5XT8
Magnesium bound apo structure of thymidylate kinase (form I) from Thermus thermophilus HB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004798 | molecular_function | thymidylate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| B | 0004798 | molecular_function | thymidylate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 201 |
| Chain | Residue |
| A | HIS192 |
| B | PRO170 |
| B | HOH362 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 202 |
| Chain | Residue |
| A | TYR62 |
| A | SER66 |
| A | ARG69 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 203 |
| Chain | Residue |
| A | ASP94 |
| A | THR127 |
| A | HOH400 |
| A | THR7 |
| A | GLU9 |
| A | TYR92 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 204 |
| Chain | Residue |
| A | GLN19 |
| A | LEU23 |
| A | HOH301 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 205 |
| Chain | Residue |
| A | GLY15 |
| A | THR17 |
| A | THR18 |
| A | CL209 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 206 |
| Chain | Residue |
| A | ARG22 |
| A | ARG139 |
| A | GLN190 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 207 |
| Chain | Residue |
| A | LYS123 |
| A | PRO124 |
| A | HOH400 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 208 |
| Chain | Residue |
| A | GLU169 |
| A | GLY171 |
| A | ARG172 |
| B | HOH378 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 209 |
| Chain | Residue |
| A | GLY13 |
| A | GLY15 |
| A | LYS16 |
| A | THR17 |
| A | MG205 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 210 |
| Chain | Residue |
| A | ALA25 |
| A | GLU28 |
| A | ALA29 |
| A | ARG140 |
| A | ALA178 |
| A | LEU180 |
| A | GLU182 |
| A | ILE185 |
| A | HOH315 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 211 |
| Chain | Residue |
| A | PHE173 |
| A | VAL175 |
| A | HOH325 |
| A | HOH336 |
| A | HOH355 |
| A | HOH389 |
| B | HOH337 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 201 |
| Chain | Residue |
| B | ARG22 |
| B | ALA83 |
| B | HOH375 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 202 |
| Chain | Residue |
| B | LYS123 |
| B | GLU169 |
| B | CL206 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 203 |
| Chain | Residue |
| B | THR7 |
| B | GLU9 |
| B | TYR92 |
| B | ASP94 |
| B | HOH370 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 204 |
| Chain | Residue |
| B | TYR62 |
| B | SER66 |
| B | ARG69 |
| B | LEU93 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 205 |
| Chain | Residue |
| B | ASP131 |
| B | ARG159 |
| B | TYR162 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue CL B 206 |
| Chain | Residue |
| A | HOH342 |
| B | GLU169 |
| B | PRO170 |
| B | GLY171 |
| B | ARG172 |
| B | MG202 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 207 |
| Chain | Residue |
| B | GLY13 |
| B | LYS16 |
| B | THR17 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 208 |
| Chain | Residue |
| B | LYS123 |
| B | PRO124 |
| B | HOH370 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 209 |
| Chain | Residue |
| A | ARG32 |
| A | HOH328 |
| A | HOH363 |
| B | PRO133 |
| B | ARG159 |
| B | HOH373 |
Functional Information from PROSITE/UniProt
| site_id | PS01331 |
| Number of Residues | 13 |
| Details | THYMIDYLATE_KINASE Thymidylate kinase signature. ISDRYldSSlAYQ |
| Chain | Residue | Details |
| A | ILE88-GLN100 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00165 |
| Chain | Residue | Details |
| A | GLY10 | |
| B | GLY10 |
