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 |
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 | 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 | 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 |