Human O-glcnac transferase in complex with a bisubstrate inhibitor, GOBLIN1

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 12% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · 4 copies · chains E, F, G, H
• UDP · Uridine-5'-diphosphate · ligand · 4 copies · chains A, E, B, F, C, G, D, H
• SO4 · Sulfate ion · ion · 31 copies · chains A, B, C, G, D, E, F, H
• NH2 · Amino group · ion · 4 copies · chains A, E, B, F, C, G, D, H

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

7 interfaces between chains.

• B–C · 995 Ų buried · 8 hydrogen bonds · protein-protein
• A–D · 973 Ų buried · 8 hydrogen bonds · protein-protein
• A–B · 544 Ų buried · 3 hydrogen bonds · protein-protein
• D–H · 495 Ų buried · 1 hydrogen bond · protein-protein
• B–F · 494 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 8 covalent, 4 modified (covalent ligand, nonstandard).

Compared structures

• 4CDR · Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1 · the same entry in another collection · chain H against H, TM-score 1.00
• O15294 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- peptide… · a predicted model of the same protein · chain A against A, TM-score 0.96

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 O15294
• Elsewhere: RCSB PDB 4CDR · PDBe 4CDR · UniProt O15294