6BW6
Human GPT (DPAGT1) H129 variant 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 | 0006047 | biological_process | UDP-N-acetylglucosamine metabolic process |
| 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 | 0019348 | biological_process | dolichol metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003975 | molecular_function | UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity |
| B | 0003976 | molecular_function | UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006047 | biological_process | UDP-N-acetylglucosamine metabolic process |
| B | 0006486 | biological_process | protein glycosylation |
| B | 0006487 | biological_process | protein N-linked glycosylation |
| B | 0006488 | biological_process | dolichol-linked oligosaccharide biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| B | 0019348 | biological_process | dolichol metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003975 | molecular_function | UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity |
| C | 0003976 | molecular_function | UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005789 | cellular_component | endoplasmic reticulum membrane |
| C | 0006047 | biological_process | UDP-N-acetylglucosamine metabolic process |
| C | 0006486 | biological_process | protein glycosylation |
| C | 0006487 | biological_process | protein N-linked glycosylation |
| C | 0006488 | biological_process | dolichol-linked oligosaccharide biosynthetic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| C | 0019348 | biological_process | dolichol metabolic process |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003975 | molecular_function | UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity |
| D | 0003976 | molecular_function | UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| D | 0006047 | biological_process | UDP-N-acetylglucosamine metabolic process |
| D | 0006486 | biological_process | protein glycosylation |
| D | 0006487 | biological_process | protein N-linked glycosylation |
| D | 0006488 | biological_process | dolichol-linked oligosaccharide biosynthetic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0016780 | molecular_function | phosphotransferase activity, for other substituted phosphate groups |
| D | 0019348 | biological_process | dolichol metabolic process |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue TUM A 501 |
| Chain | Residue |
| A | GLN44 |
| A | PHE249 |
| A | ASP252 |
| A | ARG301 |
| A | ARG303 |
| A | ILE304 |
| A | LEU46 |
| A | TRP122 |
| A | ASN182 |
| A | ASN185 |
| A | ILE186 |
| A | ALA188 |
| A | GLY189 |
| A | ASN191 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue PGW A 502 |
| Chain | Residue |
| A | ALA31 |
| A | PHE32 |
| A | HIS35 |
| A | ILE68 |
| B | CYS107 |
| B | PHE110 |
| B | LEU111 |
| B | ALA114 |
| B | HIS124 |
| B | LEU128 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue PGW B 501 |
| Chain | Residue |
| A | CYS107 |
| A | PHE110 |
| A | ALA114 |
| A | LEU118 |
| A | HIS124 |
| B | LEU28 |
| B | ALA31 |
| B | PHE32 |
| B | HIS35 |
| B | ILE68 |
| B | PHE71 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue TUM B 502 |
| Chain | Residue |
| B | GLN44 |
| B | ASP45 |
| B | LEU46 |
| B | TRP122 |
| B | LYS125 |
| B | ASN185 |
| B | ILE186 |
| B | ALA188 |
| B | GLY189 |
| B | ILE190 |
| B | ASN191 |
| B | PHE249 |
| B | ASP252 |
| B | LEU293 |
| B | HIS302 |
| B | ARG303 |
| B | ILE304 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue TUM C 501 |
| Chain | Residue |
| C | GLN44 |
| C | ASP45 |
| C | LEU46 |
| C | TRP122 |
| C | ASN185 |
| C | ILE186 |
| C | ALA188 |
| C | GLY189 |
| C | ILE190 |
| C | ASN191 |
| C | PHE249 |
| C | ASP252 |
| C | LEU293 |
| C | ARG301 |
| C | HIS302 |
| C | ARG303 |
| C | ILE304 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue PGW C 502 |
| Chain | Residue |
| C | CYS107 |
| C | PHE110 |
| C | ALA114 |
| C | LEU118 |
| C | HIS124 |
| D | LEU28 |
| D | ALA31 |
| D | PHE32 |
| D | HIS35 |
| D | ALA64 |
| D | ILE68 |
| D | PHE71 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue PGW C 503 |
| Chain | Residue |
| C | LEU28 |
| C | ALA31 |
| C | PHE32 |
| C | HIS35 |
| C | ILE68 |
| C | PHE71 |
| D | CYS107 |
| D | PHE110 |
| D | LEU111 |
| D | ALA114 |
| D | LEU118 |
| D | HIS124 |
| D | LEU127 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for residue TUM D 501 |
| Chain | Residue |
| D | ASN185 |
| D | ILE186 |
| D | ALA188 |
| D | GLY189 |
| D | ILE190 |
| D | ASN191 |
| D | PHE249 |
| D | ASP252 |
| D | LEU293 |
| D | ARG301 |
| D | HIS302 |
| D | ARG303 |
| D | ILE304 |
| D | GLN44 |
| D | ASP45 |
| D | LEU46 |
| D | TRP122 |
| D | LYS125 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 220 |
| Details | TOPO_DOM: Lumenal => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | MET1-PRO10 | |
| B | GLU214-ARG218 | |
| B | HIS270-PHE271 | |
| B | LEU401-VAL408 | |
| C | MET1-PRO10 | |
| C | LEU79-PRO91 | |
| C | PHE144-GLY166 | |
| C | GLU214-ARG218 | |
| C | HIS270-PHE271 | |
| C | LEU401-VAL408 | |
| D | MET1-PRO10 | |
| A | LEU79-PRO91 | |
| D | LEU79-PRO91 | |
| D | PHE144-GLY166 | |
| D | GLU214-ARG218 | |
| D | HIS270-PHE271 | |
| D | LEU401-VAL408 | |
| A | PHE144-GLY166 | |
| A | GLU214-ARG218 | |
| A | HIS270-PHE271 | |
| A | LEU401-VAL408 | |
| B | MET1-PRO10 | |
| B | LEU79-PRO91 | |
| B | PHE144-GLY166 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 108 |
| Details | TRANSMEM: Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | LEU11-ALA38 | |
| B | LEU11-ALA38 | |
| C | LEU11-ALA38 | |
| D | LEU11-ALA38 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 456 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | ALA39-GLN58 | |
| B | LEU294-HIS375 | |
| C | ALA39-GLN58 | |
| C | ASN119-ARG121 | |
| C | LEU187-GLY192 | |
| C | TRP243-VAL250 | |
| C | LEU294-HIS375 | |
| D | ALA39-GLN58 | |
| D | ASN119-ARG121 | |
| D | LEU187-GLY192 | |
| D | TRP243-VAL250 | |
| A | ASN119-ARG121 | |
| D | LEU294-HIS375 | |
| A | LEU187-GLY192 | |
| A | TRP243-VAL250 | |
| A | LEU294-HIS375 | |
| B | ALA39-GLN58 | |
| B | ASN119-ARG121 | |
| B | LEU187-GLY192 | |
| B | TRP243-VAL250 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 76 |
| Details | TRANSMEM: Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | GLY59-PHE78 | |
| B | GLY59-PHE78 | |
| C | GLY59-PHE78 | |
| D | GLY59-PHE78 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 104 |
| Details | TRANSMEM: Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | HIS92-LEU118 | |
| B | HIS92-LEU118 | |
| C | HIS92-LEU118 | |
| D | HIS92-LEU118 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | TRP122-ASN143 | |
| B | TRP122-ASN143 | |
| C | TRP122-ASN143 | |
| D | TRP122-ASN143 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 76 |
| Details | TRANSMEM: Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | ILE167-ILE186 | |
| B | ILE167-ILE186 | |
| C | ILE167-ILE186 | |
| D | ILE167-ILE186 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | LEU193-LEU213 | |
| B | LEU193-LEU213 | |
| C | LEU193-LEU213 | |
| D | LEU193-LEU213 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 92 |
| Details | TRANSMEM: Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | ASP219-ASN242 | |
| B | ASP219-ASN242 | |
| C | ASP219-ASN242 | |
| D | ASP219-ASN242 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 72 |
| Details | TRANSMEM: Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | GLY251-GLY269 | |
| B | GLY251-GLY269 | |
| C | GLY251-GLY269 | |
| D | GLY251-GLY269 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | SER272-LEU293 | |
| B | SER272-LEU293 | |
| C | SER272-LEU293 | |
| D | SER272-LEU293 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 96 |
| Details | TRANSMEM: Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785 |
| Chain | Residue | Details |
| A | GLU376-GLN400 | |
| B | GLU376-GLN400 | |
| C | GLU376-GLN400 | |
| D | GLU376-GLN400 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30388443 |
| Chain | Residue | Details |
| A | GLN44 | |
| C | GLU56 | |
| C | ASN191 | |
| C | ARG301 | |
| D | GLN44 | |
| D | GLU56 | |
| D | ASN191 | |
| D | ARG301 | |
| A | GLU56 | |
| A | ASN191 | |
| A | ARG301 | |
| B | GLN44 | |
| B | GLU56 | |
| B | ASN191 | |
| B | ARG301 | |
| C | GLN44 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6 |
| Chain | Residue | Details |
| A | LEU46 | |
| A | ARG303 | |
| B | LEU46 | |
| B | ARG303 | |
| C | LEU46 | |
| C | ARG303 | |
| D | LEU46 | |
| D | ARG303 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 |
| Chain | Residue | Details |
| A | ASN119 | |
| A | ASP252 | |
| B | ASN119 | |
| B | ASP252 | |
| C | ASN119 | |
| C | ASP252 | |
| D | ASN119 | |
| D | ASP252 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:30388443 |
| Chain | Residue | Details |
| A | LYS125 | |
| A | VAL178 | |
| B | LYS125 | |
| B | VAL178 | |
| C | LYS125 | |
| C | VAL178 | |
| D | LYS125 | |
| D | VAL178 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW6 |
| Chain | Residue | Details |
| A | ASN185 | |
| B | ASN185 | |
| C | ASN185 | |
| D | ASN185 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN146 | |
| B | ASN146 | |
| C | ASN146 | |
| D | ASN146 |
