4D98
Crystal structure of the hexameric purine nucleoside phosphorylase from Bacillus subtilis in space group H32 at pH 7.5
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 |
| A | 0042278 | biological_process | purine nucleoside metabolic process |
| 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 |
| B | 0042278 | biological_process | purine nucleoside metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | GLY20 |
| A | ARG87 |
| A | GLY89 |
| A | SER90 |
| A | HOH444 |
| A | HOH473 |
| A | HOH475 |
| A | HOH485 |
| B | ARG43 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | PHE154 |
| A | ASN161 |
| A | SER164 |
| A | HOH478 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 301 |
| Chain | Residue |
| A | ARG43 |
| B | GLY20 |
| B | ARG24 |
| B | ARG87 |
| B | GLY89 |
| B | SER90 |
| B | HOH478 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 302 |
| Chain | Residue |
| B | PHE154 |
| B | ASN161 |
| B | SER164 |
| B | HOH485 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 303 |
| Chain | Residue |
| A | GLY192 |
| A | HOH525 |
| A | HOH565 |
| B | ARG95 |
| B | LYS96 |
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 | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01627 |
| Chain | Residue | Details |
| A | ASP203 | |
| B | ASP203 |
| 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 | SER202 | |
| A | ARG24 | |
| A | ARG87 | |
| A | GLU178 | |
| A | SER202 | |
| B | GLY20 | |
| B | ARG24 | |
| B | ARG87 | |
| B | GLU178 |
| 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 | ARG216 | |
| B | ARG216 |
