4GYY
Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc and a peptide substrate
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE 12V A 1501 |
| Chain | Residue |
| A | HIS498 |
| A | TYR841 |
| A | LYS842 |
| A | LEU866 |
| A | VAL895 |
| A | ALA896 |
| A | LYS898 |
| A | HIS901 |
| A | ARG904 |
| A | CYS917 |
| A | HIS920 |
| A | PRO559 |
| A | THR921 |
| A | THR922 |
| A | ASP925 |
| A | HOH1604 |
| A | HOH1627 |
| A | HOH1717 |
| A | HOH1765 |
| A | HOH1786 |
| B | THR18 |
| B | PRO19 |
| A | THR560 |
| B | VAL20 |
| B | SER21 |
| B | HOH201 |
| A | LEU563 |
| A | LEU653 |
| A | GLY654 |
| A | PRO656 |
| A | PHE694 |
| A | GLN839 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1502 |
| Chain | Residue |
| A | GLY365 |
| A | LEU367 |
| A | GLN368 |
| A | HOH1769 |
| A | HOH1977 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 101 |
| Chain | Residue |
| A | LYS634 |
| A | GLY635 |
| A | HOH1798 |
| B | ASN24 |
| B | MET25 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE 12V C 1501 |
| Chain | Residue |
| C | HIS498 |
| C | PRO559 |
| C | THR560 |
| C | LEU563 |
| C | LEU653 |
| C | GLY654 |
| C | PRO656 |
| C | PHE694 |
| C | GLN839 |
| C | TYR841 |
| C | LYS842 |
| C | LEU866 |
| C | VAL895 |
| C | ALA896 |
| C | LYS898 |
| C | HIS901 |
| C | ARG904 |
| C | CYS917 |
| C | HIS920 |
| C | THR921 |
| C | THR922 |
| C | ASP925 |
| C | HOH1602 |
| C | HOH1720 |
| C | HOH1789 |
| C | HOH1835 |
| D | THR18 |
| D | PRO19 |
| D | VAL20 |
| D | SER21 |
| D | HOH201 |
| D | HOH203 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 101 |
| Chain | Residue |
| C | GLY635 |
| C | HOH1861 |
| D | ASN24 |
| D | MET25 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR CHAIN B OF CASEIN KINASE II SUBUNIT ALPHA |
| Chain | Residue |
| B | HOH201 |
| B | HOH202 |
| B | HOH203 |
| B | HOH204 |
| B | HOH208 |
| A | LEU371 |
| A | LYS375 |
| A | LEU395 |
| A | ASP400 |
| A | ASP431 |
| A | SER494 |
| A | HIS496 |
| A | HIS517 |
| A | ASN557 |
| A | HIS558 |
| A | PRO559 |
| A | TYR632 |
| A | THR633 |
| A | LYS634 |
| A | GLN839 |
| A | VAL895 |
| A | 12V1501 |
| A | HOH1620 |
| A | HOH1627 |
| B | TYR13 |
| B | SO4101 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR CHAIN D OF CASEIN KINASE II SUBUNIT ALPHA |
| Chain | Residue |
| C | LEU371 |
| C | LYS375 |
| C | LEU395 |
| C | ASP400 |
| C | ASP431 |
| C | SER494 |
| C | HIS496 |
| C | HIS517 |
| C | ASN557 |
| C | HIS558 |
| C | PRO559 |
| C | TYR632 |
| C | THR633 |
| C | LYS634 |
| C | GLN839 |
| C | VAL895 |
| C | 12V1501 |
| D | TYR13 |
| D | SO4101 |
| D | HOH201 |
| D | HOH202 |
| D | HOH203 |
| D | HOH204 |
| D | HOH205 |
| D | HOH206 |
| D | HOH207 |
| D | HOH208 |
| D | HOH212 |
| D | HOH213 |
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 | 66 |
| Details | Repeat: {"description":"TPR 10"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 11"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 12"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Repeat: {"description":"TPR 13; truncated"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 38 |
| 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 | 4 |
| Details | Motif: {"description":"DFP motif","evidences":[{"source":"PubMed","id":"27713473","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 32 |
| Details | Motif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| 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 | 20 |
| 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 | 2 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P56558","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by CDK1","evidences":[{"source":"PubMed","id":"7592773","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
