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Fc-fragment of monoclonal antibody IGG2B from mus musculus

Analyse Fc-fragment of monoclonal antibody IGG2B from mus musculus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2RGS
Type
protein
Length
413 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ig gamma-2B heavy chain
UniProt
P01867
Ligands
NAG, MAN, GAL, FUC
Pockets
4 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIg gamma-2B heavy chainprotein20611% helix, 51% strandP01867
BIg gamma-2B heavy chainprotein20711% helix, 51% strandP01867

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
  • MAN · alpha-D-mannopyranose · sugar · 6 copies · chains A, B
  • GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
  • FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1920.410.7920empty
2940.410.7820empty
3700.350.7620empty
4660.340.7614empty

Interfaces

1 interface between chains.

  • A–B · 1077 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 2RGS · FC-fragment of monoclonal antibody IGG2B from Mus musculus · the same entry in another collection · chain A against A, TM-score 1.00
  • P01867 · AlphaFold monomer V2.0 prediction for ig gamma-2B chain C region (P01867) · a predicted model of the same protein · chain A against A, TM-score 0.99

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