3HJN
Crystal structure of thymidylate kinase in complex with dTDP and ADP from Thermotoga maritima
Replaces: 2Z0HFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016310 | biological_process | phosphorylation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP A 301 |
| Chain | Residue |
| A | ILE8 |
| A | ARG138 |
| A | LYS139 |
| A | ARG176 |
| A | ILE178 |
| A | ILE181 |
| A | HOH214 |
| A | HOH215 |
| A | HOH217 |
| A | HOH220 |
| A | HOH221 |
| A | GLY10 |
| A | HOH243 |
| A | TYD401 |
| A | MG501 |
| A | SER11 |
| A | GLY12 |
| A | LYS13 |
| A | SER14 |
| A | THR15 |
| A | GLN18 |
| A | ARG35 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE TYD A 401 |
| Chain | Residue |
| A | ASP9 |
| A | LYS13 |
| A | ARG47 |
| A | PHE64 |
| A | ARG68 |
| A | ARG89 |
| A | SER93 |
| A | SER94 |
| A | TYR97 |
| A | GLN98 |
| A | LYS139 |
| A | ASN143 |
| A | PHE145 |
| A | HOH224 |
| A | HOH239 |
| A | HOH242 |
| A | ADP301 |
| A | MG501 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | SER14 |
| A | HOH239 |
| A | HOH242 |
| A | HOH243 |
| A | ADP301 |
| A | TYD401 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP B 302 |
| Chain | Residue |
| B | GLY10 |
| B | SER11 |
| B | GLY12 |
| B | LYS13 |
| B | SER14 |
| B | THR15 |
| B | LYS26 |
| B | ARG138 |
| B | GLY174 |
| B | ARG176 |
| B | SER177 |
| B | ILE178 |
| B | ILE181 |
| B | TYD402 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE TYD B 402 |
| Chain | Residue |
| B | ASP9 |
| B | LYS13 |
| B | GLU36 |
| B | ARG47 |
| B | PHE64 |
| B | ARG68 |
| B | ARG89 |
| B | SER93 |
| B | SER94 |
| B | TYR97 |
| B | GLN98 |
| B | ASN143 |
| B | PHE145 |
| B | HOH198 |
| B | ADP302 |
Functional Information from PROSITE/UniProt
| site_id | PS01331 |
| Number of Residues | 13 |
| Details | THYMIDYLATE_KINASE Thymidylate kinase signature. LLDRYtdSSvAYQ |
| Chain | Residue | Details |
| A | LEU86-GLN98 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY7 | |
| B | GLY7 |
