The human O-glcnac transferase in complex with a thiol-linked bisubstrate inhibitor

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 13% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · chains E
• 94T · [[(2~{R},3~{S},4~{R},5~{R})-5-[2,4-bis(oxidanylidene) pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] propyl hydrogen phosphate · ligand · chains A, E
• K · Potassium ion · metal · chains A
• NH2 · Amino group · ion · chains A, E

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–E · 450 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

• 5NPR · The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor · the same entry in another collection · chain A against A, 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 0.97

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 5NPR · PDBe 5NPR · UniProt O15294