1AZY
STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006196 | biological_process | AMP catabolic process |
| A | 0006206 | biological_process | pyrimidine nucleobase metabolic process |
| A | 0006213 | biological_process | pyrimidine nucleoside metabolic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0009032 | molecular_function | thymidine phosphorylase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016154 | molecular_function | pyrimidine-nucleoside phosphorylase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0046104 | biological_process | thymidine metabolic process |
| B | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006196 | biological_process | AMP catabolic process |
| B | 0006206 | biological_process | pyrimidine nucleobase metabolic process |
| B | 0006213 | biological_process | pyrimidine nucleoside metabolic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0009032 | molecular_function | thymidine phosphorylase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016154 | molecular_function | pyrimidine-nucleoside phosphorylase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0046104 | biological_process | thymidine metabolic process |
Functional Information from PDB Data
| site_id | P4A |
| Number of Residues | 6 |
| Details | PHOSPHATE BINDING SITE. |
| Chain | Residue |
| A | LYS84 |
| A | HIS85 |
| A | SER86 |
| A | SER95 |
| A | SER113 |
| A | THR123 |
| site_id | P4B |
| Number of Residues | 6 |
| Details | PHOSPHATE BINDING SITE. |
| Chain | Residue |
| B | LYS84 |
| B | HIS85 |
| B | SER86 |
| B | SER95 |
| B | SER113 |
| B | THR123 |
| site_id | TYA |
| Number of Residues | 3 |
| Details | THYMIDINE BINDING SITE. |
| Chain | Residue |
| A | ARG171 |
| A | SER186 |
| A | LYS190 |
| site_id | TYB |
| Number of Residues | 3 |
| Details | THYMIDINE BINDING SITE. |
| Chain | Residue |
| B | ARG171 |
| B | SER186 |
| B | LYS190 |
Functional Information from PROSITE/UniProt
| site_id | PS00647 |
| Number of Residues | 16 |
| Details | THYMID_PHOSPHORYLASE Thymidine and pyrimidine-nucleoside phosphorylases signature. SGRGLghTGGTlDkLE |
| Chain | Residue | Details |
| A | SER113-GLU128 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 413 |
| Chain | Residue | Details |
| A | ASP83 | proton shuttle (general acid/base) |
| A | LYS84 | activator, electrostatic stabiliser |
| A | HIS85 | electrostatic stabiliser |
| A | SER86 | electrostatic stabiliser |
| A | THR123 | electrostatic stabiliser |
| A | ARG171 | electrostatic stabiliser |
| A | SER186 | electrostatic stabiliser |
| A | LYS190 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | LYS191 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 413 |
| Chain | Residue | Details |
| B | ASP83 | proton shuttle (general acid/base) |
| B | LYS84 | activator, electrostatic stabiliser |
| B | HIS85 | electrostatic stabiliser |
| B | SER86 | electrostatic stabiliser |
| B | THR123 | electrostatic stabiliser |
| B | ARG171 | electrostatic stabiliser |
| B | SER186 | electrostatic stabiliser |
| B | LYS190 | electrostatic stabiliser, proton shuttle (general acid/base) |
| B | LYS191 | electrostatic stabiliser |
