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 | 28 |
Details | BINDING SITE FOR RESIDUE GDU A 404 |
Chain | Residue |
A | PRO187 |
A | LYS279 |
A | GLY292 |
A | TRP314 |
A | GLY315 |
A | GLU317 |
A | ASP318 |
A | HIS344 |
A | HIS347 |
A | ASP350 |
A | ASN353 |
A | PHE188 |
A | MN403 |
A | HOH1007 |
A | HOH1017 |
A | HOH1041 |
A | HOH1057 |
A | HOH1065 |
A | HOH1074 |
A | HOH1098 |
A | HOH1159 |
A | ARG189 |
A | ARG191 |
A | PHE226 |
A | ARG228 |
A | ASP252 |
A | VAL253 |
A | ASP254 |
site_id | AC2 |
Number of Residues | 28 |
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 | TYR289 |
B | GLY292 |
B | TRP314 |
B | GLY315 |
B | GLU317 |
B | HIS344 |
B | HIS347 |
B | ASP350 |
B | ASN353 |
B | MN805 |
B | HOH1004 |
B | HOH1005 |
B | HOH1064 |
B | HOH1089 |
B | HOH1105 |
B | HOH1149 |
B | HOH1179 |
B | HOH1269 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 403 |
Chain | Residue |
A | ASP254 |
A | HIS344 |
A | HIS347 |
A | GDU404 |
A | HOH1007 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 805 |
Chain | Residue |
B | ASP254 |
B | HIS344 |
B | HIS347 |
B | GDU806 |
B | HOH1004 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 900 |
Chain | Residue |
A | ARG265 |
A | PHE267 |
A | SER268 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 901 |
Chain | Residue |
A | HIS347 |
A | SER348 |
A | HOH1019 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 902 |
Chain | Residue |
A | ARG346 |
A | HOH1334 |
A | HOH1352 |
A | HOH1360 |
B | THR263 |
B | ARG265 |
B | PHE267 |
B | HOH1085 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 904 |
Chain | Residue |
B | ARG265 |
B | PHE267 |
B | SER268 |
B | HOH1373 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 905 |
Chain | Residue |
B | HIS347 |
B | SER348 |
B | HOH1054 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 906 |
Chain | Residue |
B | SER348 |
B | ARG349 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 907 |
Chain | Residue |
B | LYS166 |
B | LEU167 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MES A 860 |
Chain | Residue |
A | LYS230 |
A | THR379 |
A | ILE398 |
A | GLY399 |
A | THR400 |
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 |