1E98
Wild type human thymidylate kinase complexed with AZTMP and ADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
A | 0004798 | molecular_function | thymidylate kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
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 | 0016740 | molecular_function | transferase activity |
A | 0043627 | biological_process | response to estrogen |
A | 0045445 | biological_process | myoblast differentiation |
A | 0046105 | biological_process | thymidine biosynthetic process |
A | 0046686 | biological_process | response to cadmium ion |
A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
A | 0071363 | biological_process | cellular response to growth factor stimulus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | SER20 |
A | ADP214 |
A | HOH2068 |
A | HOH2159 |
A | HOH2166 |
A | HOH2167 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 402 |
Chain | Residue |
A | HOH2082 |
A | HOH2087 |
A | HOH2087 |
A | HOH2030 |
A | HOH2030 |
A | HOH2082 |
site_id | AC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE ADP A 214 |
Chain | Residue |
A | ARG16 |
A | ALA17 |
A | GLY18 |
A | LYS19 |
A | SER20 |
A | THR21 |
A | ARG143 |
A | ALA180 |
A | LYS182 |
A | ARG183 |
A | ILE184 |
A | ARG192 |
A | MG401 |
A | HOH2137 |
A | HOH2156 |
A | HOH2157 |
A | HOH2158 |
A | HOH2159 |
A | HOH2160 |
A | HOH2161 |
A | HOH2162 |
A | HOH2163 |
A | HOH2164 |
A | HOH2165 |
A | HOH2167 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ATM A 301 |
Chain | Residue |
A | PHE42 |
A | LEU57 |
A | PHE72 |
A | ARG76 |
A | ARG97 |
A | GLY102 |
A | PHE105 |
A | TYR151 |
A | GLN157 |
A | ARG200 |
A | HOH2010 |
A | HOH2068 |
A | HOH2106 |
A | HOH2166 |
A | HOH2167 |
A | HOH2168 |
A | HOH2169 |
A | HOH2170 |
A | HOH2171 |
A | HOH2172 |
Functional Information from PROSITE/UniProt
site_id | PS01331 |
Number of Residues | 13 |
Details | THYMIDYLATE_KINASE Thymidylate kinase signature. VVDRYafSGvAFT |
Chain | Residue | Details |
A | VAL94-THR106 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12614151, ECO:0007744|PDB:1NMX, ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NN0, ECO:0007744|PDB:1NN3 |
Chain | Residue | Details |
A | ARG16 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12614151, ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NMZ, ECO:0007744|PDB:1NN1 |
Chain | Residue | Details |
A | ARG97 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1NMX, ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NN0, ECO:0007744|PDB:1NN3 |
Chain | Residue | Details |
A | LYS182 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NMZ, ECO:0007744|PDB:1NN1, ECO:0007744|PDB:1NN5 |
Chain | Residue | Details |
A | ARG192 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | ALA2 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS169 |