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Fc abvance: increasing our knowledge of antibody structural space to enable faster and better decision-making in antibody drug discovery.

Analyse Fc abvance: increasing our knowledge of antibody structural space to enable… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5WAV
Type
protein
Length
414 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Immunoglobulin gamma-1 heavy CHAIN,IMMUNOGLOBULIN gamma-1 heavy chain
UniProt
P0DOX5
Ligands
NAG, MAN, FUC
Pockets
1 · best druggability 0.27

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AImmunoglobulin gamma-1 heavy CHAIN,IMMUNOGLOBULIN gamma-1 heavy chainprotein20712% helix, 48% strandP0DOX5
BImmunoglobulin gamma-1 heavy CHAIN,IMMUNOGLOBULIN gamma-1 heavy chainprotein20712% helix, 47% strandP0DOX5

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
  • FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A
  • GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.270.7516empty

Interfaces

1 interface between chains.

  • A–B · 1141 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 5WAV · Fc AbVance: Increasing our knowledge of antibody structural space to enable faster and… · the same entry in another collection · chain A against A, TM-score 1.00

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