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Crystal structure of the haemagglutinin from a transmissible H10N7 seal influenza virus isolated in netherland

Analyse Crystal structure of the haemagglutinin from a transmissible H10N7 seal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6TVC
Type
protein
Length
1,473 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Haemagglutinin HA1; Haemagglutinin HA2
UniProt
A0A0A7HR51
Ligands
NAG
Pockets
16 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, EHaemagglutinin HA1protein3198% helix, 41% strandA0A0A7HR51
B, D, FHaemagglutinin HA2protein17254% helix, 14% strandA0A0A7HR51

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, E, F

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

Pockets

16 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111680.840.85141empty
21860.830.9724empty
3800.750.9817empty
4800.740.9717empty
5760.730.9716empty

Interfaces

15 interfaces between chains.

  • A–B · 3246 Ų buried · 43 hydrogen bonds · protein-protein
  • E–F · 3236 Ų buried · 46 hydrogen bonds · protein-protein
  • C–D · 3180 Ų buried · 41 hydrogen bonds · protein-protein
  • D–F · 1509 Ų buried · 20 hydrogen bonds · protein-protein
  • B–F · 1487 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 17 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

  • 6TVC · Crystal structure of the haemagglutinin from a transmissible H10N7 seal influenza virus… · the same entry in another collection · chain A against A, TM-score 1.00

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