Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
| A | 0004798 | molecular_function | dTMP kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006227 | biological_process | dUDP biosynthetic process |
| A | 0006233 | biological_process | dTDP biosynthetic process |
| A | 0006235 | biological_process | dTTP biosynthetic process |
| A | 0008150 | biological_process | biological_process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0120136 | molecular_function | dUMP kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue TMP A 301 |
| Chain | Residue |
| A | LYS35 |
| A | HOH411 |
| A | HOH413 |
| A | HOH424 |
| A | HOH428 |
| A | HOH430 |
| A | HOH436 |
| A | HOH440 |
| A | HOH454 |
| A | ARG39 |
| A | LEU51 |
| A | PHE67 |
| A | ARG71 |
| A | ARG92 |
| A | GLY97 |
| A | TYR100 |
| A | TYR161 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue ADP A 302 |
| Chain | Residue |
| A | LEU12 |
| A | ASP13 |
| A | ARG14 |
| A | SER15 |
| A | GLY16 |
| A | LYS17 |
| A | SER18 |
| A | THR19 |
| A | ARG153 |
| A | LYS154 |
| A | LYS194 |
| A | THR195 |
| A | ILE196 |
| A | MG303 |
| A | HOH416 |
| A | HOH417 |
| A | HOH432 |
| A | HOH443 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 303 |
| Chain | Residue |
| A | ASP13 |
| A | ADP302 |
| A | HOH424 |
| A | HOH432 |
| A | HOH454 |
| A | HOH471 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 304 |
| Chain | Residue |
| A | ASP13 |
| A | GLY155 |
| A | GLU162 |
| A | HOH450 |
Functional Information from PROSITE/UniProt
| site_id | PS01331 |
| Number of Residues | 13 |
| Details | THYMIDYLATE_KINASE Thymidylate kinase signature. ILDRYiySGiAYT |
| Chain | Residue | Details |
| A | ILE89-THR101 | |
