4NSN
Crystal structure of purine nucleoside phosphorylase from Porphyromonas gingivalis ATCC 33277, NYSGRC Target 030972, orthorhombic symmetry
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 | 0016740 | molecular_function | transferase activity |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0009116 | biological_process | nucleoside metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase 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 | 0016740 | molecular_function | transferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0016763 | molecular_function | pentosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADE A 301 |
| Chain | Residue |
| A | ALA129 |
| A | HOH493 |
| A | ALA130 |
| A | GLY131 |
| A | GLU208 |
| A | TYR213 |
| A | GLY225 |
| A | MSE226 |
| A | THR249 |
| A | ASN250 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | GLY45 |
| A | SER46 |
| A | HIS77 |
| A | ARG97 |
| A | HIS99 |
| A | ASN128 |
| A | ALA129 |
| A | SER227 |
| A | HOH431 |
| A | HOH446 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADE B 301 |
| Chain | Residue |
| B | ALA129 |
| B | ALA130 |
| B | GLY131 |
| B | GLU208 |
| B | TYR213 |
| B | ILE224 |
| B | GLY225 |
| B | MSE226 |
| B | THR249 |
| B | ASN250 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 B 302 |
| Chain | Residue |
| B | GLY45 |
| B | SER46 |
| B | HIS77 |
| B | ARG97 |
| B | HIS99 |
| B | ASN128 |
| B | ALA129 |
| B | SER227 |
| B | HOH424 |
| B | HOH462 |
| B | HOH490 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADE C 301 |
| Chain | Residue |
| C | ALA129 |
| C | GLY131 |
| C | GLU208 |
| C | TYR213 |
| C | ILE224 |
| C | GLY225 |
| C | MSE226 |
| C | THR249 |
| C | ASN250 |
| C | VAL266 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 C 302 |
| Chain | Residue |
| C | GLY45 |
| C | SER46 |
| C | HIS77 |
| C | ARG97 |
| C | HIS99 |
| C | ASN128 |
| C | ALA129 |
| C | SER227 |
| C | HOH412 |
| C | HOH430 |
Functional Information from PROSITE/UniProt
| site_id | PS01240 |
| Number of Residues | 42 |
| Details | PNP_MTAP_2 Purine and other phosphorylases family 2 signature. VamqGrfHyYegysMdqvTfpIrVmkllGien.LFvsNAaGGI |
| Chain | Residue | Details |
| A | VAL92-ILE133 |
