Mouse POFUT1 in complex with O-glucosylated mouse NOTCH1 EGF12 mutant (D464G) and GDP

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 18% strand (DSSP).

Ligands and binding sites

• GDP · Guanosine-5'-diphosphate · ligand · chains A
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
• BGC · beta-D-glucopyranose · sugar · 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, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 961 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide, 2 glycan (disulfide, N-glycosylation, O-glycosylation).

Compared structures

• 5KY8 · mouse POFUT1 in complex with O-glucosylated mouse Notch1 EGF12 mutant (D464G) and GDP · the same entry in another collection · chain A against A, TM-score 1.00
• Q91ZW2 · AlphaFold monomer V2.0 prediction for GDP-fucose protein O-fucosyltransferase 1 (Q91ZW2) · a predicted model of the same protein · chain A against A, TM-score 0.99
• Q01705 · AlphaFold monomer V2.0 prediction for neurogenic locus notch homolog protein 1 (Q01705) · a predicted model of the same protein · chain B against A, TM-score 0.81

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 Q91ZW2
• Every structure of UniProt Q01705
• Elsewhere: RCSB PDB 5KY8 · PDBe 5KY8 · UniProt Q91ZW2 · UniProt Q01705