1QHV

HUMAN ADENOVIRUS SEROTYPE 2 FIBRE HEAD


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.51 Å
  • R-Value Free: 0.143 
  • R-Value Work: 0.109 

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This is version 1.3 of the entry. See complete history


Literature

Structure of the human adenovirus serotype 2 fiber head domain at 1.5 A resolution.

van Raaij, M.J.Louis, N.Chroboczek, J.Cusack, S.

(1999) Virology 262: 333-343

  • DOI: https://doi.org/10.1006/viro.1999.9849
  • Primary Citation of Related Structures:  
    1QHV

  • PubMed Abstract: 

    Adenovirus binds to its receptor via the head domain of its fiber protein. We have crystallized the adenovirus serotype 2 (subgroup C) receptor binding domain and solved the structure at 1.5 A resolution by the molecular replacement technique using the known adenovirus type 5 head structure. Included in the high-resolution model are 306 water molecules, five alternative side chain conformations, and individual anisotropic temperature factors for each atom. The overall structure of the serotype 2 head is very similar to its serotype 5 homologue, apart from differences in some of the flexible loops. All but subgroup B adenoviruses are believed to use the recently identified protein CAR (Coxsackievirus and adenovirus receptor) as receptor. By comparison of the two structures and sequence alignment of CAR binding and non-CAR binding serotype fiber heads, we discuss possible receptor binding sites and propose a receptor binding site in a crevice between two monomers on the side of the trimer. The structural basis of the extraordinary stability of the fiber head trimer is also discussed.


  • Organizational Affiliation

    c/o Institut Laue Langevin, 6 rue Jules Horowitz, Grenoble Cedex 9, 38000, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (ADENOVIRUS FIBRE)195Human adenovirus 2Mutation(s): 0 
Gene Names: LOCUS AD2H2
UniProt
Find proteins for P03275 (Human adenovirus C serotype 2)
Explore P03275 
Go to UniProtKB:  P03275
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03275
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.51 Å
  • R-Value Free: 0.143 
  • R-Value Work: 0.109 
  • Space Group: P 3 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 95.35α = 90
b = 95.35β = 90
c = 48.8γ = 120
Software Package:
Software NamePurpose
AMoREphasing
REFMACrefinement
MOSFLMdata reduction
CCP4data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-09-29
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2023-08-16
    Changes: Data collection, Database references, Derived calculations, Refinement description