5X8C
AMPPCP and TMP bound crystal structure of 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 | 14 |
| Details | binding site for residue TMP A 201 |
| Chain | Residue |
| A | ASP12 |
| A | SER96 |
| A | TYR99 |
| A | GLN100 |
| A | LEU147 |
| A | HOH304 |
| A | ARG38 |
| A | GLU39 |
| A | PRO40 |
| A | ARG48 |
| A | PHE65 |
| A | ARG69 |
| A | ARG91 |
| A | SER95 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 202 |
| Chain | Residue |
| A | THR7 |
| A | GLU9 |
| A | TYR92 |
| A | ASP94 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 203 |
| Chain | Residue |
| A | TYR62 |
| A | SER66 |
| A | ARG69 |
| A | LEU93 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 204 |
| Chain | Residue |
| A | GLU39 |
| A | PRO40 |
| A | PHE65 |
| A | ASP68 |
| A | ARG69 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 205 |
| Chain | Residue |
| A | THR17 |
| A | ACP209 |
| A | HOH340 |
| A | HOH355 |
| A | HOH367 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 206 |
| Chain | Residue |
| A | LEU165 |
| A | ALA168 |
| A | GLU169 |
| A | HOH373 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 207 |
| Chain | Residue |
| A | GLU169 |
| A | PRO170 |
| A | GLY171 |
| A | ARG172 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 208 |
| Chain | Residue |
| A | LEU4 |
| A | PHE5 |
| A | HOH314 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | binding site for residue ACP A 209 |
| Chain | Residue |
| A | LEU11 |
| A | ASP12 |
| A | GLY13 |
| A | SER14 |
| A | GLY15 |
| A | LYS16 |
| A | THR17 |
| A | THR18 |
| A | GLN54 |
| A | ARG91 |
| A | ALA178 |
| A | LEU180 |
| A | GLU182 |
| A | MG205 |
| A | HOH304 |
| A | HOH316 |
| A | HOH340 |
| A | HOH354 |
| A | HOH367 |
| site_id | AD1 |
| Number of Residues | 11 |
| Details | binding site for residue TMP B 201 |
| Chain | Residue |
| B | ASP12 |
| B | ARG38 |
| B | PRO40 |
| B | ARG48 |
| B | PHE65 |
| B | ARG69 |
| B | SER95 |
| B | SER96 |
| B | TYR99 |
| B | GLN100 |
| B | HOH304 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 202 |
| Chain | Residue |
| B | TYR62 |
| B | SER66 |
| B | ARG69 |
| B | LEU93 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 203 |
| Chain | Residue |
| B | PRO40 |
| B | PHE65 |
| B | ASP68 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 204 |
| Chain | Residue |
| B | THR7 |
| B | GLU9 |
| B | TYR92 |
| B | ASP94 |
| B | THR127 |
| B | HOH352 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 205 |
| Chain | Residue |
| B | ASP12 |
| B | TYR99 |
| B | HOH304 |
| B | HOH341 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 206 |
| Chain | Residue |
| B | GLN19 |
| B | ARG22 |
| B | LEU23 |
| B | ILE189 |
| B | HOH350 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 207 |
| Chain | Residue |
| B | LEU165 |
| B | GLU169 |
| B | HOH361 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 208 |
| Chain | Residue |
| B | HOH306 |
| B | HOH359 |
| B | ASP177 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 209 |
| Chain | Residue |
| B | LYS123 |
| B | PRO124 |
| B | HOH318 |
| B | HOH352 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 210 |
| Chain | Residue |
| B | GLY13 |
| B | SER14 |
| B | GLY15 |
| B | LYS16 |
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 |
