Role of the hinge and C-gamma-2/C-gamma-3 interface in immunoglobin G1 Fc domain motions: implications for Fc engineering

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 48% strand (DSSP).

Ligands and binding sites

• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
• MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B
• GAL · beta-D-galactopyranose · sugar · 3 copies · chains A, B
• BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
• FUL · beta-L-fucopyranose · sugar · 2 copies · chains A, B
• PG4 · Tetraethylene glycol · additive · chains A

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

Interfaces

1 interface between chains.

• A–B · 1166 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

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

Compared structures

• 4KU1 · Role of the hinge and C-gamma-2/C-gamma-3 interface in immunoglobin G1 Fc domain motions… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P01857
• Elsewhere: RCSB PDB 4KU1 · PDBe 4KU1 · UniProt P01857