5BNW
The active site of O-GlcNAc transferase imposes constraints on substrate sequence
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 31 |
Details | binding site for residue 12V A 1101 |
Chain | Residue |
A | HIS498 |
A | LYS842 |
A | LEU866 |
A | VAL895 |
A | ALA896 |
A | LYS898 |
A | HIS901 |
A | ARG904 |
A | CYS917 |
A | HIS920 |
A | THR921 |
A | PRO559 |
A | THR922 |
A | ASP925 |
A | HOH1205 |
A | HOH1222 |
A | HOH1227 |
A | HOH1240 |
A | HOH1271 |
D | SER186 |
D | ARG187 |
D | VAL188 |
A | THR560 |
D | THR189 |
D | HOH201 |
A | LEU563 |
A | LEU653 |
A | PRO656 |
A | PHE694 |
A | GLN839 |
A | TYR841 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 33 |
Details | Repeat: {"description":"TPR 9"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 33 |
Details | Repeat: {"description":"TPR 10"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 33 |
Details | Repeat: {"description":"TPR 11"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 33 |
Details | Repeat: {"description":"TPR 12"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 10 |
Details | Repeat: {"description":"TPR 13; truncated"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 19 |
Details | Region: {"description":"Required for phosphatidylinositol 3,4,5-triphosphate binding","evidences":[{"source":"UniProtKB","id":"P56558","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Motif: {"description":"DFP motif","evidences":[{"source":"PubMed","id":"27713473","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 16 |
Details | Motif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21240259","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26678539","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23103939","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4GYW","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by AMPK","evidences":[{"source":"PubMed","id":"24563466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37541260","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P56558","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"O-linked (GlcNAc) serine; by autocatalysis","evidences":[{"source":"PubMed","id":"27713473","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"O-linked (GlcNAc) threonine","evidences":[{"source":"PubMed","id":"26237509","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |