Human alpha-1,6-fucosyltransferase (FUT8) bound to GDP and A3-asn

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).

Ligands and binding sites

• GDP · Guanosine-5'-diphosphate · ligand · 8 copies · chains A, B, C, D, E, F, G, H
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains A, D, E, H
• BMA · beta-D-mannopyranose · sugar · 4 copies · chains A, D, E, H
• MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, D, E, H
• GOL · Glycerol · additive · 2 copies · chains A, F

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Interfaces

9 interfaces between chains.

• A–B · 3386 Ų buried · 28 hydrogen bonds · protein-protein
• C–D · 3362 Ų buried · 24 hydrogen bonds · protein-protein
• E–F · 3272 Ų buried · 28 hydrogen bonds · protein-protein
• G–H · 3175 Ų buried · 24 hydrogen bonds · protein-protein
• B–C · 925 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 disulfide (disulfide).

Compared structures

• 6X5T · Human Alpha-1,6-fucosyltransferase (FUT8) bound to GDP and A3-Asn · the same entry in another collection · chain C against C, 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 6X5T · PDBe 6X5T · UniProt Q9BYC5