4GYW
Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide
Functional Information from GO Data
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by CDK1 => ECO:0000269|PubMed:7592773 |
Chain | Residue | Details |
B | THR18 | |
D | THR18 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23103939, ECO:0007744|PDB:4GYW |
Chain | Residue | Details |
A | GLN839 | |
C | HIS901 | |
C | HIS920 | |
C | ASP925 | |
A | LYS842 | |
A | ALA896 | |
A | HIS901 | |
A | HIS920 | |
A | ASP925 | |
C | GLN839 | |
C | LYS842 | |
C | ALA896 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by AMPK => ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:37541260 |
Chain | Residue | Details |
A | THR444 | |
C | THR444 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P56558 |
Chain | Residue | Details |
A | TYR979 | |
C | TYR979 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GlcNAc) serine; by autocatalysis => ECO:0000269|PubMed:27713473 |
Chain | Residue | Details |
A | SER389 | |
C | SER389 |