1EK5
STRUCTURE OF HUMAN UDP-GALACTOSE 4-EPIMERASE IN COMPLEX WITH NAD+
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD A 400 |
| Chain | Residue |
| A | GLY9 |
| A | ALA38 |
| A | MET65 |
| A | ASP66 |
| A | ILE67 |
| A | PHE88 |
| A | GLY90 |
| A | LYS92 |
| A | SER130 |
| A | SER131 |
| A | TYR157 |
| A | GLY12 |
| A | LYS161 |
| A | TYR185 |
| A | PHE186 |
| A | PRO188 |
| A | ASN206 |
| A | HOH605 |
| A | HOH606 |
| A | HOH625 |
| A | HOH631 |
| A | HOH653 |
| A | TYR13 |
| A | HOH655 |
| A | HOH656 |
| A | HOH658 |
| A | HOH660 |
| A | ILE14 |
| A | ASP33 |
| A | ASN34 |
| A | PHE35 |
| A | HIS36 |
| A | ASN37 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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 | 15 |
| 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 | 2 |
| 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 | 5 |
| 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 | 1 |
| 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 | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS161 | |
| A | SER130 | |
| A | TYR157 | |
| A | ASN108 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR141 | |
| A | LYS161 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS161 | |
| A | TYR157 |
