1HZJ
HUMAN UDP-GALACTOSE 4-EPIMERASE: ACCOMMODATION OF UDP-N-ACETYLGLUCOSAMINE WITHIN THE ACTIVE SITE
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, Leloir pathway |
| 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, Leloir pathway |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 950 |
| Chain | Residue |
| A | LYS100 |
| A | PRO101 |
| A | LEU102 |
| B | HOH1278 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 951 |
| Chain | Residue |
| A | HOH1349 |
| B | LYS100 |
| B | PRO101 |
| B | LEU102 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 952 |
| Chain | Residue |
| A | TYR80 |
| A | SER81 |
| A | LYS4 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 960 |
| Chain | Residue |
| A | HOH1287 |
| A | HOH1292 |
| A | HOH1313 |
| A | HOH1409 |
| A | HOH1749 |
| A | HOH1941 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD A 400 |
| Chain | Residue |
| A | GLY9 |
| A | GLY12 |
| A | TYR13 |
| A | ILE14 |
| A | ASP33 |
| A | ASN34 |
| A | PHE35 |
| A | HIS36 |
| A | ASN37 |
| 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 | UD1401 |
| A | HOH1101 |
| A | HOH1104 |
| A | HOH1113 |
| A | HOH1129 |
| A | HOH1141 |
| A | HOH1161 |
| A | HOH1203 |
| A | HOH1335 |
| A | HOH1482 |
| A | HOH1518 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE UD1 A 401 |
| Chain | Residue |
| A | VAL94 |
| A | SER132 |
| A | THR134 |
| A | ASN187 |
| A | ASN206 |
| A | ASN207 |
| A | LEU208 |
| A | LEU223 |
| A | ASN224 |
| A | VAL225 |
| A | PHE226 |
| A | GLY237 |
| A | ARG239 |
| A | TYR241 |
| A | VAL277 |
| A | ARG300 |
| A | ASP303 |
| A | NAD400 |
| A | HOH1189 |
| A | HOH1206 |
| A | HOH1208 |
| A | HOH1254 |
| A | HOH1308 |
| A | HOH1518 |
| A | HOH1519 |
| A | HOH1534 |
| A | HOH1598 |
| A | HOH1775 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD B 900 |
| Chain | Residue |
| B | PHE186 |
| B | PRO188 |
| B | UD1901 |
| B | HOH1100 |
| B | HOH1105 |
| B | HOH1122 |
| B | HOH1194 |
| B | HOH1299 |
| B | HOH1643 |
| B | GLY9 |
| B | GLY12 |
| B | TYR13 |
| B | ILE14 |
| B | ASP33 |
| B | ASN34 |
| B | HIS36 |
| B | ASN37 |
| B | MET65 |
| B | ASP66 |
| B | ILE67 |
| B | PHE88 |
| B | ALA89 |
| B | GLY90 |
| B | LYS92 |
| B | SER130 |
| B | SER131 |
| B | TYR157 |
| B | LYS161 |
| B | TYR185 |
| site_id | AC8 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE UD1 B 901 |
| Chain | Residue |
| B | LYS92 |
| B | VAL94 |
| B | SER132 |
| 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 | ARG300 |
| B | ASP303 |
| B | NAD900 |
| B | HOH1121 |
| B | HOH1135 |
| B | HOH1158 |
| B | HOH1200 |
| B | HOH1204 |
| B | HOH1228 |
| B | HOH1255 |
| B | HOH1698 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10801319","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11279032","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11279193","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15175331","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10801319","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11279032","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11279193","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10801319","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11279032","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11279193","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15175331","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11279032","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11279193","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10801319","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
