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Open data
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Basic information
| Entry | Database: PDB / ID: 9q2c | |||||||||||||||||||||||||||||||||
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| Title | Rad55-Rad57-SHU-Rad51 bound to ssDNA with AMP-PNP | |||||||||||||||||||||||||||||||||
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Keywords | DNA BINDING PROTEIN/DNA / Homologous Recombination Complex / Rad51 Paralog Complex / DNA BINDING PROTEIN / DNA BINDING PROTEIN-DNA complex | |||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationShu complex / positive regulation of single-strand break repair via homologous recombination / error-free postreplication DNA repair / heteroduplex formation / Rad51C-XRCC3 complex / Rad51B-Rad51C-Rad51D-XRCC2 complex / meiotic DNA recombinase assembly / methylated-DNA-[protein]-cysteine S-methyltransferase / methylated-DNA-[protein]-cysteine S-methyltransferase activity / meiotic chromosome segregation ...Shu complex / positive regulation of single-strand break repair via homologous recombination / error-free postreplication DNA repair / heteroduplex formation / Rad51C-XRCC3 complex / Rad51B-Rad51C-Rad51D-XRCC2 complex / meiotic DNA recombinase assembly / methylated-DNA-[protein]-cysteine S-methyltransferase / methylated-DNA-[protein]-cysteine S-methyltransferase activity / meiotic chromosome segregation / maintenance of rDNA / mitotic recombination-dependent replication fork processing / chromosome organization involved in meiotic cell cycle / DNA recombinase assembly / DNA strand invasion / mitotic recombination / DNA strand exchange activity / telomere maintenance via recombination / reciprocal meiotic recombination / recombinational repair / error-free translesion synthesis / ATP-dependent DNA damage sensor activity / DNA replication origin binding / ATP-dependent activity, acting on DNA / replication fork / telomere maintenance / condensed nuclear chromosome / double-strand break repair / site of double-strand break / single-stranded DNA binding / double-stranded DNA binding / methylation / DNA recombination / DNA repair / nucleolus / DNA binding / ATP binding / metal ion binding / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||||||||
| Biological species | ![]() ![]() synthetic construct (others) | |||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.06 Å | |||||||||||||||||||||||||||||||||
Authors | Yatskevich, S. / Koo, C.W. / Ciferri, C. | |||||||||||||||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: To Be PublishedTitle: Rad51 Paralog Complex Dynamically Templates Rad51 Filament Nucleation Authors: Yatskevich, S. / Koo, C.W. / Ciferri, C. | |||||||||||||||||||||||||||||||||
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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 | 9q2c.cif.gz | 704.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9q2c.ent.gz | 571.2 KB | Display | PDB format |
| PDBx/mmJSON format | 9q2c.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q2/9q2c ftp://data.pdbj.org/pub/pdb/validation_reports/q2/9q2c | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 72156MC ![]() 9q2eC ![]() 9q2fC ![]() 9q2hC ![]() 9q2iC ![]() 9q2lC 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
-DNA repair protein ... , 2 types, 2 molecules GB
| #1: Protein | Mass: 45239.727 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: AWRI1631_51620 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: B5VHM3 |
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| #3: Protein | Mass: 52308.301 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RAD57, YDR004W, YD8119.10 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P25301 |
-Protein , 3 types, 3 molecules ADC
| #2: Protein | Mass: 70243.594 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: RAD55, YDR076W, D4426 / Production host: Trichoplusia ni (cabbage looper)References: UniProt: E5BBQ0, UniProt: P38953, methylated-DNA-[protein]-cysteine S-methyltransferase |
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| #6: Protein | Mass: 32385.123 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: PSY3, YLR376C, L8039.17 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q12318 |
| #7: Protein | Mass: 24983.680 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: CSM2, YIL132C / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P40465 |
-Suppressor of ... , 2 types, 2 molecules EF
| #4: Protein | Mass: 17138.637 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SHU1, YHL006C / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P38751 |
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| #5: Protein | Mass: 30179.885 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SHU2, C1Q_04575 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: C7GVQ9 |
-DNA chain , 1 types, 1 molecules H
| #8: DNA chain | Mass: 2692.778 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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-Non-polymers , 4 types, 5 molecules 






| #9: Chemical | ChemComp-ANP / | ||
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| #10: Chemical | ChemComp-ADP / | ||
| #11: Chemical | | #12: 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: Rad55-Rad57-SHU-Rad51 bound to AMP-PNP and ssDNA / Type: COMPLEX / Entity ID: #1-#8 / Source: RECOMBINANT |
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| Molecular weight | Value: 0.271980 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) |
| Buffer solution | pH: 7.2 |
| 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: 2600 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 56 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.06 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 38044 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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Trichoplusia ni (cabbage looper)
FIELD EMISSION GUN