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 | 29 |
| Details | BINDING SITE FOR RESIDUE GDU A 2 |
| Chain | Residue |
| A | MG1 |
| A | ASP254 |
| A | LYS279 |
| A | TYR289 |
| A | GLY292 |
| A | TRP314 |
| A | GLY315 |
| A | GLU317 |
| A | ASP318 |
| A | HIS344 |
| A | HIS347 |
| A | PRO187 |
| A | ASP350 |
| A | ASN353 |
| A | HOH909 |
| A | HOH913 |
| A | HOH928 |
| A | HOH929 |
| A | HOH967 |
| A | HOH982 |
| A | HOH1012 |
| A | HOH1420 |
| A | PHE188 |
| A | ARG189 |
| A | ARG191 |
| A | PHE226 |
| A | ARG228 |
| A | ASP252 |
| A | VAL253 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE GDU B 404 |
| Chain | Residue |
| B | PRO187 |
| B | PHE188 |
| B | ARG189 |
| B | ARG191 |
| B | PHE226 |
| B | ARG228 |
| B | ASP252 |
| B | VAL253 |
| B | ASP254 |
| B | LYS279 |
| B | TYR289 |
| B | GLY292 |
| B | TRP314 |
| B | GLY315 |
| B | GLU317 |
| B | HIS344 |
| B | HIS347 |
| B | ASP350 |
| B | ASN353 |
| B | MG403 |
| B | HOH905 |
| B | HOH912 |
| B | HOH933 |
| B | HOH952 |
| B | HOH962 |
| B | HOH1084 |
| B | HOH1268 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1 |
| Chain | Residue |
| A | GDU2 |
| A | ASP254 |
| A | HIS344 |
| A | HIS347 |
| A | HOH1420 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 403 |
| Chain | Residue |
| B | ASP254 |
| B | HIS344 |
| B | HIS347 |
| B | GDU404 |
| B | HOH905 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 856 |
| Chain | Residue |
| B | ASN310 |
| B | ARG362 |
| B | HOH953 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 857 |
| Chain | Residue |
| B | LYS181 |
| B | ASP244 |
| B | GLN358 |
| B | HOH1417 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 858 |
| Chain | Residue |
| A | PHE267 |
| A | SER268 |
| A | HOH1195 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 859 |
| Chain | Residue |
| A | HIS347 |
| A | SER348 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 855 |
| Chain | Residue |
| B | HIS347 |
| B | SER348 |
| B | HOH1239 |
| B | HOH1317 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DIO A 860 |
| Chain | Residue |
| A | PRO135 |
| A | GLU136 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DIO A 861 |
| Chain | Residue |
| A | GLY399 |
| A | THR400 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MES B 870 |
| Chain | Residue |
| B | LYS230 |
| B | THR379 |
| B | GLY399 |
| B | THR400 |
| B | HOH1341 |
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 | 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 |
