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Complex of influenza M2E and antibody

Analyse Complex of influenza M2E and antibody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DLM
Type
protein
Length
882 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heavy chain of monoclonal antibody; Light chain of monoclonal antibody; Matrix protein 2
UniProt
A4U6V3
Ligands
SO4
Pockets
11 · best druggability 0.77

Structure

x-ray diffraction · 4 distinct chains · 6% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HHeavy chain of monoclonal antibodyprotein2167% helix, 53% strand—
L, MLight chain of monoclonal antibodyprotein2176% helix, 53% strand—
IHeavy chain of monoclonal antibodyprotein2146% helix, 52% strand—
X, YMatrix protein 2protein90% helix, 0% strandA4U6V3

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains L, M

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

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111430.770.7987SO4
26490.660.7559empty
32490.540.7726empty
41990.520.7735empty
51450.450.7626empty

Interfaces

9 interfaces between chains.

  • I–M · 1737 Ų buried · 16 hydrogen bonds · protein-protein
  • H–L · 1685 Ų buried · 14 hydrogen bonds · protein-protein
  • L–M · 533 Ų buried · 3 hydrogen bonds · protein-protein
  • H–X · 465 Ų buried · 13 hydrogen bonds · protein-protein
  • I–Y · 449 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 5DLM · Complex of Influenza M2e and Antibody · the same entry in another collection · chain H against H, TM-score 1.00

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