Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004576 | molecular_function | oligosaccharyl transferase activity |
A | 0004579 | molecular_function | dolichyl-diphosphooligosaccharide-protein glycotransferase activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0006486 | biological_process | protein glycosylation |
A | 0016020 | cellular_component | membrane |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0018279 | biological_process | protein N-linked glycosylation via asparagine |
A | 0043687 | biological_process | post-translational protein modification |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MN A 801 |
Chain | Residue |
A | ASP56 |
A | ASP154 |
A | GLU319 |
A | HOH902 |
A | HOH903 |
A | HOH910 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MN A 802 |
Chain | Residue |
A | ASP475 |
A | HOH906 |
A | ARG65 |
A | GLN73 |
A | ASP76 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue 9UB A 803 |
Chain | Residue |
A | ASP56 |
A | TYR79 |
A | TYR196 |
A | SER198 |
A | GLN289 |
A | TYR293 |
A | MET368 |
A | ARG375 |
A | PHE376 |
A | TYR379 |
A | TYR468 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue NA A 804 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for Ligand residues PPN B 16 through GLY B 17 bound to THR B 15 |
Chain | Residue |
A | GLU315 |
A | THR316 |
A | ILE317 |
A | MET318 |
A | ASN321 |
A | VAL575 |
B | THR15 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | MET1-SER12 | |
A | TYR125-LEU127 | |
A | LYS177-ASP178 | |
A | HIS218-LYS222 | |
A | LYS257-ASN262 | |
A | LYS351-SER355 | |
A | GLU400-SER407 | |
Chain | Residue | Details |
A | ILE13-TRP37 | |
A | PHE99-GLU124 | |
A | THR128-ASN146 | |
A | THR155-ASN176 | |
A | ILE179-TRP194 | |
A | TYR200-PHE217 | |
A | ILE223-LEU235 | |
A | TRP240-PHE256 | |
A | PHE263-SER280 | |
A | PHE328-LEU350 | |
A | MET356-ALA372 | |
A | THR377-LEU399 | |
A | LEU408-TYR432 | |
Chain | Residue | Details |
A | ALA38-SER98 | |
A | ARG147-ASP154 | |
A | TRP195-SER199 | |
A | SER236-ALA239 | |
A | GLY281-VAL327 | |
A | GLY373-PHE376 | |
A | TYR433-ARG712 | |
Chain | Residue | Details |
A | ASP56 | |
A | ASP154 | |
A | GLU319 | |
Chain | Residue | Details |
A | TYR468 | |
A | TYR196 | |
A | TYR293 | |
A | ARG375 | |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | SITE: Interacts with target acceptor peptide in protein substrate => ECO:0000269|PubMed:21677752 |
Chain | Residue | Details |
A | ASP56 | |
A | GLU319 | |
A | ILE572 | |
Chain | Residue | Details |
A | ARG147 | |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | SITE: Interacts with target acceptor peptide in protein substrate; important for extended sequon recognition => ECO:0000269|PubMed:21677752 |
Chain | Residue | Details |
A | ARG331 | |
Chain | Residue | Details |
A | GLN535 | |
A | PRO556 | |