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Open data
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Basic information
| Entry | Database: PDB / ID: 9lgo | |||||||||||||||
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| Title | Cryo-EM structure of the SPATA5-SPATA5L1-CINP-C1orf109 complex | |||||||||||||||
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Keywords | CYTOSOLIC PROTEIN / ribosomal biogenesis / SPATA5 / ATPase complex | |||||||||||||||
| Function / homology | Function and homology informationpreribosome binding / mitotic spindle disassembly / VCP-NPL4-UFD1 AAA ATPase complex / retrograde protein transport, ER to cytosol / non-chaperonin molecular chaperone ATPase / polyubiquitin modification-dependent protein binding / autophagosome maturation / ribosomal large subunit biogenesis / brain development / spindle ...preribosome binding / mitotic spindle disassembly / VCP-NPL4-UFD1 AAA ATPase complex / retrograde protein transport, ER to cytosol / non-chaperonin molecular chaperone ATPase / polyubiquitin modification-dependent protein binding / autophagosome maturation / ribosomal large subunit biogenesis / brain development / spindle / spermatogenesis / proteasome-mediated ubiquitin-dependent protein catabolic process / cell differentiation / DNA replication / cell division / DNA repair / ATP hydrolysis activity / ATP binding / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.51 Å | |||||||||||||||
Authors | Dai, Y. / Zhang, Y. / Gao, N. | |||||||||||||||
| Funding support | China, 1items
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Citation | Journal: To Be PublishedTitle: cryo-EM structure of the SPATA5-SPATA5L1-CINP-C1orf109 complex Authors: Dai, Y. / Zhang, Y. / Gao, N. | |||||||||||||||
| 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 | 9lgo.cif.gz | 851.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9lgo.ent.gz | 694.3 KB | Display | PDB format |
| PDBx/mmJSON format | 9lgo.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9lgo_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 9lgo_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 9lgo_validation.xml.gz | 118.9 KB | Display | |
| Data in CIF | 9lgo_validation.cif.gz | 191.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lg/9lgo ftp://data.pdbj.org/pub/pdb/validation_reports/lg/9lgo | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 63069MC 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
-ATPase family gene 2 protein homolog ... , 2 types, 6 molecules AEDBFC
| #1: Protein | Mass: 97276.453 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AFG2A, SPAF, SPATA5 / Production host: Homo sapiens (human)References: UniProt: Q8NB90, non-chaperonin molecular chaperone ATPase #4: Protein | Mass: 80409.742 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AFG2B, SPATA5L1 / Production host: Homo sapiens (human)References: UniProt: Q9BVQ7, non-chaperonin molecular chaperone ATPase |
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-Protein , 2 types, 4 molecules JIHG
| #2: Protein | Mass: 27421.090 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CINP / Production host: Homo sapiens (human) / References: UniProt: Q9BW66#3: Protein | Mass: 31592.270 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) / References: UniProt: B4DRQ5 |
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-Non-polymers , 2 types, 9 molecules 


| #5: Chemical | ChemComp-ATP / #6: Chemical | ChemComp-MG / | |
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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: The SPATA5 complex / Type: COMPLEX / Entity ID: #1-#4 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| Specimen | Conc.: 1.2 mg/ml / 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: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
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| 3D reconstruction | Resolution: 3.51 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 194789 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.51 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
China, 1items
Citation



PDBj





FIELD EMISSION GUN