Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004798 | molecular_function | dTMP kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006227 | biological_process | dUDP biosynthetic process |
| A | 0006233 | biological_process | dTDP biosynthetic process |
| A | 0006235 | biological_process | dTTP biosynthetic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046044 | biological_process | TMP metabolic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004798 | molecular_function | dTMP kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006227 | biological_process | dUDP biosynthetic process |
| B | 0006233 | biological_process | dTDP biosynthetic process |
| B | 0006235 | biological_process | dTTP biosynthetic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046044 | biological_process | TMP metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue YUI A 301 |
| Chain | Residue |
| A | ASP9 |
| A | TYR103 |
| A | HOH419 |
| A | PHE36 |
| A | PRO37 |
| A | LEU52 |
| A | HIS53 |
| A | PHE70 |
| A | ARG74 |
| A | ARG95 |
| A | ASN100 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | GLY10 |
| A | ALA11 |
| A | GLY12 |
| A | LYS13 |
| A | HOH425 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue YUI B 301 |
| Chain | Residue |
| B | ASP9 |
| B | PHE36 |
| B | PRO37 |
| B | LEU52 |
| B | PHE70 |
| B | ARG74 |
| B | ARG95 |
| B | ASN100 |
| B | TYR103 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 302 |
| Chain | Residue |
| B | GLY10 |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
Functional Information from PROSITE/UniProt
| site_id | PS01331 |
| Number of Residues | 13 |
| Details | THYMIDYLATE_KINASE Thymidylate kinase signature. ILDRYvaSNaAYS |
| Chain | Residue | Details |
| A | ILE92-SER104 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {} |
5NR7
