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Inhibitory mechanism of an allosteric antibody targeting the glucagon receptor

Analyse Inhibitory mechanism of an allosteric antibody targeting the glucagon receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4LF3
Type
protein
Length
1,079 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab heavy chain; Fab light chain; Glucagon receptor
UniProt
P47871
Pockets
11 · best druggability 0.57

Structure

x-ray diffraction · 4 distinct chains · 12% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DFab heavy chainprotein2146% helix, 50% strand—
B, EFab light chainprotein2319% helix, 53% strand—
CGlucagon receptorprotein9521% helix, 25% strandP47871
FGlucagon receptorprotein9427% helix, 26% strandP47871

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12210.570.8030empty
22000.540.7829empty
31780.530.7936empty
42430.490.7437empty
51580.460.7622empty

Interfaces

7 interfaces between chains.

  • D–E · 1781 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 1725 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 639 Ų buried · 10 hydrogen bonds · protein-protein
  • E–F · 614 Ų buried · 11 hydrogen bonds · protein-protein
  • B–E · 348 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

  • 4LF3 · Inhibitory Mechanism of an Allosteric Antibody Targeting the Glucagon Receptor · the same entry in another collection · chain A against A, TM-score 1.00
  • P47871 · AlphaFold monomer V2.0 prediction for glucagon receptor (P47871) · a predicted model of the same protein · chain F against A, TM-score 0.98

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