4N3A
Crystal Structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (1-26)E10A
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UDP A 1201 |
| Chain | Residue |
| A | PRO559 |
| A | HIS920 |
| A | THR921 |
| A | THR922 |
| A | ASP925 |
| A | HOH1309 |
| A | HOH1324 |
| A | HOH1325 |
| A | HOH1338 |
| A | GLN839 |
| A | LYS842 |
| A | LEU866 |
| A | VAL895 |
| A | ALA896 |
| A | LYS898 |
| A | HIS901 |
| A | ARG904 |
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 |
