4GMD
The crystal structure of thymidylate kinase from Pseudomonas aeruginosa PAO1 in complex with AZT Monophosphate
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 |
| C | 0004798 | molecular_function | thymidylate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006227 | biological_process | dUDP biosynthetic process |
| C | 0006233 | biological_process | dTDP biosynthetic process |
| C | 0006235 | biological_process | dTTP biosynthetic process |
| C | 0009165 | biological_process | nucleotide biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| D | 0004798 | molecular_function | thymidylate kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006227 | biological_process | dUDP biosynthetic process |
| D | 0006233 | biological_process | dTDP biosynthetic process |
| D | 0006235 | biological_process | dTTP biosynthetic process |
| D | 0009165 | biological_process | nucleotide biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ATM A 301 |
| Chain | Residue |
| A | ARG50 |
| A | PHE155 |
| A | HOH423 |
| A | MET70 |
| A | ARG74 |
| A | ARG96 |
| A | ALA100 |
| A | THR101 |
| A | TYR104 |
| A | GLN105 |
| A | ARG151 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | ARG20 |
| A | THR37 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | PRO178 |
| A | GLU179 |
| A | TYR181 |
| A | GLN182 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ATM B 301 |
| Chain | Residue |
| B | GLU39 |
| B | PRO40 |
| B | ARG50 |
| B | MET70 |
| B | ARG74 |
| B | ARG96 |
| B | PHE97 |
| B | ALA100 |
| B | THR101 |
| B | TYR104 |
| B | GLN105 |
| B | ASP153 |
| B | PHE155 |
| B | HOH417 |
| B | HOH422 |
| B | HOH448 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 302 |
| Chain | Residue |
| B | ARG20 |
| B | THR37 |
| B | ARG38 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 303 |
| Chain | Residue |
| B | PRO11 |
| B | GLU12 |
| B | GLY13 |
| B | ALA14 |
| B | GLY15 |
| B | LYS16 |
| B | SER17 |
| B | HOH423 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 304 |
| Chain | Residue |
| B | ARG26 |
| B | GLU29 |
| C | ARG48 |
| C | GLU51 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ATM C 301 |
| Chain | Residue |
| C | GLU39 |
| C | PRO40 |
| C | ARG50 |
| C | MET70 |
| C | ARG74 |
| C | ARG96 |
| C | THR101 |
| C | TYR104 |
| C | GLN105 |
| C | PHE155 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 302 |
| Chain | Residue |
| C | ARG20 |
| C | THR37 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 303 |
| Chain | Residue |
| C | GLY10 |
| C | PRO11 |
| C | TYR104 |
| C | TYR170 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATM D 301 |
| Chain | Residue |
| D | GLU12 |
| D | GLU39 |
| D | PRO40 |
| D | ARG50 |
| D | MET70 |
| D | ARG74 |
| D | ARG96 |
| D | ALA100 |
| D | THR101 |
| D | TYR104 |
| D | GLN105 |
| D | ASP153 |
| D | PHE155 |
| D | HOH436 |
| D | HOH490 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 302 |
| Chain | Residue |
| B | GLN157 |
| D | GLU158 |
| D | ASP159 |
| D | HOH497 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 303 |
| Chain | Residue |
| D | GLY10 |
| D | PRO11 |
| D | ARG96 |
| D | TYR104 |
| D | TYR170 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 304 |
| Chain | Residue |
| D | ARG20 |
| D | THR37 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY10 | |
| B | GLY10 | |
| C | GLY10 | |
| D | GLY10 |
