Human alpha-1,6-fucosyltransferase (FUT8) bound to GDP and A2-asn

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).

Ligands and binding sites

• GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, C, B, D
• MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B
• BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
• MN · Manganese (II) ion · metal · 2 copies · chains A, B
• EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
• GOL · Glycerol · additive · chains B

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

Pockets

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Interfaces

4 interfaces between chains.

• A–B · 476 Ų buried · 6 hydrogen bonds · protein-protein
• B–D · 73 Ų buried · 1 hydrogen bond · protein-protein
• A–C · 63 Ų buried · 1 hydrogen bond · protein-protein
• A–D · 13 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

• 6X5R · Human Alpha-1,6-fucosyltransferase (FUT8) bound to GDP and A2-Asn · the same entry in another collection · chain A against A, TM-score 1.00
• Q9BYC5 · AlphaFold monomer V2.0 prediction for alpha-(1,6)-fucosyltransferase (Q9BYC5) · a predicted model of the same protein · 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 Q9BYC5
• Elsewhere: RCSB PDB 6X5R · PDBe 6X5R · UniProt Q9BYC5