1I3M
MOLECULAR BASIS FOR SEVERE EPIMERASE-DEFICIENCY GALACTOSEMIA: X-RAY STRUCTURE OF THE HUMAN V94M-SUBSTITUTED UDP-GALACTOSE 4-EPIMERASE
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 | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 990 |
| Chain | Residue |
| B | HIS243 |
| B | ASP246 |
| B | THR271 |
| B | ALA322 |
| B | LEU324 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 991 |
| Chain | Residue |
| B | GLU3 |
| B | TYR80 |
| B | SER81 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 992 |
| Chain | Residue |
| B | SER44 |
| B | LEU45 |
| B | GLY43 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 993 |
| Chain | Residue |
| A | LYS4 |
| A | TYR80 |
| A | SER81 |
| A | HOH1542 |
| A | HOH1902 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 994 |
| Chain | Residue |
| A | SER312 |
| A | GLU316 |
| A | HOH1296 |
| A | HOH1648 |
| B | HOH1468 |
| B | HOH1598 |
| site_id | AC6 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD 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 | HOH1109 |
| A | HOH1121 |
| A | HOH1124 |
| A | HOH1173 |
| A | HOH1310 |
| A | HOH1444 |
| A | HOH1534 |
| A | HOH1823 |
| A | HOH1824 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE UD1 A 401 |
| Chain | Residue |
| A | ALA93 |
| A | TYR157 |
| 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 | GLY302 |
| A | ASP303 |
| A | VAL304 |
| A | HOH1137 |
| A | HOH1231 |
| A | HOH1303 |
| A | HOH1321 |
| A | HOH1461 |
| A | HOH1647 |
| A | HOH1823 |
| A | HOH1826 |
| A | HOH1827 |
| site_id | AC8 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD B 900 |
| Chain | Residue |
| B | SER132 |
| B | TYR157 |
| B | LYS161 |
| B | TYR185 |
| B | PRO188 |
| B | UD1901 |
| B | HOH1103 |
| B | HOH1104 |
| B | HOH1128 |
| B | HOH1148 |
| B | HOH1152 |
| B | HOH1167 |
| B | HOH1479 |
| B | HOH1706 |
| 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 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UD1 B 901 |
| Chain | Residue |
| B | SER132 |
| B | THR134 |
| B | TYR157 |
| 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 | NAD900 |
| B | HOH1123 |
| B | HOH1149 |
| B | HOH1157 |
| B | HOH1416 |
| B | HOH1828 |
| B | HOH1832 |
| B | HOH1901 |
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 |
