5X8A
Crystal structure of ATP bound thymidylate kinase from thermus thermophilus HB8
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004798 | molecular_function | thymidylate kinase activity |
A | 0005524 | molecular_function | ATP binding |
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 | 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 | 2 |
Details | binding site for residue MG A 201 |
Chain | Residue |
A | VAL175 |
B | HOH335 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue CL A 202 |
Chain | Residue |
A | GLU169 |
A | GLY171 |
A | ARG172 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CL A 203 |
Chain | Residue |
A | GLY13 |
A | GLY15 |
A | LYS16 |
A | THR17 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue CL A 204 |
Chain | Residue |
A | LYS123 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CL A 205 |
Chain | Residue |
A | ARG22 |
A | ARG139 |
A | HOH301 |
A | HOH323 |
site_id | AC6 |
Number of Residues | 23 |
Details | binding site for residue ATP B 201 |
Chain | Residue |
B | PRO2 |
B | LEU11 |
B | ASP12 |
B | GLY13 |
B | SER14 |
B | GLY15 |
B | LYS16 |
B | THR17 |
B | THR18 |
B | GLU28 |
B | GLY31 |
B | ARG91 |
B | ARG140 |
B | VAL141 |
B | LEU180 |
B | PRO181 |
B | GLU182 |
B | ILE185 |
B | MG202 |
B | PEG206 |
B | HOH301 |
B | HOH304 |
B | HOH322 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue MG B 202 |
Chain | Residue |
B | THR17 |
B | ATP201 |
B | HOH301 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue MG B 203 |
Chain | Residue |
B | PHE65 |
B | SER96 |
B | GLN100 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue CL B 204 |
Chain | Residue |
A | HOH335 |
B | GLU169 |
B | GLY171 |
B | ARG172 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue PEG B 205 |
Chain | Residue |
B | GLU113 |
B | ARG116 |
B | GLU117 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue PEG B 206 |
Chain | Residue |
B | GLU28 |
B | ARG32 |
B | VAL34 |
B | GLU182 |
B | ATP201 |
Functional Information from PROSITE/UniProt
site_id | PS01331 |
Number of Residues | 13 |
Details | THYMIDYLATE_KINASE Thymidylate kinase signature. ISDRYldSSlAYQ |
Chain | Residue | Details |
A | ILE88-GLN100 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00165 |
Chain | Residue | Details |
A | GLY10 | |
B | GLY10 |