5X8B
Crystal structure of ATP-TMP and ADP bound thymidylate kinase 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 | 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 | 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 | 23 |
| Details | binding site for residue ATP A 201 |
| Chain | Residue |
| A | LEU11 |
| A | ARG91 |
| A | ALA178 |
| A | LEU180 |
| A | GLU182 |
| A | TMP202 |
| A | MG203 |
| A | HOH325 |
| A | HOH331 |
| A | HOH332 |
| A | HOH336 |
| A | ASP12 |
| A | HOH344 |
| A | HOH353 |
| A | HOH357 |
| A | HOH374 |
| A | GLY13 |
| A | SER14 |
| A | GLY15 |
| A | LYS16 |
| A | THR17 |
| A | THR18 |
| A | GLN54 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue TMP A 202 |
| Chain | Residue |
| A | ASP12 |
| A | ARG38 |
| A | PRO40 |
| A | ARG48 |
| A | PHE65 |
| A | ARG69 |
| A | ARG91 |
| A | SER95 |
| A | SER96 |
| A | TYR99 |
| A | GLN100 |
| A | LEU147 |
| A | LEU150 |
| A | ATP201 |
| A | HOH353 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 203 |
| Chain | Residue |
| A | THR17 |
| A | ATP201 |
| A | HOH325 |
| A | HOH331 |
| A | HOH353 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 204 |
| Chain | Residue |
| A | TYR62 |
| A | SER66 |
| A | ARG69 |
| A | LEU93 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 205 |
| Chain | Residue |
| A | GLY10 |
| A | LEU11 |
| A | LEU130 |
| A | ASP131 |
| A | LEU132 |
| A | HOH346 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 206 |
| Chain | Residue |
| A | THR7 |
| A | GLU9 |
| A | TYR92 |
| A | ASP94 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 201 |
| Chain | Residue |
| B | TYR62 |
| B | SER66 |
| B | ARG69 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 202 |
| Chain | Residue |
| B | ASP12 |
| B | TYR99 |
| B | PHE155 |
| B | HOH377 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 203 |
| Chain | Residue |
| B | THR17 |
| B | ADP204 |
| B | HOH301 |
| B | HOH302 |
| B | HOH360 |
| B | HOH403 |
| site_id | AD1 |
| Number of Residues | 20 |
| Details | binding site for residue ADP B 204 |
| Chain | Residue |
| A | GLY105 |
| B | LEU11 |
| B | ASP12 |
| B | GLY13 |
| B | SER14 |
| B | GLY15 |
| B | LYS16 |
| B | THR17 |
| B | THR18 |
| B | LEU138 |
| B | ARG139 |
| B | LEU180 |
| B | GLU182 |
| B | MG203 |
| B | HOH301 |
| B | HOH302 |
| B | HOH332 |
| B | HOH360 |
| B | HOH391 |
| B | HOH411 |
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 |
