› 8tja

X-ray diffraction
2.05Å resolution

CRYSTAL STRUCTURE OF THE A/Ecuador/1374/2016(H3N2) INFLUENZA VIRUS HEMAGGLUTININ WITH HUMAN RECEPTOR ANALOG 6'-SLNLN

Released:
DOI: 10.2210/pdb8tja/pdb
PDB entry 8tja coloured by chain, front view.
PDB entry 8tja coloured by chain, side view.
PDB entry 8tja coloured by chain, top view.
Source organism: H3N2 subtype
Primary publication:
Evolution of human H3N2 influenza virus receptor specificity has substantially expanded the receptor-binding domain site.
Thompson AJ, Wu NC, Canales A, Kikuchi C, Zhu X, de Toro BF, Cañada FJ, Worth C, Wang S, McBride R, Peng W, Nycholat CM, Jiménez-Barbero J, Wilson IA, Paulson JC
Cell Host Microbe (2024)
PMID: 38307019

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-269279 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (5 distinct):
Hemagglutinin Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 35.79 KDa
Source organism: H3N2 subtype
Expression system: Trichoplusia ni
UniProt:
  • Canonical: A0A4P8J8E1 (Residues: 27-345; Coverage: 56%)
Gene name: HA
Sequence domains: Haemagglutinin
Hemagglutinin Chain: B
Molecule details ›
Chain: B
Length: 174 amino acids
Theoretical weight: 20 KDa
Source organism: H3N2 subtype
Expression system: Trichoplusia ni
UniProt:
  • Canonical: A0A3G1NFN9 (Residues: 314-487; Coverage: 33%)
Gene name: HA
Sequence domains: Haemagglutinin

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, GAL, SIA
Carbohydrate polymer
5 bound ligands:
Ligand NAG 4 x NAG
Ligand PG4 2 x PG4
Ligand EDO 9 x EDO
Ligand PEG 4 x PEG
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: R32
Unit cell:
a: 100.687Å b: 100.687Å c: 394.716Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.18 0.207
Expression system: Trichoplusia ni

Quick links

Citations

1 mention without citation

Epistasis mediates the evolution of the receptor binding mode in recent human H3N2 hemagglutinin.
Lei et al. (2024)