› 4wea

X-ray diffraction
2.2Å resolution

Structure and receptor binding prefereneces of recombinant human A(H3N2) virus hemagglutinins

Released:
DOI: 10.2210/pdb4wea/pdb
PDB 4wea coloured by chain and viewed from the front.
PDB 4wea coloured by chain and viewed from the side.
PDB 4wea coloured by chain and viewed from the top.
Source organism: Influenza A virus (A/Singapore/H2011.447/2011(H3N2))
Primary publication:
Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins.
Yang H, Carney PJ, Chang JC, Guo Z, Villanueva JM, Stevens J
Virology 477C 18-31 (2015)
PMID: 25617824

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Hemagglutinin Chain: A
Molecule details ›
Chain: A
Length: 515 amino acids
Theoretical weight: 57.84 KDa
Source organism: Influenza A virus (A/Singapore/H2011.447/2011(H3N2))
Expression system: Trichoplusia ni
UniProt:
  • Canonical: R9U684 (Residues: 17-519; Coverage: 89%)
Gene name: HA
Sequence domains: Haemagglutinin
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 7 x NAG
Ligand SIA 1 x SIA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: R32
Unit cell:
a: 100.733Å b: 100.733Å c: 382.613Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.19 0.223
Expression system: Trichoplusia ni

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Citations

7 review citations

A changing trend in diagnostic methods of Influenza A (H3N2) virus in human: a review.
Ravina et al. (2021)
6 more

6 mentions without citation

Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins.
Yang et al. (2015)
5 more