1I3K
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, 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 | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 950 |
| Chain | Residue |
| A | SER44 |
| A | LEU45 |
| A | HOH1257 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 951 |
| Chain | Residue |
| B | PRO101 |
| B | LEU102 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 952 |
| Chain | Residue |
| B | HOH1721 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 953 |
| Chain | Residue |
| B | SER81 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 960 |
| Chain | Residue |
| A | HOH1645 |
| A | HOH1646 |
| A | HOH1703 |
| B | HOH1474 |
| A | SER312 |
| A | HOH1323 |
| 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 | PHE35 |
| 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 | HOH1110 |
| A | HOH1118 |
| A | HOH1158 |
| A | HOH1172 |
| A | HOH1311 |
| A | HOH1356 |
| A | HOH1503 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE UPG A 401 |
| Chain | Residue |
| A | SER132 |
| A | ALA133 |
| A | THR134 |
| A | TYR185 |
| 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 | NAD400 |
| A | HOH1119 |
| A | HOH1279 |
| A | HOH1307 |
| A | HOH1437 |
| A | HOH1461 |
| A | HOH2081 |
| A | HOH2082 |
| site_id | AC8 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD B 900 |
| Chain | Residue |
| B | HOH1137 |
| B | HOH1141 |
| B | HOH1495 |
| B | HOH1566 |
| B | HOH1712 |
| 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 | PRO188 |
| B | UPG901 |
| B | HOH1101 |
| B | HOH1113 |
| B | HOH1114 |
| B | HOH1134 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UPG B 901 |
| Chain | Residue |
| B | SER132 |
| B | THR134 |
| 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 | NAD900 |
| B | HOH1103 |
| B | HOH1117 |
| B | HOH1199 |
| B | HOH1345 |
| B | HOH2083 |
| B | HOH2085 |
| B | HOH2086 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 970 |
| Chain | Residue |
| B | PRO139 |
| B | LEU142 |
| B | HOH1321 |
| B | HOH1410 |
| B | HOH1751 |
| B | HOH1752 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 971 |
| Chain | Residue |
| A | GLY26 |
| A | HOH1506 |
| A | HOH1842 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 972 |
| Chain | Residue |
| B | GLY71 |
| B | GLN74 |
| B | ARG75 |
| B | LYS78 |
| B | HOH1433 |
| B | HOH2060 |
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 |
