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- PDB-8zl9: ASFV p72 in complex with Fab G6 -

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Basic information

Entry
Database: PDB / ID: 8zl9
TitleASFV p72 in complex with Fab G6
Components
  • B646L
  • G6 Heavy chain
  • G6 Light chain
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / ASFV / P72 / antibody / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homologyMajor capsid protein, C-terminal / Major capsid protein, C-terminal domain superfamily / Large eukaryotic DNA virus major capsid protein / Group II dsDNA virus coat/capsid protein / viral capsid / structural molecule activity / B646L
Function and homology information
Biological speciesSus scrofa (pig)
African swine fever virus
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.36 Å
AuthorsWang, X. / Fu, W. / Yu, Q.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Cell Discov / Year: 2024
Title: p72 antigenic mapping reveals a potential supersite of vulnerability for African swine fever virus.
Authors: Qi Yu / Dening Liang / Wangjun Fu / Li Zhang / Jinglin Wang / Zhenjiang Zhang / Yao Sun / Dandan Zhu / BinYang Zheng / Ling Zhu / Ye Xiang / Dongming Zhao / Xiangxi Wang /
History
DepositionMay 17, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 18, 2024Provider: repository / Type: Initial release
Revision 1.1Oct 9, 2024Group: Data collection / Database references ...Data collection / Database references / Other / Structure summary
Category: database_2 / em_admin ...database_2 / em_admin / em_obsolete / pdbx_database_related / pdbx_entry_details / pdbx_modification_feature
Item: _em_admin.current_status / _em_admin.last_update ..._em_admin.current_status / _em_admin.last_update / _em_admin.map_release_date / _pdbx_database_related.db_id
Revision 1.2Oct 30, 2024Group: Data collection / Category: em_admin / Item: _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: G6 Heavy chain
B: G6 Light chain
C: B646L
D: B646L
E: B646L


Theoretical massNumber of molelcules
Total (without water)262,4315
Polymers262,4315
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Antibody G6 Heavy chain


Mass: 13254.960 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Sus scrofa (pig) / Production host: Homo sapiens (human)
#2: Antibody G6 Light chain


Mass: 12384.794 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Sus scrofa (pig) / Production host: Homo sapiens (human)
#3: Protein B646L / p72 / B646L CDS protein / Major capsid protein p72


Mass: 78930.531 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) African swine fever virus / Gene: p72, B646L, B646L CDS, ASFV-Georgia_4-106 / Production host: Homo sapiens (human) / References: UniProt: Q5IZK2
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: ASFV p72 in complex with Fab G6 / Type: COMPLEX / Entity ID: #2, #1, #3 / Source: RECOMBINANT
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
11African swine fever virus10497
21Sus scrofa (pig)9823
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

MicroscopyModel: FEI TITAN
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: DARK FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

CTF correctionType: NONE
3D reconstructionResolution: 4.36 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 265660 / Symmetry type: POINT

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