1EK6
STRUCTURE OF HUMAN UDP-GALACTOSE 4-EPIMERASE COMPLEXED WITH NADH AND UDP-GLUCOSE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
| A | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006012 | biological_process | galactose metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019388 | biological_process | galactose catabolic process |
| A | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0003974 | molecular_function | UDP-N-acetylglucosamine 4-epimerase activity |
| B | 0003978 | molecular_function | UDP-glucose 4-epimerase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006012 | biological_process | galactose metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019388 | biological_process | galactose catabolic process |
| B | 0033499 | biological_process | galactose catabolic process via UDP-galactose |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 960 |
| Chain | Residue |
| A | HOH1546 |
| A | HOH1635 |
| A | HOH1803 |
| B | HOH1286 |
| B | HOH1795 |
| B | HOH1798 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 961 |
| Chain | Residue |
| A | HOH1943 |
| A | HOH1944 |
| A | HOH1945 |
| A | HOH1143 |
| A | HOH1484 |
| A | HOH1942 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAI A 400 |
| Chain | Residue |
| A | GLY9 |
| A | GLY12 |
| A | TYR13 |
| A | ILE14 |
| A | ASP33 |
| A | ASN34 |
| A | HIS36 |
| A | ASN37 |
| A | ALA38 |
| A | MET65 |
| A | ASP66 |
| A | ILE67 |
| A | PHE88 |
| A | ALA89 |
| A | GLY90 |
| A | LYS92 |
| A | SER130 |
| A | SER131 |
| A | SER132 |
| A | TYR157 |
| A | LYS161 |
| A | TYR185 |
| A | PRO188 |
| A | UPG401 |
| A | HOH1102 |
| A | HOH1108 |
| A | HOH1110 |
| A | HOH1113 |
| A | HOH1268 |
| A | HOH1272 |
| A | HOH1405 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE UPG A 401 |
| Chain | Residue |
| A | SER132 |
| A | THR134 |
| A | TYR157 |
| A | PHE186 |
| A | ASN187 |
| A | ASN206 |
| A | ASN207 |
| A | LEU208 |
| A | ASN224 |
| A | VAL225 |
| A | PHE226 |
| A | GLY237 |
| A | ARG239 |
| A | TYR241 |
| A | VAL277 |
| A | ARG300 |
| A | ASP303 |
| A | NAI400 |
| A | HOH1114 |
| A | HOH1127 |
| A | HOH1195 |
| A | HOH1199 |
| A | HOH1485 |
| A | HOH1496 |
| A | HOH1511 |
| A | HOH1532 |
| A | HOH1666 |
| A | HOH1791 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAI B 402 |
| Chain | Residue |
| B | HOH1198 |
| B | HOH1242 |
| B | HOH1266 |
| B | HOH1282 |
| B | HOH1393 |
| B | GLY9 |
| B | GLY12 |
| B | TYR13 |
| B | ILE14 |
| B | ASP33 |
| B | ASN34 |
| B | PHE35 |
| B | HIS36 |
| B | ASN37 |
| B | ALA38 |
| B | MET65 |
| B | ASP66 |
| B | ILE67 |
| B | PHE88 |
| B | ALA89 |
| B | GLY90 |
| B | LYS92 |
| B | SER130 |
| B | SER131 |
| B | TYR157 |
| B | LYS161 |
| B | TYR185 |
| B | PHE186 |
| B | PRO188 |
| B | UPG403 |
| B | HOH1128 |
| B | HOH1158 |
| B | HOH1177 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE UPG B 403 |
| Chain | Residue |
| B | LYS92 |
| B | SER132 |
| B | THR134 |
| B | TYR157 |
| B | TYR185 |
| B | PHE186 |
| B | ASN187 |
| B | ASN206 |
| B | ASN207 |
| B | LEU208 |
| B | ASN224 |
| B | VAL225 |
| B | PHE226 |
| B | GLY237 |
| B | ARG239 |
| B | TYR241 |
| B | VAL277 |
| B | ARG300 |
| B | ASP303 |
| B | NAI402 |
| B | HOH1136 |
| B | HOH1261 |
| B | HOH1307 |
| B | HOH1345 |
| B | HOH1351 |
| B | HOH1354 |
| B | HOH1365 |
| B | HOH1371 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TMA A 950 |
| Chain | Residue |
| A | LYS257 |
| A | GLU260 |
| A | VAL296 |
| A | GLU317 |
| A | HOH1274 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TMA B 951 |
| Chain | Residue |
| B | HIS122 |
| B | PRO139 |
| B | GLN140 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TMA A 952 |
| Chain | Residue |
| A | MET1 |
| A | ALA25 |
| A | GLY26 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193, ECO:0000303|PubMed:15175331 |
| Chain | Residue | Details |
| A | TYR157 | |
| B | TYR157 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 |
| Chain | Residue | Details |
| A | GLY12 | |
| B | GLY12 | |
| B | ASP33 | |
| B | ASP66 | |
| B | PHE88 | |
| B | LYS92 | |
| B | LYS161 | |
| B | ASN206 | |
| B | ASN224 | |
| B | ARG239 | |
| A | ASP33 | |
| A | ASP66 | |
| A | PHE88 | |
| A | LYS92 | |
| A | LYS161 | |
| A | ASN206 | |
| A | ASN224 | |
| A | ARG239 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10801319, ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193, ECO:0000303|PubMed:15175331 |
| Chain | Residue | Details |
| A | SER132 | |
| B | SER132 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10801319 |
| Chain | Residue | Details |
| A | TYR185 | |
| B | TYR185 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11279032, ECO:0000269|PubMed:11279193 |
| Chain | Residue | Details |
| A | ARG300 | |
| B | ARG300 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS161 | |
| A | TYR157 | |
| A | SER132 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS161 | |
| B | TYR157 | |
| B | SER132 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS161 | |
| A | SER130 | |
| A | TYR157 | |
| A | ASN108 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS161 | |
| B | SER130 | |
| B | TYR157 | |
| B | ASN108 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR141 | |
| A | LYS161 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR141 | |
| B | LYS161 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS161 | |
| A | TYR157 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS161 | |
| B | TYR157 |
