex / establishment of meiotic sister chromatid cohesion / ascospore formation / attachment of spindle microtubules to kinetochore / centromeric DNA binding / CENP-A containing chromatin assembly / protein localization to chromosome, centromeric region / kinetochore assembly / outer kinetochore / establishment of mitotic sister chromatid cohesion / cellular response to methionine / mitotic spindle assembly checkpoint signaling / chromosome, centromeric region / DNA replication initiation / meiotic cell cycle / chromosome segregation / kinetochore / DNA-binding transcription repressor activity, RNA polymerase II-specific / DNA-binding transcription activator activity, RNA polymerase II-specific / RNA polymerase II-specific DNA-binding transcription factor binding / protein dimerization activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / chromatin remodeling / DNA-binding transcription factor activity / cell division / regulation of transcription by RNA polymerase II / protein-containing complex binding / structural molecule activity / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / mitochondrion / nucleus Similarity search - Function | |||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å | |||||||||||||||||||||
Authors | Mengqiu, J. / Sue, B. | |||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: Native yeast kinetochore structures identify an essential inner kinetochore interaction Authors: Mengqiu, J. / Sue, B. | |||||||||||||||||||||
| 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 | 10dq.cif.gz | 684 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb10dq.ent.gz | 524.4 KB | Display | PDB format |
| PDBx/mmJSON format | 10dq.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/0d/10dq ftp://data.pdbj.org/pub/pdb/validation_reports/0d/10dq | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 75095 ![]() 75131 ![]() 75213 ![]() 10ehC ![]() 10fiC ![]() 10jcC 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
-Protein , 2 types, 3 molecules ABU
| #1: Protein | Mass: 39444.715 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | | Mass: 37562.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-DNA chain , 2 types, 2 molecules DE
| #2: DNA chain | Mass: 156413.875 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
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| #16: DNA chain | Mass: 157288.578 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
-Inner kinetochore subunit ... , 12 types, 12 molecules HIKLNOPQTWYZ
| #3: Protein | Mass: 21166.100 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #4: Protein | Mass: 84345.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 27602.541 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 28093.223 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 52743.723 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 43028.879 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 42841.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 47427.246 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 41359.785 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 10255.458 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 27006.451 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 17877.033 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Details
| Has protein modification | N |
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-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
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| Molecular weight |
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| Source (natural) |
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| Source (recombinant) | Organism: DNA molecule (others) | ||||||||||||||||||||||||||||||
| 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: 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: 2000 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 50 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: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 11639 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.9 Å 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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Escherichia phage 933W (virus)
FIELD EMISSION GUN