5H70
Crystal structure of ADP bound dTMP kinase (st1543) from Sulfolobus Tokodaii Strain7
Replaces: 4RZUFunctional 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 | 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 | 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 | 14 |
| Details | binding site for residue ADP B 301 |
| Chain | Residue |
| B | GLY14 |
| B | PRO194 |
| B | ILE197 |
| B | MG303 |
| B | HOH401 |
| B | HOH402 |
| B | SER15 |
| B | GLY16 |
| B | LYS17 |
| B | SER18 |
| B | SER19 |
| B | ARG138 |
| B | LYS192 |
| B | THR193 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | ASP108 |
| B | TRP111 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 303 |
| Chain | Residue |
| B | SER18 |
| B | ASP92 |
| B | ADP301 |
| B | HOH401 |
| B | HOH402 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue ADP A 301 |
| Chain | Residue |
| A | ASP13 |
| A | GLY14 |
| A | SER15 |
| A | GLY16 |
| A | LYS17 |
| A | SER18 |
| A | SER19 |
| A | ARG138 |
| A | SER142 |
| A | LYS192 |
| A | PRO194 |
| A | MG304 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | PHE63 |
| A | ARG105 |
| A | ASP154 |
| A | PGE303 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 303 |
| Chain | Residue |
| A | HIS46 |
| A | HIS67 |
| A | GLN149 |
| A | ASP154 |
| A | EDO302 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 304 |
| Chain | Residue |
| A | SER18 |
| A | ASP92 |
| A | ADP301 |
| A | HOH403 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| B | GLY11 | |
| A | GLY11 |
