4EDH
The crystal structure of thymidylate kinase from Pseudomonas aeruginosa PAO1 in complex with ADP,TMP and Mg.
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE TMP A 301 |
Chain | Residue |
A | GLU39 |
A | GLN105 |
A | PHE155 |
A | HOH422 |
A | HOH440 |
A | HOH441 |
A | HOH472 |
A | HOH600 |
A | HOH601 |
A | PRO40 |
A | ARG50 |
A | MET70 |
A | ARG74 |
A | ARG96 |
A | ALA100 |
A | THR101 |
A | TYR104 |
site_id | AC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ADP A 302 |
Chain | Residue |
A | GLY13 |
A | ALA14 |
A | GLY15 |
A | LYS16 |
A | SER17 |
A | THR18 |
A | ARG145 |
A | ALA186 |
A | LEU188 |
A | PRO189 |
A | LEU190 |
A | VAL193 |
A | MG303 |
A | HOH408 |
A | HOH475 |
A | HOH532 |
A | HOH536 |
A | HOH552 |
A | HOH576 |
A | HOH600 |
A | HOH603 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 303 |
Chain | Residue |
A | SER17 |
A | ADP302 |
A | HOH472 |
A | HOH599 |
A | HOH600 |
A | HOH603 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRS A 304 |
Chain | Residue |
A | ASP185 |
A | GLY187 |
A | HOH442 |
A | HOH526 |
B | PRO138 |
B | ILE141 |
B | ASP185 |
B | GLY187 |
B | HOH431 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 305 |
Chain | Residue |
A | ARG128 |
A | ARG180 |
A | HOH594 |
A | HOH598 |
B | EDO304 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE TMP B 301 |
Chain | Residue |
B | GLU12 |
B | GLU39 |
B | PRO40 |
B | ARG50 |
B | MET70 |
B | ARG74 |
B | ARG96 |
B | ALA100 |
B | THR101 |
B | TYR104 |
B | GLN105 |
B | PHE155 |
B | HOH414 |
B | HOH415 |
B | HOH416 |
B | HOH536 |
B | HOH621 |
B | HOH622 |
B | HOH623 |
site_id | AC7 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ADP B 302 |
Chain | Residue |
A | ASP126 |
A | HOH515 |
B | GLY13 |
B | ALA14 |
B | GLY15 |
B | LYS16 |
B | SER17 |
B | THR18 |
B | ARG145 |
B | ALA186 |
B | LEU188 |
B | LEU190 |
B | MG303 |
B | HOH430 |
B | HOH434 |
B | HOH481 |
B | HOH490 |
B | HOH578 |
B | HOH583 |
B | HOH621 |
B | HOH624 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 303 |
Chain | Residue |
B | ADP302 |
B | HOH621 |
B | HOH622 |
B | HOH623 |
B | HOH624 |
B | SER17 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 304 |
Chain | Residue |
A | ALA177 |
A | GLU179 |
A | SO4305 |
B | ARG38 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | GLY10 | |
B | GLY10 |