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Structure of influenza haemagglutinin at the pH of membrane fusion

Analyse Structure of influenza haemagglutinin at the pH of membrane fusion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HTM
Type
protein
Length
379 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hemagglutinin HA1 chain; Hemagglutinin HA2 chain
UniProt
P03437
Pockets
5 · best druggability 0.47

Structure

x-ray diffraction · 5 distinct chains · 67% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHemagglutinin HA1 chainprotein50% helix, 40% strandP03437
BHemagglutinin HA2 chainprotein11475% helix, 4% strandP03437
CHemagglutinin HA1 chainprotein60% helix, 50% strandP03437
D, FHemagglutinin HA2 chainprotein12370% helix, 5% strandP03437
EHemagglutinin HA1 chainprotein80% helix, 50% strandP03437

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11620.470.7628empty
21360.430.7624empty
3740.350.7615empty
4880.340.7514empty
5760.330.7515empty

Interfaces

6 interfaces between chains.

  • B–F · 1827 Ų buried · 23 hydrogen bonds · protein-protein
  • D–F · 1704 Ų buried · 19 hydrogen bonds · protein-protein
  • B–D · 1650 Ų buried · 14 hydrogen bonds · protein-protein
  • E–F · 535 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 401 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 1HTM · Structure of influenza haemagglutinin at the pH of membrane fusion · the same entry in another collection · chain A against A, TM-score 1.00

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