5O5E
Crystal structure of human UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) (V264G mutant) in complex with tunicamycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003975 | molecular_function | UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity |
| A | 0003976 | molecular_function | UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006486 | biological_process | protein glycosylation |
| A | 0006487 | biological_process | protein N-linked glycosylation |
| A | 0006488 | biological_process | dolichol-linked oligosaccharide biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue P6L A 501 |
| Chain | Residue |
| A | TRP243 |
| A | ARG377 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | binding site for residue 9LH A 502 |
| Chain | Residue |
| A | ASN185 |
| A | ILE186 |
| A | ALA188 |
| A | GLY189 |
| A | ILE190 |
| A | ASN191 |
| A | PHE249 |
| A | ASP252 |
| A | PHE286 |
| A | ARG301 |
| A | HIS302 |
| A | ARG303 |
| A | ILE304 |
| A | HOH601 |
| A | HOH603 |
| A | HOH604 |
| A | GLN44 |
| A | LEU46 |
| A | GLU56 |
| A | TRP122 |
| A | LYS125 |
| A | LEU126 |
| A | ASN182 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 55 |
| Details | TOPO_DOM: Lumenal => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | MET1-PRO10 | |
| A | LEU79-PRO91 | |
| A | PHE144-GLY166 | |
| A | GLU214-ARG218 | |
| A | HIS270-PHE271 | |
| A | LEU401-VAL408 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 27 |
| Details | TRANSMEM: Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | LEU11-ALA38 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 114 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | ALA39-GLN58 | |
| A | ASN119-ARG121 | |
| A | LEU187-GLY192 | |
| A | TRP243-VAL250 | |
| A | LEU294-HIS375 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | GLY59-PHE78 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 26 |
| Details | TRANSMEM: Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | HIS92-LEU118 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | TRP122-ASN143 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | ILE167-ILE186 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | LEU193-LEU213 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 23 |
| Details | TRANSMEM: Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | ASP219-ASN242 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | GLY251-GLY269 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | SER272-LEU293 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 24 |
| Details | TRANSMEM: Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | GLU376-GLN400 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30388443 |
| Chain | Residue | Details |
| A | GLN44 | |
| A | GLU56 | |
| A | ASN191 | |
| A | ARG301 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6 |
| Chain | Residue | Details |
| A | LEU46 | |
| A | ARG303 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 |
| Chain | Residue | Details |
| A | ASN119 | |
| A | ASP252 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:30388443 |
| Chain | Residue | Details |
| A | LYS125 | |
| A | VAL178 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW6 |
| Chain | Residue | Details |
| A | ASN185 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN146 |
