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Open data
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Basic information
| Entry | Database: PDB / ID: 11wz | |||||||||
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| Title | MPXV polymerase-E5 primase core complex | |||||||||
Components |
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Keywords | VIRAL PROTEIN/DNA / MPXV / replisome / replication / VIRAL PROTEIN / VIRAL PROTEIN-DNA complex / VIRUS / VIRAL PROTEIN-DNA-RNA complex | |||||||||
| Function / homology | Function and homology informationuracil-DNA glycosylase / uracil DNA N-glycosylase activity / viral DNA genome replication / helicase activity / DNA recombination / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / DNA replication / hydrolase activity / nucleotide binding ...uracil-DNA glycosylase / uracil DNA N-glycosylase activity / viral DNA genome replication / helicase activity / DNA recombination / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / DNA replication / hydrolase activity / nucleotide binding / DNA repair / DNA binding / ATP binding Similarity search - Function | |||||||||
| Biological species | Monkeypox virus | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||
Authors | Yu, Z. / Abarham, J. | |||||||||
| Funding support | 1items
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Citation | Journal: Nature / Year: 2026Title: Structure and operating principles of a monkeypox virus replisome Authors: Yu, Z. / Sathyanarayana, P. / Tan, J.M.J.T. / Hu, S. / Fan, X. / Gao, A. / Kranzusch, P.J. / Loparo, J.J. / Abraham, J. | |||||||||
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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 | 11wz.cif.gz | 423.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb11wz.ent.gz | 324 KB | Display | PDB format |
| PDBx/mmJSON format | 11wz.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1w/11wz ftp://data.pdbj.org/pub/pdb/validation_reports/1w/11wz | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 76148MC ![]() 10wpC ![]() 9nspC 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
-Protein , 4 types, 5 molecules ABEDC
| #1: Protein | Mass: 117176.055 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Monkeypox virusGene: F8L, E9L, MPXV-CAM1990_02-049, MPXV-Congo_8-050, MPXV-GAB1988_001-050, MPXV-Ikubi-049, MPXV_DRC_Yandongi_058, MPXV_RCG2003_358_062, MPXV_ROC_2010_001, MPXV_SUD2005_01_058, MPXV_ZAI1979_005_062, MPXVgp057 Production host: Homo sapiens (human) / References: UniProt: Q3I8V7, DNA-directed DNA polymerase | ||
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| #2: Protein | Mass: 25107.742 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Monkeypox virus / Gene: OPG116, UNG, MPXVgp099 / Production host: Homo sapiens (human) / References: UniProt: M1LL92, uracil-DNA glycosylase | ||
| #4: Protein | Mass: 90475.359 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Monkeypox virusGene: E5R, MPXV-CAM1990_02-094, MPXV-Congo_8-095, MPXV-GAB1988_001-095, MPXV-Ikubi-094, MPXV_DRC_Yandongi_103, MPXV_RCG2003_358_107, MPXV_ROC_2010_046, MPXV_SUD2005_01_103, MPXV_ZAI1979_005_107, MPXVgp102 Production host: Homo sapiens (human) / References: UniProt: Q3I8R2#5: Protein | | Mass: 49203.926 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Monkeypox virus / Gene: OPG148, MPXVgp132 / Production host: Homo sapiens (human) / References: UniProt: A0A7H0DNC0 |
-DNA chain / RNA chain , 2 types, 2 molecules TG
| #3: DNA chain | Mass: 4817.118 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Monkeypox virus |
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| #6: RNA chain | Mass: 1279.842 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Monkeypox virus |
-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
| Component | Name: RNA/DNA bound MPXV replisome in RNA elongation state / Type: COMPLEX / Entity ID: #1, #4, #2 / Source: RECOMBINANT |
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| Source (natural) | Organism: Monkeypox virus |
| Source (recombinant) | Organism: Homo sapiens (human) |
| 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: 800 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: NONE | |||||||||
| 3D reconstruction | Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 25351 / Symmetry type: POINT |
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Monkeypox virus
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Homo sapiens (human)
FIELD EMISSION GUN