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Crystal structure of H15 hemagglutinin from A/SHEARWATER/WA/2576/1979 H15N9 influenza virus

Analyse Crystal structure of H15 hemagglutinin from A/SHEARWATER/WA/2576/1979 H15N9… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TG8
Type
protein
Length
994 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hemagglutinin HA1 chain; Hemagglutinin HA2 chain
UniProt
L0L3X3
Ligands
NAG
Pockets
10 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CHemagglutinin HA1 chainprotein3288% helix, 37% strandL0L3X3
B, DHemagglutinin HA2 chainprotein16947% helix, 15% strandL0L3X3

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, C, B, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17010.640.7467NAG
22060.600.8122empty
32000.600.8122empty
4930.440.8019empty
51050.440.7821empty

Interfaces

4 interfaces between chains.

  • A–B · 3066 Ų buried · 54 hydrogen bonds · protein-protein
  • C–D · 3047 Ų buried · 50 hydrogen bonds · protein-protein
  • A–D · 285 Ų buried · 1 hydrogen bond · protein-protein
  • A–C · 76 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

  • 5TG8 · Crystal structure of H15 hemagglutinin from A/shearwater/WA/2576/1979 H15N9 influenza… · the same entry in another collection · chain A against A, TM-score 1.00

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