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Crystal structure of stabilized H3N2 A/HONG KONG/1/1968 hemagglutinin at 2.2 ångström

Analyse Crystal structure of stabilized H3N2 A/HONG KONG/1/1968 hemagglutinin at 2.2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7QA4
Type
protein
Length
488 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hemagglutinin
UniProt
Q91MA7
Ligands
NAG, BMA, MAN, NO3
Pockets
3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHemagglutininprotein48825% helix, 32% strandQ91MA7

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A
  • BMA · beta-D-mannopyranose · sugar · 2 copies
  • MAN · alpha-D-mannopyranose · sugar · 2 copies
  • NO3 · Nitrate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.590.9217empty
2640.510.8617empty
31560.410.7425empty

Modifications

Observed in the structure: 6 disulfide, 5 glycan (disulfide, N-glycosylation).

Compared structures

  • 7QA4 · Crystal structure of stabilized H3N2 A/Hong Kong/1/1968 Hemagglutinin at 2.2 Angstrom · the same entry in another collection · chain A against A, TM-score 1.00

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