Beat Fc with improved heterodimerization (Q3A-D84.4Q)

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 49% 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
• BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
• GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
• FUL · beta-L-fucopyranose · sugar · 2 copies · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 1109 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

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

Compared structures

• 6G1E · BEAT Fc with improved heterodimerization (Q3A-D84.4Q) · the same entry in another collection · chain A against A, TM-score 1.00
• P01860 · AlphaFold monomer V2.0 prediction for immunoglobulin heavy constant gamma 3 (P01860) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P01860
• Every structure of UniProt P0DOX5
• Elsewhere: RCSB PDB 6G1E · PDBe 6G1E · UniProt P01857 · UniProt P01860 · UniProt P0DOX5