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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 |