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Open data
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Basic information
| Entry | Database: PDB / ID: 9r78 | |||||||||||||||||||||||||||
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| Title | Human Adenovirus D 10 Capsid Structure | |||||||||||||||||||||||||||
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Keywords | VIRUS / adenovirus / capsid / conjunctivitis | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationhexon binding / viral capsid, decoration / T=25 icosahedral viral capsid / lysis of host organelle involved in viral entry into host cell / viral procapsid / microtubule-dependent intracellular transport of viral material towards nucleus / viral release from host cell / viral capsid / host cell / host cell cytoplasm ...hexon binding / viral capsid, decoration / T=25 icosahedral viral capsid / lysis of host organelle involved in viral entry into host cell / viral procapsid / microtubule-dependent intracellular transport of viral material towards nucleus / viral release from host cell / viral capsid / host cell / host cell cytoplasm / endocytosis involved in viral entry into host cell / symbiont entry into host cell / virion attachment to host cell / host cell nucleus / structural molecule activity Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Human adenovirus D10 | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||||||||||||||
Authors | Waraich, K. / Mundy, R.M. / Bates, E.A. / da Fonseca, P. / Morris, E. / Rizkallah, P.J. / Baker, A.T. / Young, M.T. / Parker, A.L. / Bhella, D. | |||||||||||||||||||||||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: Biorxiv / Year: 2025Title: Identification of a novel structural motif and overexpression of key transcripts elucidated in Adenovirus 10 Authors: Mundy, R.M. / Waraich, K. / Bates, E.A. / Rizkallah, P.J. / Baker, A.T. / Young, M.T. / Morris, E. / da Fonseca, P.C.A. / Bliss, C.M. / Matthews, D. / Bhella, D. / Parker, A.L. | |||||||||||||||||||||||||||
| 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 | 9r78.cif.gz | 4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9r78.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9r78.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r7/9r78 ftp://data.pdbj.org/pub/pdb/validation_reports/r7/9r78 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 53736MC C: citing same article ( 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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| 1 | x 60![]()
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Components
-Protein , 4 types, 25 molecules 12345678ABCDEFGHIJKLMQRST
| #1: Protein | Mass: 25546.086 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human adenovirus D10 / Gene: L3 / Production host: Homo sapiens (human) / References: UniProt: K7ZRR7#2: Protein | Mass: 106268.430 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human adenovirus D10 / Gene: L3 / Production host: Homo sapiens (human) / References: UniProt: K7ZJY8#3: Protein | | Mass: 58631.703 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human adenovirus D10 / Gene: L2 / Production host: Homo sapiens (human) / References: UniProt: K7ZQ23#6: Protein | Mass: 13773.352 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human adenovirus D10 / Gene: pIX, IX / Production host: Homo sapiens (human) / References: UniProt: K7ZLM2 |
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-Pre-hexon-linking protein ... , 2 types, 3 molecules NOP
| #4: Protein | Mass: 62170.395 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human adenovirus D10 / Gene: L1 / Production host: Homo sapiens (human) / References: UniProt: K7ZMX4 |
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| #5: Protein | Mass: 24660.668 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human adenovirus D10 / Gene: L4 / Production host: Homo sapiens (human) / References: UniProt: K7ZJY9 |
-Details
| Has protein modification | Y |
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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
| Component | Name: Human adenovirus D10 / Type: VIRUS Details: Propagation of viral stock in immortalised human cell line and purification by Caesium chloride density gradients. Entity ID: all / Source: RECOMBINANT |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Human adenovirus D10 |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Details of virus | Empty: YES / Enveloped: NO / Isolate: SPECIES / Type: VIRION |
| Buffer solution | pH: 7.4 Details: Phosphate Buffered Saline (PBS) 137 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, and 1.8 mM KH2PO4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/2 |
| 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 magnification: 105000 X / Nominal defocus max: 2200 nm / Nominal defocus min: 200 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: I (icosahedral) | ||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 5524 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT / Space: REAL |
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About Yorodumi




Human adenovirus D10
United Kingdom, 1items
Citation

PDBj




Homo sapiens (human)
FIELD EMISSION GUN