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Crystal structure of H7 hemagglutinin mutant H7-svtq ( A138S, P221T, L226Q) with 3'SLN

Analyse Crystal structure of H7 hemagglutinin mutant H7-svtq ( A138S, P221T, L226Q)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IDZ
Type
protein
Length
479 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hemagglutinin HA1 chain; Hemagglutinin HA2 chain
UniProt
R4NN21
Ligands
NAG, GAL, SIA
Pockets
4 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHemagglutinin HA1 chainprotein3179% helix, 40% strandR4NN21
BHemagglutinin HA2 chainprotein16253% helix, 12% strandR4NN21

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B
  • GAL · beta-D-galactopyranose · sugar · 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
12290.630.8225empty
2980.470.8021empty
3540.400.8218empty
4500.270.7413empty

Interfaces

1 interface between chains.

  • A–B · 3161 Ų buried · 47 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 6IDZ · Crystal structure of H7 hemagglutinin mutant H7-SVTQ ( A138S, P221T, L226Q) with 3'SLN · the same entry in another collection · chain A against A, TM-score 1.00

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