3V9P
Crystal structure of Thymidylate kinase from Burkholderia thailandensis
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 | 6 |
Details | BINDING SITE FOR RESIDUE MRD A 250 |
Chain | Residue |
A | MET72 |
A | ARG76 |
A | THR103 |
A | TYR106 |
A | GLN107 |
A | HOH280 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 252 |
Chain | Residue |
A | HOH329 |
B | ALA170 |
B | ARG174 |
B | GLN177 |
A | PHE183 |
A | ILE185 |
A | HOH208 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 253 |
Chain | Residue |
A | GLU190 |
A | PRO191 |
A | ILE192 |
A | HOH297 |
B | ALA81 |
B | LEU82 |
B | PRO86 |
B | HOH232 |
B | HOH284 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACT A 255 |
Chain | Residue |
A | GLU44 |
A | PRO45 |
A | GLY46 |
A | GLY47 |
A | GLY51 |
A | GLY75 |
A | ARG76 |
A | HOH216 |
A | HOH237 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MRD B 250 |
Chain | Residue |
B | MET72 |
B | ARG76 |
B | THR103 |
B | TYR106 |
B | GLN107 |
B | HOH305 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACT B 255 |
Chain | Residue |
B | GLU44 |
B | PRO45 |
B | GLY46 |
B | GLY47 |
B | GLY51 |
B | GLY75 |
B | ARG76 |
B | HOH227 |
B | HOH291 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG B 207 |
Chain | Residue |
A | PRO180 |
B | ALA166 |
B | ARG169 |
B | ALA170 |
B | HOH319 |
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 | GLY11 | |
B | GLY11 |