7OOY
Purine nucleoside phosphorylase(DeoD-type) from H. pylori with 6-benzylthio-2-chloropurine
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 | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016763 | molecular_function | pentosyltransferase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
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 | 0016757 | molecular_function | glycosyltransferase activity |
B | 0016763 | molecular_function | pentosyltransferase activity |
Functional Information from PROSITE/UniProt
site_id | PS01232 |
Number of Residues | 16 |
Details | PNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiAScTIyvtEL |
Chain | Residue | Details |
A | GLY61-LEU76 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01627 |
Chain | Residue | Details |
A | ASP204 | |
B | ASP204 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P50389 |
Chain | Residue | Details |
A | HIS4 | |
A | ARG43 | |
B | HIS4 | |
B | ARG43 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:P50389 |
Chain | Residue | Details |
A | GLY20 | |
B | SER203 | |
A | ARG24 | |
A | ARG87 | |
A | GLU179 | |
A | SER203 | |
B | GLY20 | |
B | ARG24 | |
B | ARG87 | |
B | GLU179 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627 |
Chain | Residue | Details |
A | ARG217 | |
B | ARG217 |