6LA7

Cryo-EM structure of echovirus 11 complexed with its uncoating receptor FcRn at pH 5.5


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.82 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Molecular and structural basis of Echovirus 11 infection by using the dual-receptor system of CD55 and FcRn.

Niu, S.Liu, C.Liu, C.Liu, S.Song, Y.Zhang, Y.Tian, W.Zhao, X.Wang, P.Gao, F.G.

(2020) Chin Sci Bull 


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP1285Echovirus E11Mutation(s): 0 
UniProt
Find proteins for Q2LJ73 (Echovirus E11)
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Go to UniProtKB:  Q2LJ73
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UniProt GroupQ2LJ73
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP2251Echovirus E11Mutation(s): 0 
UniProt
Find proteins for A0A0R5YS56 (Echovirus E11)
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Go to UniProtKB:  A0A0R5YS56
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UniProt GroupA0A0R5YS56
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP3238Echovirus E11Mutation(s): 0 
UniProt
Find proteins for A0A346I7K2 (Echovirus E11)
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Go to UniProtKB:  A0A346I7K2
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UniProt GroupA0A346I7K2
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP470Echovirus E11Mutation(s): 0 
UniProt
Find proteins for E0WN77 (Echovirus E11)
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UniProt GroupE0WN77
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
IgG receptor FcRn large subunit p51263Homo sapiensMutation(s): 0 
Gene Names: FCRN
UniProt & NIH Common Fund Data Resources
Find proteins for P55899 (Homo sapiens)
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PHAROS:  P55899
GTEx:  ENSG00000104870 
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UniProt GroupP55899
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-2-microglobulin99Homo sapiensMutation(s): 0 
Gene Names: B2M
UniProt & NIH Common Fund Data Resources
Find proteins for P61769 (Homo sapiens)
Explore P61769 
Go to UniProtKB:  P61769
PHAROS:  P61769
GTEx:  ENSG00000166710 
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UniProt GroupP61769
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Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.82 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2020-10-07
    Type: Initial release