4WSV

The crystal structure of hemagglutinin from A/Taiwan/1/2013 in complex with 6'SLN

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.10 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.246 
  • R-Value Observed: 0.248 

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Literature

Structure and receptor binding preferences of recombinant hemagglutinins from avian and human h6 and h10 influenza a virus subtypes.

Yang, H., Carney, P.J., Chang, J.C., Villanueva, J.M., Stevens, J.

(2015) J Virol 89: 4612-4623

  • DOI: https://doi.org/10.1128/JVI.03456-14
  • Primary Citation of Related Structures:  
    4WSR, 4WSS, 4WST, 4WSU, 4WSV, 4WSW, 4WSX

  • PubMed Abstract: 

    During 2013, three new avian influenza A virus subtypes, A(H7N9), A(H6N1), and A(H10N8), resulted in human infections. While the A(H7N9) virus resulted in a significant epidemic in China across 19 provinces and municipalities, both A(H6N1) and A(H10N8) viruses resulted in only a few human infections. This study focuses on the major surface glycoprotein hemagglutinins from both of these novel human viruses. The detailed structural and glycan microarray analyses presented here highlight the idea that both A(H6N1) and A(H10N8) virus hemagglutinins retain a strong avian receptor binding preference and thus currently pose a low risk for sustained human infections.

    • Organizational Affiliation: 

    Influenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hemagglutinin HA1 chainA,
B [auth C],
C [auth E]		334H6N1 subtypeMutation(s): 0 
UniProt
Find proteins for A0A0J9X248 (H6N1 subtype)
Explore A0A0J9X248 
Go to UniProtKB:  A0A0J9X248
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0J9X248
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Hemagglutinin HA2 chainD [auth B],
E [auth D],
F		181H6N1 subtypeMutation(s): 0 
UniProt
Find proteins for A0A0J9X249 (H6N1 subtype)
Explore A0A0J9X249 
Go to UniProtKB:  A0A0J9X249
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0J9X249
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SIA
Query on SIA
Download Ideal Coordinates CCD File 
J [auth A],
Q [auth E]		N-acetyl-alpha-neuraminic acid
C11 H19 N O9
SQVRNKJHWKZAKO-YRMXFSIDSA-N
NAG
Query on NAG
Download Ideal Coordinates CCD File 
G [auth A]
H [auth A]
I [auth A]
K [auth C]
L [auth C]
G [auth A],
H [auth A],
I [auth A],
K [auth C],
L [auth C],
M [auth C],
N [auth E],
O [auth E],
P [auth E]
2-acetamido-2-deoxy-beta-D-glucopyranose
C8 H15 N O6
OVRNDRQMDRJTHS-FMDGEEDCSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.10 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.246 
  • R-Value Observed: 0.248 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 186.438α = 90
b = 99.584β = 125.96
c = 134.216γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-02-25
    Type: Initial release
  • Version 1.1: 2015-04-01
    Changes: Database references
  • Version 1.2: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Database references, Derived calculations, Source and taxonomy, Structure summary
  • Version 1.3: 2023-12-27
    Changes: Data collection, Database references, Structure summary