› 7qa4

X-ray diffraction
2.19Å resolution

Crystal structure of stabilized H3N2 A/Hong Kong/1/1968 Hemagglutinin at 2.2 Angstrom

Released:
DOI: 10.2210/pdb7qa4/pdb
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PDB entry 7qa4 coloured by chain, front view.
PDB entry 7qa4 coloured by chain, side view.
PDB entry 7qa4 coloured by chain, top view.
Source organism: Influenza A virus (A/Hong Kong/1/1968(H3N2))
Primary publication:
Universal stabilization of the influenza hemagglutinin by structure-based redesign of the pH switch regions.
Milder FJ, Jongeneelen M, Ritschel T, Bouchier P, Bisschop IJM, de Man M, Veldman D, Le L, Kaufmann B, Bakkers MJG, Juraszek J, Brandenburg B, Langedijk JPM
OpenAccess logo Proc Natl Acad Sci U S A 119 (2022)
PMID: 35131851

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-187533 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Hemagglutinin Chain: A
Molecule details ›
Chain: A
Length: 512 amino acids
Theoretical weight: 57.13 KDa
Source organism: Influenza A virus (A/Hong Kong/1/1968(H3N2))
Expression system: Homo sapiens
UniProt:
  • Canonical: Q91MA7 (Residues: 17-521; Coverage: 92%)
Gene name: HA
Sequence domains: Haemagglutinin

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand NO3 1 x NO3
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X10SA
Spacegroup: I213
Unit cell:
a: 154.094Å b: 154.094Å c: 154.094Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.251
Expression system: Homo sapiens

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Citations

3 review citations

Stabilisation of Viral Membrane Fusion Proteins in Prefusion Conformation by Structure-Based Design for Structure Determination and Vaccine Development.
Ebel et al. (2022)
2 more

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