5H5K
ATP and CMP bound Crystal structure of thymidylate kinase (aq_969) from Aquifex Aeolicus VF5
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue MG A 201 |
Chain | Residue |
A | THR14 |
A | ATP202 |
A | C5P206 |
A | HOH308 |
A | HOH314 |
site_id | AC2 |
Number of Residues | 18 |
Details | binding site for residue ATP A 202 |
Chain | Residue |
A | GLY12 |
A | LYS13 |
A | THR14 |
A | THR15 |
A | ARG90 |
A | ARG139 |
A | ARG145 |
A | GLY176 |
A | GLU177 |
A | GLU178 |
A | MG201 |
A | C5P206 |
A | HOH308 |
A | HOH309 |
A | ILE8 |
A | ASP9 |
A | GLY10 |
A | SER11 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 203 |
Chain | Residue |
A | VAL31 |
A | LYS84 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 204 |
Chain | Residue |
A | ARG58 |
B | GLU115 |
B | ARG119 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue EDO A 205 |
Chain | Residue |
A | ARG119 |
B | ARG58 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue C5P A 206 |
Chain | Residue |
A | ASP9 |
A | ARG47 |
A | PHE64 |
A | ARG90 |
A | SER94 |
A | THR95 |
A | TYR98 |
A | GLN99 |
A | ARG145 |
A | MG201 |
A | ATP202 |
A | HOH301 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue MG B 201 |
Chain | Residue |
B | THR14 |
B | ATP202 |
B | C5P203 |
site_id | AC8 |
Number of Residues | 17 |
Details | binding site for residue ATP B 202 |
Chain | Residue |
B | ILE8 |
B | ASP9 |
B | GLY10 |
B | SER11 |
B | GLY12 |
B | LYS13 |
B | THR14 |
B | THR15 |
B | ARG90 |
B | ARG139 |
B | GLY176 |
B | GLU177 |
B | GLU178 |
B | MG201 |
B | C5P203 |
B | HOH314 |
B | HOH322 |
site_id | AC9 |
Number of Residues | 11 |
Details | binding site for residue C5P B 203 |
Chain | Residue |
B | ASP9 |
B | ARG47 |
B | PHE64 |
B | ARG90 |
B | SER94 |
B | THR95 |
B | TYR98 |
B | GLN99 |
B | MG201 |
B | ATP202 |
B | HOH302 |
Functional Information from PROSITE/UniProt
site_id | PS01331 |
Number of Residues | 13 |
Details | THYMIDYLATE_KINASE Thymidylate kinase signature. ILDRFvlSTiAYQ |
Chain | Residue | Details |
A | ILE87-GLN99 |
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 |