1PK9
Crystal Structure of E. coli purine nucleoside phosphorylase complexed with 2-fluoroadenosine and sulfate/phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006152 | biological_process | purine nucleoside catabolic process |
| A | 0009116 | biological_process | nucleoside metabolic process |
| A | 0009164 | biological_process | nucleoside catabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0042278 | biological_process | purine nucleoside metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0006152 | biological_process | purine nucleoside catabolic process |
| B | 0009116 | biological_process | nucleoside metabolic process |
| B | 0009164 | biological_process | nucleoside catabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0042278 | biological_process | purine nucleoside metabolic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| C | 0006152 | biological_process | purine nucleoside catabolic process |
| C | 0009116 | biological_process | nucleoside metabolic process |
| C | 0009164 | biological_process | nucleoside catabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0016763 | molecular_function | pentosyltransferase activity |
| C | 0042278 | biological_process | purine nucleoside metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 309 |
| Chain | Residue |
| A | GLY20 |
| A | ARG43 |
| A | ARG87 |
| A | GLY89 |
| A | SER90 |
| A | 2FA306 |
| A | HOH328 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 310 |
| Chain | Residue |
| B | GLY89 |
| B | SER90 |
| B | 2FA307 |
| B | HOH339 |
| C | ARG43 |
| B | GLY20 |
| B | ARG87 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 311 |
| Chain | Residue |
| B | ARG43 |
| C | GLY20 |
| C | ARG24 |
| C | ARG87 |
| C | GLY89 |
| C | SER90 |
| C | 2FA308 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 2FA A 306 |
| Chain | Residue |
| A | HIS4 |
| A | ARG43 |
| A | MET64 |
| A | ARG87 |
| A | SER90 |
| A | CYS91 |
| A | GLY92 |
| A | PHE159 |
| A | VAL178 |
| A | GLU179 |
| A | MET180 |
| A | GLU181 |
| A | ASP204 |
| A | PO4309 |
| A | HOH356 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 2FA B 307 |
| Chain | Residue |
| B | ARG87 |
| B | SER90 |
| B | CYS91 |
| B | GLY92 |
| B | PHE159 |
| B | VAL178 |
| B | GLU179 |
| B | MET180 |
| B | GLU181 |
| B | SER203 |
| B | ASP204 |
| B | PO4310 |
| B | HOH402 |
| C | HIS4 |
| C | ARG43 |
| C | HOH346 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 2FA C 308 |
| Chain | Residue |
| B | HIS4 |
| B | ARG43 |
| B | HOH341 |
| C | MET64 |
| C | ARG87 |
| C | SER90 |
| C | CYS91 |
| C | GLY92 |
| C | PHE159 |
| C | VAL178 |
| C | GLU179 |
| C | MET180 |
| C | GLU181 |
| C | ASP204 |
| C | PO4311 |
| C | HOH326 |
Functional Information from PROSITE/UniProt
| site_id | PS01232 |
| Number of Residues | 16 |
| Details | PNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL |
| Chain | Residue | Details |
| A | GLY61-LEU76 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12937174","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12937174","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a69 |
| Chain | Residue | Details |
| A | ASP204 | |
| A | ARG217 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a69 |
| Chain | Residue | Details |
| B | ASP204 | |
| B | ARG217 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a69 |
| Chain | Residue | Details |
| C | ASP204 | |
| C | ARG217 |
