2X5I

Crystal structure echovirus 7


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.10 Å
  • R-Value Work: 0.288 
  • R-Value Observed: 0.288 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Interaction of Decay-Accelerating Factor with Echovirus 7.

Plevka, P.Hafenstein, S.Harris, K.G.Cifuente, J.O.Zhang, Y.Bowman, V.D.Chipman, P.R.Bator, C.M.Lin, F.Medof, M.E.Rossmann, M.G.

(2010) J Virol 84: 12665

  • DOI: https://doi.org/10.1128/JVI.00837-10
  • Primary Citation of Related Structures:  
    2X5I, 3IYP

  • PubMed Abstract: 

    Echovirus 7 (EV7) belongs to the Enterovirus genus within the family Picornaviridae. Many picornaviruses use IgG-like receptors that bind in the viral canyon and are required to initiate viral uncoating during infection. However, in addition, some of the enteroviruses use an alternative or additional receptor that binds outside the canyon. Decay-accelerating factor (DAF) has been identified as a cellular receptor for EV7. The crystal structure of EV7 has been determined to 3.1-Å resolution and used to interpret the 7.2-Å-resolution cryo-electron microscopy reconstruction of EV7 complexed with DAF. Each DAF binding site on EV7 is near a 2-fold icosahedral symmetry axis, which differs from the binding site of DAF on the surface of coxsackievirus B3, indicating that there are independent evolutionary processes by which DAF was selected as a picornavirus accessory receptor. This suggests that there is an advantage for these viruses to recognize DAF during the initial process of infection.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907-2054, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
VP1292Echovirus E7Mutation(s): 0 
UniProt
Find proteins for Q6W9E5 (Echovirus E7)
Explore Q6W9E5 
Go to UniProtKB:  Q6W9E5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6W9E5
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
VP2260Echovirus E7Mutation(s): 0 
UniProt
Find proteins for Q6W9E5 (Echovirus E7)
Explore Q6W9E5 
Go to UniProtKB:  Q6W9E5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6W9E5
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
VP3238Echovirus E7Mutation(s): 0 
UniProt
Find proteins for Q6W9E5 (Echovirus E7)
Explore Q6W9E5 
Go to UniProtKB:  Q6W9E5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6W9E5
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
VP470Echovirus E7Mutation(s): 0 
UniProt
Find proteins for Q6W9E5 (Echovirus E7)
Explore Q6W9E5 
Go to UniProtKB:  Q6W9E5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6W9E5
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
DAO
Query on DAO

Download Ideal Coordinates CCD File 
E [auth A]LAURIC ACID
C12 H24 O2
POULHZVOKOAJMA-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.10 Å
  • R-Value Work: 0.288 
  • R-Value Observed: 0.288 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 297.1α = 119
b = 297.7β = 100.1
c = 300.6γ = 108.4
Software Package:
Software NamePurpose
HKL-2000data reduction
HKL-2000data scaling
GLRFphasing
CNSphasing
CNSrefinement

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-12-22
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-05-08
    Changes: Data collection, Experimental preparation, Other
  • Version 1.4: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description