4YEK
X-ray structure of the thymidine phosphorylase from Salmonella typhimurium in complex with thymidine
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 | 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 | 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 | 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 | 0046104 | biological_process | thymidine metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | ALA175 |
| A | THR176 |
| A | VAL177 |
| A | ASP178 |
| B | ARG9 |
| B | ARG12 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| B | ALA175 |
| B | THR176 |
| B | VAL177 |
| B | ASP178 |
| A | GLN5 |
| A | ARG9 |
| A | ARG12 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | ARG271 |
| A | ARG388 |
| A | HOH602 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | HIS15 |
| A | ALA16 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | ARG23 |
| A | ASN27 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 506 |
| Chain | Residue |
| A | ASP292 |
| A | ASP293 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue THM A 507 |
| Chain | Residue |
| A | THR87 |
| A | ARG171 |
| A | VAL177 |
| A | SER186 |
| A | PHE210 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue THM A 508 |
| Chain | Residue |
| A | SER248 |
| A | SER249 |
| A | ARG257 |
| A | GLU258 |
| A | GLN261 |
| A | TYR267 |
| A | THR384 |
| A | ASP385 |
| A | ARG436 |
| A | ARG437 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 509 |
| Chain | Residue |
| A | TYR214 |
| A | GLU215 |
| A | GLU218 |
| A | PHE273 |
| A | GLN301 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 510 |
| Chain | Residue |
| A | ASP138 |
| A | ARG141 |
| A | LYS321 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 511 |
| Chain | Residue |
| A | GLU328 |
| A | ASN329 |
| A | TYR330 |
| A | ASP331 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 512 |
| Chain | Residue |
| A | ARG115 |
| A | ASP375 |
| A | THR376 |
| B | ARG56 |
| B | ALA219 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 501 |
| Chain | Residue |
| B | LYS84 |
| B | SER86 |
| B | SER95 |
| B | SER113 |
| B | THR123 |
| B | HOH615 |
| B | HOH602 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | TYR267 |
| B | PRO270 |
| B | ARG388 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | PRO270 |
| B | ARG271 |
| B | ARG388 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | ARG23 |
| B | ASN27 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue THM B 505 |
| Chain | Residue |
| B | SER248 |
| B | SER249 |
| B | GLU258 |
| B | GLN261 |
| B | TYR267 |
| B | THR384 |
| B | ASP385 |
| site_id | AD9 |
| Number of Residues | 9 |
| Details | binding site for residue THM B 506 |
| Chain | Residue |
| B | HIS85 |
| B | SER86 |
| B | THR87 |
| B | TYR168 |
| B | ARG171 |
| B | VAL177 |
| B | SER186 |
| B | LYS190 |
| B | PHE210 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| B | ARG268 |
| B | GLN301 |
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 |
