Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE GDU A 404 |
| Chain | Residue |
| A | PRO187 |
| A | LYS279 |
| A | TYR289 |
| A | GLY292 |
| A | TRP314 |
| A | GLY315 |
| A | GLU317 |
| A | MET344 |
| A | HIS347 |
| A | ASP350 |
| A | MN403 |
| A | PHE188 |
| A | HOH1005 |
| A | HOH1011 |
| A | HOH1050 |
| A | HOH1051 |
| A | HOH1069 |
| A | HOH1071 |
| A | HOH1178 |
| A | HOH1238 |
| A | ARG189 |
| A | ARG191 |
| A | PHE226 |
| A | ARG228 |
| A | ASP252 |
| A | VAL253 |
| A | ASP254 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE GDU B 806 |
| Chain | Residue |
| B | PRO187 |
| B | PHE188 |
| B | ARG189 |
| B | ARG191 |
| B | PHE226 |
| B | ARG228 |
| B | ASP252 |
| B | VAL253 |
| B | ASP254 |
| B | LYS279 |
| B | GLY292 |
| B | TRP314 |
| B | GLY315 |
| B | GLU317 |
| B | ASP318 |
| B | MET344 |
| B | HIS347 |
| B | ASP350 |
| B | MN805 |
| B | HOH1036 |
| B | HOH1038 |
| B | HOH1091 |
| B | HOH1100 |
| B | HOH1105 |
| B | HOH1176 |
| B | HOH1231 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 805 |
| Chain | Residue |
| B | ASP254 |
| B | MET344 |
| B | HIS347 |
| B | GDU806 |
| B | HOH1002 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 403 |
| Chain | Residue |
| A | ASP254 |
| A | MET344 |
| A | HIS347 |
| A | GDU404 |
| A | HOH1011 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 901 |
| Chain | Residue |
| B | ALA221 |
| B | GLY222 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 902 |
| Chain | Residue |
| B | ARG265 |
| B | CYS266 |
| B | PHE267 |
| B | SER268 |
| B | HOH1182 |
| B | HOH1450 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 903 |
| Chain | Residue |
| A | ARG265 |
| A | CYS266 |
| A | PHE267 |
| A | SER268 |
| A | HOH1402 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 904 |
| Chain | Residue |
| B | HIS347 |
| B | SER348 |
| B | HOH1298 |
| B | HOH1344 |
| B | HOH1388 |
| B | HOH1424 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 900 |
| Chain | Residue |
| A | ALA221 |
| A | GLY222 |
| A | GLU223 |
| A | LEU383 |
| A | GLU384 |
| A | THR395 |
| A | HOH1217 |
| A | HOH1375 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DIO A 905 |
| Chain | Residue |
| A | LEU155 |
| A | TYR388 |
| A | HOH1052 |
| A | HOH1200 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DIO B 906 |
| Chain | Residue |
| B | LEU155 |
| B | TYR391 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP260 | |
| B | PHE327 | |
| B | ARG387 | |
| B | PRO389 | |
| A | GLN299 | |
| A | ALA326 | |
| A | PHE327 | |
| A | ARG387 | |
| A | PRO389 | |
| B | ASP260 | |
| B | GLN299 | |
| B | ALA326 | |
| Chain | Residue | Details |
| A | PRO163 | |
| B | PRO163 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN190 | |
| B | ASN190 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1fr8 |
| Chain | Residue | Details |
| A | ARG359 | |
| A | GLU317 | |
| A | ASP319 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1fr8 |
| Chain | Residue | Details |
| B | ARG359 | |
| B | GLU317 | |
| B | ASP319 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 570 |
| Chain | Residue | Details |
| A | LEU325 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | PHE327 | metal ligand |
| A | ARG387 | electrostatic stabiliser, hydrogen bond donor |
| A | LEU390 | electrostatic stabiliser, hydrogen bond acceptor |
| A | TYR391 | activator, electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 570 |
| Chain | Residue | Details |
| B | LEU325 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | PHE327 | metal ligand |
| B | ARG387 | electrostatic stabiliser, hydrogen bond donor |
| B | LEU390 | electrostatic stabiliser, hydrogen bond acceptor |
| B | TYR391 | activator, electrostatic stabiliser, proton acceptor, proton donor |
