5OLN
X-Ray Structure of the Complex Pyrimidine-nucleoside phosphorylase from Bacillus subtilis at 1.88 A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| A | 0004850 | molecular_function | uridine phosphorylase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006206 | biological_process | pyrimidine nucleobase metabolic process |
| A | 0006213 | biological_process | pyrimidine nucleoside metabolic process |
| A | 0009032 | molecular_function | thymidine phosphorylase activity |
| A | 0016154 | molecular_function | pyrimidine-nucleoside phosphorylase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047847 | molecular_function | deoxyuridine phosphorylase activity |
| B | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| B | 0004850 | molecular_function | uridine phosphorylase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006206 | biological_process | pyrimidine nucleobase metabolic process |
| B | 0006213 | biological_process | pyrimidine nucleoside metabolic process |
| B | 0009032 | molecular_function | thymidine phosphorylase activity |
| B | 0016154 | molecular_function | pyrimidine-nucleoside phosphorylase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047847 | molecular_function | deoxyuridine phosphorylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue IMD A 501 |
| Chain | Residue |
| A | TYR165 |
| A | ARG168 |
| A | SER183 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | ASP35 |
| A | ALA166 |
| A | LEU167 |
| A | HOH731 |
| B | TYR36 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue IMD B 501 |
| Chain | Residue |
| B | ARG168 |
| B | ILE180 |
| B | SER183 |
| B | ILE184 |
| B | HOH794 |
| B | TYR165 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue IMD B 502 |
| Chain | Residue |
| B | HOH661 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | THR92 |
| B | LYS108 |
| B | SER110 |
| B | THR120 |
| B | HOH670 |
Functional Information from PROSITE/UniProt
| site_id | PS00647 |
| Number of Residues | 16 |
| Details | THYMID_PHOSPHORYLASE Thymidine and pyrimidine-nucleoside phosphorylases signature. SGRGLghTGGTiDkLE |
| Chain | Residue | Details |
| A | SER110-GLU125 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P77836 |
| Chain | Residue | Details |
| A | ARG168 | |
| A | LYS187 | |
| A | LEU243 | |
| A | ALA246 | |
| A | GLU255 | |
| B | LYS81 | |
| B | GLY88 | |
| B | THR90 | |
| B | THR92 | |
| B | LYS108 | |
| B | THR120 | |
| B | ARG168 | |
| B | LYS187 | |
| B | LEU243 | |
| B | ALA246 | |
| B | GLU255 | |
| A | LYS81 | |
| A | GLY88 | |
| A | THR90 | |
| A | THR92 | |
| A | LYS108 | |
| A | THR120 |
