1JDU
CRYSTAL STRUCTURE OF 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0009116 | biological_process | nucleoside metabolic process |
| A | 0009164 | biological_process | nucleoside catabolic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0017061 | molecular_function | S-methyl-5-thioadenosine phosphorylase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0009116 | biological_process | nucleoside metabolic process |
| B | 0009164 | biological_process | nucleoside catabolic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0017061 | molecular_function | S-methyl-5-thioadenosine phosphorylase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0009116 | biological_process | nucleoside metabolic process |
| C | 0009164 | biological_process | nucleoside catabolic process |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0016763 | molecular_function | pentosyltransferase activity |
| C | 0017061 | molecular_function | S-methyl-5-thioadenosine phosphorylase activity |
Functional Information from PROSITE/UniProt
| site_id | PS01232 |
| Number of Residues | 16 |
| Details | PNP_UDP_1 Purine and other phosphorylases family 1 signature. ThGIGgPSiAIvleEL |
| Chain | Residue | Details |
| A | THR61-LEU76 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11489901 |
| Chain | Residue | Details |
| A | HIS5 | |
| B | HIS5 | |
| C | HIS5 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:11489901, ECO:0007744|PDB:1JDS, ECO:0007744|PDB:1JE0 |
| Chain | Residue | Details |
| A | GLY21 | |
| A | ARG25 | |
| A | ARG86 | |
| B | GLY21 | |
| B | ARG25 | |
| B | ARG86 | |
| C | GLY21 | |
| C | ARG25 | |
| C | ARG86 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11489901, ECO:0007744|PDB:1JE0 |
| Chain | Residue | Details |
| A | ARG43 | |
| B | ARG43 | |
| C | ARG43 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:11489901 |
| Chain | Residue | Details |
| A | GLU163 | |
| A | SER204 | |
| B | GLU163 | |
| B | SER204 | |
| C | GLU163 | |
| C | SER204 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:11489901, ECO:0007744|PDB:1JDT, ECO:0007744|PDB:1JE1 |
| Chain | Residue | Details |
| A | GLU180 | |
| B | GLU180 | |
| C | GLU180 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cg6 |
| Chain | Residue | Details |
| A | LEU207 | |
| A | ASP205 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cg6 |
| Chain | Residue | Details |
| B | LEU207 | |
| B | ASP205 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cg6 |
| Chain | Residue | Details |
| C | LEU207 | |
| C | ASP205 |
