› 4f23

X-ray diffraction
1.7Å resolution

Influenza A virus hemagglutinin H16 HA0 structure with an alpha-helix conformation in the cleavage site: a potential drug target

Released:
DOI: 10.2210/pdb4f23/pdb
PDB entry 4f23 coloured by chain, front view.
PDB entry 4f23 coloured by chain, side view.
PDB entry 4f23 coloured by chain, top view.
Source organism: Influenza A virus (A/black-headed gull/Sweden/2/99(H16N3))
Primary publication:
Insights into avian influenza virus pathogenicity: the hemagglutinin precursor HA0 of subtype H16 has an alpha-helix structure in its cleavage site with inefficient HA1/HA2 cleavage.
Lu X, Shi Y, Gao F, Xiao H, Wang M, Qi J, Gao GF
J Virol 86 12861-70 (2012)
PMID: 22993148

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Hemagglutinin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 515 amino acids
Theoretical weight: 58.01 KDa
Source organism: Influenza A virus (A/black-headed gull/Sweden/2/99(H16N3))
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q5DL24 (Residues: 14-519; Coverage: 90%)
Gene name: HA
Sequence domains: Haemagglutinin
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand NAG 3 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P21
Unit cell:
a: 69.332Å b: 240.944Å c: 69.673Å
α: 90° β: 119.79° γ: 90°
R-values:
R R work R free
0.161 0.16 0.192
Expression system: Spodoptera frugiperda

Quick links

Citations

4 review citations

Evolutionary dynamics of highly pathogenic avian influenza A/H5N1 HA clades and vaccine implementation in Vietnam.
Le et al. (2014)
3 more

8 mentions without citation

Role of electrostatic repulsion in controlling pH-dependent conformational changes of viral fusion proteins.
Harrison et al. (2013)
7 more