5XB3
ADP-dTMP 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 | 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 | 16 |
Details | binding site for residue ADP A 201 |
Chain | Residue |
A | GLY10 |
A | GLU177 |
A | GLU178 |
A | HOH323 |
A | HOH339 |
A | HOH357 |
A | HOH376 |
A | HOH388 |
A | SER11 |
A | GLY12 |
A | LYS13 |
A | THR14 |
A | THR15 |
A | ARG139 |
A | ARG145 |
A | GLY176 |
site_id | AC2 |
Number of Residues | 14 |
Details | binding site for residue TMP A 202 |
Chain | Residue |
A | ASP9 |
A | GLU36 |
A | ARG47 |
A | PHE64 |
A | ARG90 |
A | THR95 |
A | TYR98 |
A | GLN99 |
A | HOH323 |
A | HOH339 |
A | HOH359 |
A | HOH363 |
A | HOH397 |
A | HOH402 |
site_id | AC3 |
Number of Residues | 20 |
Details | binding site for residue ADP B 201 |
Chain | Residue |
B | GLY10 |
B | SER11 |
B | GLY12 |
B | LYS13 |
B | THR14 |
B | THR15 |
B | ARG139 |
B | LYS143 |
B | ARG145 |
B | GLY176 |
B | GLU177 |
B | GLU178 |
B | HOH303 |
B | HOH311 |
B | HOH340 |
B | HOH346 |
B | HOH352 |
B | HOH359 |
B | HOH360 |
B | HOH379 |
site_id | AC4 |
Number of Residues | 17 |
Details | binding site for residue TMP B 202 |
Chain | Residue |
B | ASP9 |
B | GLU36 |
B | ARG47 |
B | PHE64 |
B | ARG90 |
B | THR95 |
B | TYR98 |
B | GLN99 |
B | ARG145 |
B | HOH301 |
B | HOH340 |
B | HOH352 |
B | HOH358 |
B | HOH378 |
B | HOH384 |
B | HOH393 |
B | HOH406 |
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 |