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Influenza neuraminidase N1-MI15-snap-174

Analyse Influenza neuraminidase N1-MI15-snap-174 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7U2T
Type
protein
Length
1,336 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Influenza N1-MI15-snap-174
Ligands
NAG
Pockets
20 · best druggability 0.64

Structure

electron microscopy · 1 distinct chain · 3% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DInfluenza N1-MI15-snap-174protein3343% helix, 51% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12830.640.8135empty
22590.640.8234empty
32800.640.8135empty
42690.640.8135empty
52280.600.8127empty

Interfaces

4 interfaces between chains.

  • B–C · 1316 Ų buried · 10 hydrogen bonds · protein-protein
  • C–D · 1315 Ų buried · 10 hydrogen bonds · protein-protein
  • A–D · 1315 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 1312 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 disulfide, 8 glycan (disulfide, N-glycosylation).

Compared structures

  • 7U2T · Influenza Neuraminidase N1-MI15-sNAp-174 · the same entry in another collection · chain A against A, TM-score 1.00

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