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Cryo-EM structure of mouse TLR3 in complex with UNC93B1

Analyse Cryo-EM structure of mouse TLR3 in complex with UNC93B1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7C77
Type
protein
Length
1,183 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Toll-like receptor 3; Protein unc-93 homolog B1
UniProt
Q99MB1, Q8VCW4
Ligands
NAG, BMA
Pockets
7 · best druggability 0.86

Structure

electron microscopy · 2 distinct chains · 35% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AToll-like receptor 3protein70012% helix, 17% strandQ99MB1
BProtein unc-93 homolog B1protein48369% helix, 0% strandQ8VCW4

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 19 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19280.860.8787empty
2580.670.9616empty
3880.590.8721empty
41050.400.7615empty
5670.390.7815empty

Interfaces

1 interface between chains.

  • A–B · 1456 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 glycan, 5 disulfide (N-glycosylation, disulfide).

Compared structures

  • 7C77 · Cryo-EM structure of mouse TLR3 in complex with UNC93B1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8VCW4 · AlphaFold monomer V2.0 prediction for protein unc-93 homolog B1 (Q8VCW4) · a predicted model of the same protein · chain B against A, TM-score 0.98
  • Q99MB1 · AlphaFold monomer V2.0 prediction for toll-like receptor 3 (Q99MB1) · a predicted model of the same protein · chain A against A, TM-score 0.97

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