High-resolution crystal structure of Fc bound to its human receptor Fc-gamma-ri

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 49% strand (DSSP).

Ligands and binding sites

• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains A, B, C
• MAN · alpha-D-mannopyranose · sugar · 7 copies · chains A, B
• BMA · beta-D-mannopyranose · sugar · 3 copies · chains A, B
• GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
• FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A
• ZN · Zinc ion · metal · 6 copies · chains A, B, C
• ACT · Acetate ion · additive · 9 copies · chains A, B, C
• GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

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

Interfaces

3 interfaces between chains.

• A–B · 1205 Ų buried · 7 hydrogen bonds · protein-protein
• A–C · 671 Ų buried · 6 hydrogen bonds · protein-protein
• B–C · 532 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

• 4W4O · High-resolution crystal structure of Fc bound to its human receptor Fc-gamma-RI · the same entry in another collection · chain A against A, TM-score 1.00
• P12314 · AlphaFold monomer V2.0 prediction for high affinity immunoglobulin gamma Fc receptor I… · a predicted model of the same protein · chain C against A, TM-score 0.92

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
• Every structure of UniProt P12314
• Elsewhere: RCSB PDB 4W4O · PDBe 4W4O · UniProt P01857 · UniProt P12314