4D8X
Crystal structure of the hexameric purine nucleoside phosphorylase from Bacillus subtilis in space group P6322 at pH 4.6
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
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 |
Functional Information from PROSITE/UniProt
site_id | PS01232 |
Number of Residues | 16 |
Details | PNP_UDP_1 Purine and other phosphorylases family 1 signature. GtGMGvPSiSIyvnEL |
Chain | Residue | Details |
A | GLY61-LEU76 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
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 | 2 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P50389","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P50389","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01627","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |