Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| A | 0006012 | biological_process | galactose metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0020015 | cellular_component | glycosome |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| B | 0006012 | biological_process | galactose metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0020015 | cellular_component | glycosome |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| C | 0006012 | biological_process | galactose metabolic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0020015 | cellular_component | glycosome |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| D | 0006012 | biological_process | galactose metabolic process |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0020015 | cellular_component | glycosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAD A1382 |
| Chain | Residue |
| A | GLY7 |
| A | THR37 |
| A | GLY74 |
| A | ASP75 |
| A | VAL76 |
| A | MET98 |
| A | CYS99 |
| A | ALA100 |
| A | LEU102 |
| A | ASN117 |
| A | SER140 |
| A | GLY10 |
| A | SER141 |
| A | SER142 |
| A | TYR173 |
| A | LYS177 |
| A | TYR200 |
| A | PHE201 |
| A | ALA203 |
| A | HOH2021 |
| A | HOH2108 |
| A | HOH2192 |
| A | TYR11 |
| A | HOH2207 |
| A | HOH2325 |
| A | HOH2326 |
| A | HOH2327 |
| A | HOH2328 |
| A | HOH2329 |
| A | HOH2330 |
| A | ILE12 |
| A | ASP32 |
| A | SER33 |
| A | LEU34 |
| A | VAL35 |
| A | GLY36 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE UDP A1383 |
| Chain | Residue |
| A | ASN202 |
| A | THR220 |
| A | HIS221 |
| A | LEU222 |
| A | ILE225 |
| A | MET252 |
| A | PRO253 |
| A | ILE254 |
| A | PHE255 |
| A | CYS266 |
| A | ARG268 |
| A | ARG335 |
| A | ASP338 |
| A | HOH2325 |
| A | HOH2331 |
| A | HOH2332 |
| A | HOH2333 |
| A | HOH2334 |
| A | HOH2335 |
| A | HOH2336 |
| A | HOH2337 |
| site_id | AC3 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE NAD B1382 |
| Chain | Residue |
| B | GLY7 |
| B | GLY10 |
| B | TYR11 |
| B | ILE12 |
| B | ASP32 |
| B | SER33 |
| B | LEU34 |
| B | VAL35 |
| B | GLY36 |
| B | THR37 |
| B | GLY74 |
| B | ASP75 |
| B | VAL76 |
| B | MET98 |
| B | CYS99 |
| B | ALA100 |
| B | LEU102 |
| B | ASN117 |
| B | SER140 |
| B | SER141 |
| B | SER142 |
| B | TYR173 |
| B | LYS177 |
| B | TYR200 |
| B | PHE201 |
| B | ALA203 |
| B | HOH2009 |
| B | HOH2187 |
| B | HOH2206 |
| B | HOH2216 |
| B | HOH2339 |
| B | HOH2340 |
| B | HOH2341 |
| B | HOH2342 |
| B | HOH2343 |
| B | HOH2344 |
| B | HOH2349 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE UDP B1383 |
| Chain | Residue |
| B | MET252 |
| B | PRO253 |
| B | ILE254 |
| B | PHE255 |
| B | CYS266 |
| B | ARG268 |
| B | ARG335 |
| B | ASP338 |
| B | HOH2204 |
| B | HOH2223 |
| B | HOH2224 |
| B | HOH2345 |
| B | HOH2346 |
| B | HOH2347 |
| B | HOH2348 |
| B | HOH2349 |
| B | HOH2350 |
| B | ASN202 |
| B | THR220 |
| B | HIS221 |
| B | LEU222 |
| B | ILE225 |
| site_id | AC5 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAD C1382 |
| Chain | Residue |
| C | GLY7 |
| C | GLY10 |
| C | TYR11 |
| C | ILE12 |
| C | ASP32 |
| C | SER33 |
| C | LEU34 |
| C | VAL35 |
| C | GLY36 |
| C | THR37 |
| C | GLY74 |
| C | ASP75 |
| C | VAL76 |
| C | MET98 |
| C | CYS99 |
| C | ALA100 |
| C | LEU102 |
| C | ASN117 |
| C | SER140 |
| C | SER141 |
| C | SER142 |
| C | TYR173 |
| C | LYS177 |
| C | TYR200 |
| C | PHE201 |
| C | ALA203 |
| C | HOH2010 |
| C | HOH2193 |
| C | HOH2332 |
| C | HOH2333 |
| C | HOH2334 |
| C | HOH2335 |
| C | HOH2336 |
| C | HOH2337 |
| C | HOH2338 |
| C | HOH2342 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE UDP C1383 |
| Chain | Residue |
| C | ASN202 |
| C | THR220 |
| C | HIS221 |
| C | LEU222 |
| C | ILE225 |
| C | MET252 |
| C | PRO253 |
| C | ILE254 |
| C | PHE255 |
| C | CYS266 |
| C | ARG268 |
| C | ARG335 |
| C | ASP338 |
| C | HOH2192 |
| C | HOH2239 |
| C | HOH2339 |
| C | HOH2340 |
| C | HOH2341 |
| C | HOH2342 |
| C | HOH2344 |
| C | HOH2345 |
| site_id | AC7 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAD D1382 |
| Chain | Residue |
| D | GLY7 |
| D | GLY10 |
| D | TYR11 |
| D | ILE12 |
| D | ASP32 |
| D | SER33 |
| D | LEU34 |
| D | VAL35 |
| D | GLY36 |
| D | THR37 |
| D | GLY74 |
| D | ASP75 |
| D | VAL76 |
| D | MET98 |
| D | CYS99 |
| D | ALA100 |
| D | LEU102 |
| D | ASN117 |
| D | SER140 |
| D | SER141 |
| D | SER142 |
| D | TYR173 |
| D | LYS177 |
| D | TYR200 |
| D | PHE201 |
| D | ALA203 |
| D | HOH2030 |
| D | HOH2125 |
| D | HOH2160 |
| D | HOH2242 |
| D | HOH2243 |
| D | HOH2244 |
| D | HOH2245 |
| D | HOH2246 |
| D | HOH2247 |
| D | HOH2248 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UDP D1383 |
| Chain | Residue |
| D | ASN202 |
| D | THR220 |
| D | HIS221 |
| D | LEU222 |
| D | ILE225 |
| D | MET252 |
| D | PRO253 |
| D | ILE254 |
| D | PHE255 |
| D | CYS266 |
| D | ARG268 |
| D | ARG335 |
| D | ASP338 |
| D | HOH2149 |
| D | HOH2249 |
| D | HOH2250 |
| D | HOH2251 |
| D | HOH2252 |
| D | HOH2253 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER142 | |
| A | LYS177 | |
| A | TYR173 | |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS177 | |
| B | TYR173 | |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS177 | |
| C | TYR173 | |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS177 | |
| D | TYR173 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER142 | |
| B | LYS177 | |
| B | TYR173 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | SER142 | |
| C | LYS177 | |
| C | TYR173 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | SER142 | |
| D | LYS177 | |
| D | TYR173 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASN118 | |
| A | SER142 | |
| A | LYS177 | |
| A | TYR173 | |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | ASN118 | |
| B | SER142 | |
| B | LYS177 | |
| B | TYR173 | |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ASN118 | |
| C | SER142 | |
| C | LYS177 | |
| C | TYR173 | |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | ASN118 | |
| D | SER142 | |
| D | LYS177 | |
| D | TYR173 | |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS177 | |
| A | TYR173 | |
