5X86
Crystal structure of TMP 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 | 5 |
Details | binding site for residue CL B 201 |
Chain | Residue |
B | GLY13 |
B | SER14 |
B | GLY15 |
B | LYS16 |
B | THR17 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue MG B 202 |
Chain | Residue |
B | TYR62 |
B | SER66 |
B | ARG69 |
B | ALA115 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MG B 203 |
Chain | Residue |
B | ARG157 |
B | GLY161 |
B | HOH376 |
B | HOH429 |
B | HOH454 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG B 204 |
Chain | Residue |
B | THR7 |
B | GLU9 |
B | TYR92 |
B | ASP94 |
B | THR127 |
B | HOH383 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue MG B 205 |
Chain | Residue |
B | GLU160 |
B | ARG167 |
B | HOH439 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue MG B 206 |
Chain | Residue |
B | ASP12 |
B | TYR99 |
B | PHE155 |
B | HOH312 |
B | HOH373 |
site_id | AC7 |
Number of Residues | 17 |
Details | binding site for residue TMP B 207 |
Chain | Residue |
B | ASP12 |
B | ARG38 |
B | GLU39 |
B | PRO40 |
B | ARG48 |
B | PHE65 |
B | ARG69 |
B | ARG91 |
B | SER95 |
B | SER96 |
B | TYR99 |
B | GLN100 |
B | HOH301 |
B | HOH312 |
B | HOH362 |
B | HOH389 |
B | HOH408 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CL A 201 |
Chain | Residue |
A | GLY13 |
A | GLY15 |
A | LYS16 |
A | THR17 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue MG A 202 |
Chain | Residue |
A | TYR62 |
A | SER66 |
A | ARG69 |
A | LEU93 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue MG A 203 |
Chain | Residue |
A | PRO109 |
A | HOH420 |
B | HOH328 |
B | HOH340 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue MG A 204 |
Chain | Residue |
A | THR7 |
A | GLU9 |
A | TYR92 |
A | ASP94 |
A | HOH355 |
site_id | AD3 |
Number of Residues | 16 |
Details | binding site for residue TMP A 205 |
Chain | Residue |
A | ASP12 |
A | ARG38 |
A | PRO40 |
A | ARG48 |
A | PHE65 |
A | ARG69 |
A | ARG91 |
A | SER95 |
A | SER96 |
A | TYR99 |
A | GLN100 |
A | LEU147 |
A | LEU150 |
A | HOH306 |
A | HOH376 |
A | HOH422 |
Functional Information from PROSITE/UniProt
site_id | PS01331 |
Number of Residues | 13 |
Details | THYMIDYLATE_KINASE Thymidylate kinase signature. ISDRYldSSlAYQ |
Chain | Residue | Details |
B | 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 |
B | GLY10 | |
A | GLY10 |