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

Analyse Structure and receptor binding prefereneces of recombinant human A(H3N2) virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4WEA
Type
protein
Length
491 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hemagglutinin
UniProt
R9U684
Ligands
NAG, SIA
Pockets
4 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHemagglutininprotein49124% helix, 32% strandR9U684

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A
  • SIA · N-acetyl-alpha-neuraminic acid · sugar · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.590.9217empty
21560.410.7427empty
3680.360.7715empty
4820.330.7417SIA

Modifications

Observed in the structure: 8 glycan, 6 disulfide (N-glycosylation, disulfide).

Compared structures

  • 4WEA · Structure and receptor binding prefereneces of recombinant human A(H3N2) virus… · the same entry in another collection · chain A against A, TM-score 1.00

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