1TCU
Crystal Structure of the Purine Nucleoside Phosphorylase from Schistosoma mansoni in complex with phosphate and acetate
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 | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0009116 | biological_process | nucleoside metabolic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0047975 | molecular_function | guanosine phosphorylase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0009116 | biological_process | nucleoside metabolic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0047975 | molecular_function | guanosine phosphorylase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| C | 0009116 | biological_process | nucleoside metabolic process |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0047975 | molecular_function | guanosine phosphorylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACT A 700 |
| Chain | Residue |
| A | ALA119 |
| A | HOH799 |
| A | GLY120 |
| A | TYR202 |
| A | GLU203 |
| A | VAL219 |
| A | GLY220 |
| A | MET221 |
| A | ASN245 |
| A | HOH726 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT B 701 |
| Chain | Residue |
| B | ALA119 |
| B | GLY120 |
| B | TYR202 |
| B | GLU203 |
| B | VAL219 |
| B | GLY220 |
| B | MET221 |
| B | ASN245 |
| B | HOH794 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACT C 702 |
| Chain | Residue |
| C | ALA119 |
| C | GLY120 |
| C | TYR202 |
| C | GLU203 |
| C | VAL219 |
| C | GLY220 |
| C | MET221 |
| C | ASN245 |
| C | HOH716 |
| C | HOH756 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 706 |
| Chain | Residue |
| A | GLY34 |
| A | SER35 |
| A | ARG86 |
| A | HIS88 |
| A | ASN117 |
| A | ALA118 |
| A | SER222 |
| A | HOH806 |
| A | HOH830 |
| A | HOH852 |
| A | HOH880 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 707 |
| Chain | Residue |
| B | GLY34 |
| B | ARG86 |
| B | HIS88 |
| B | ASN117 |
| B | ALA118 |
| B | SER222 |
| B | HOH718 |
| B | HOH798 |
| B | HOH816 |
| B | HOH834 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 C 708 |
| Chain | Residue |
| C | GLY34 |
| C | SER35 |
| C | ARG86 |
| C | HIS88 |
| C | ASN117 |
| C | ALA118 |
| C | SER222 |
| C | HOH891 |
| C | HOH897 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS A 703 |
| Chain | Residue |
| A | ALA99 |
| A | ARG103 |
| A | ILE148 |
| A | VAL150 |
| A | HOH813 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS B 704 |
| Chain | Residue |
| B | ALA99 |
| B | ARG103 |
| B | ILE148 |
| B | VAL150 |
| B | HOH833 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DMS C 705 |
| Chain | Residue |
| C | ASN95 |
| C | ALA99 |
| C | ARG103 |
| C | ILE148 |
| C | VAL150 |
| C | GLN154 |
| C | HOH732 |
| C | HOH768 |
