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 | 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 | 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 | 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 | 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 | CSA1 |
Number of Residues | 3 |
Details | a catalytic site defined by CSA, PubMed 9698549 |
Chain | Residue | Details |
A | HIS85 | |
A | ARG171 | |
A | LYS190 |
site_id | CSA2 |
Number of Residues | 3 |
Details | a catalytic site defined by CSA, PubMed 9698549 |
Chain | Residue | Details |
B | HIS85 | |
B | ARG171 | |
B | LYS190 |
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 |