4NZY
Crystal structure (type-2) of dTMP kinase (st1543) from Sulfolobus Tokodaii Strain7
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 | 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 | 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 | 8 |
Details |
Chain | Residue |
A | TYR35 |
A | THR37 |
A | SER41 |
A | SER42 |
A | ASP43 |
A | ARG74 |
A | TYR78 |
A | HOH473 |
site_id | AC2 |
Number of Residues | 6 |
Details |
Chain | Residue |
A | SER15 |
A | GLY16 |
A | LYS17 |
A | SER18 |
A | HOH446 |
A | GLY14 |
site_id | AC3 |
Number of Residues | 7 |
Details |
Chain | Residue |
A | VAL107 |
A | ASP108 |
A | TRP111 |
A | HOH461 |
A | HOH501 |
B | SER117 |
B | PHE118 |
site_id | AC4 |
Number of Residues | 7 |
Details |
Chain | Residue |
A | TRP39 |
A | SER42 |
A | HIS67 |
A | ASP70 |
A | ARG74 |
A | HOH429 |
A | HOH488 |
site_id | AC5 |
Number of Residues | 2 |
Details |
Chain | Residue |
A | LYS195 |
A | ARG202 |
site_id | AC6 |
Number of Residues | 5 |
Details |
Chain | Residue |
A | SER103 |
A | LEU171 |
A | GLU174 |
A | VAL175 |
A | LYS178 |
site_id | AC7 |
Number of Residues | 8 |
Details |
Chain | Residue |
A | TYR96 |
A | PRO122 |
A | ASP123 |
A | ILE124 |
A | THR125 |
A | GLU183 |
A | ASN184 |
B | PG4301 |
site_id | AC8 |
Number of Residues | 4 |
Details |
Chain | Residue |
A | ARG129 |
A | VAL130 |
A | ASP189 |
A | HOH433 |
site_id | AC9 |
Number of Residues | 2 |
Details |
Chain | Residue |
A | ARG129 |
A | HOH483 |
site_id | BC1 |
Number of Residues | 7 |
Details |
Chain | Residue |
A | ARG93 |
A | ARG101 |
A | GLN149 |
A | TYR168 |
A | HOH404 |
A | HOH463 |
A | HOH480 |
site_id | BC2 |
Number of Residues | 2 |
Details |
Chain | Residue |
A | LYS140 |
A | GLN200 |
site_id | BC3 |
Number of Residues | 6 |
Details |
Chain | Residue |
A | LYS121 |
A | GLU183 |
A | PEG307 |
B | ARG129 |
B | ASP177 |
B | HOH404 |
site_id | BC4 |
Number of Residues | 4 |
Details |
Chain | Residue |
A | LYS113 |
B | SER103 |
B | GLU174 |
B | LYS178 |
site_id | BC5 |
Number of Residues | 7 |
Details |
Chain | Residue |
B | ILE12 |
B | ASP13 |
B | GLY14 |
B | SER15 |
B | GLY16 |
B | LYS17 |
B | SER18 |
site_id | BC6 |
Number of Residues | 4 |
Details |
Chain | Residue |
A | SER117 |
B | ASP108 |
B | TRP111 |
B | 1PE311 |
site_id | BC7 |
Number of Residues | 6 |
Details |
Chain | Residue |
A | SER131 |
A | GLY170 |
A | THR173 |
A | GLU174 |
B | LYS53 |
B | ASP56 |
site_id | BC8 |
Number of Residues | 4 |
Details |
Chain | Residue |
B | PRO132 |
B | GLY170 |
B | THR173 |
B | HOH402 |
site_id | BC9 |
Number of Residues | 3 |
Details |
Chain | Residue |
B | LEU58 |
B | PHE63 |
B | ASP154 |
site_id | CC1 |
Number of Residues | 2 |
Details |
Chain | Residue |
B | SER117 |
B | PHE118 |
site_id | CC2 |
Number of Residues | 1 |
Details |
Chain | Residue |
B | HOH450 |
site_id | CC3 |
Number of Residues | 4 |
Details |
Chain | Residue |
B | PHE71 |
B | TYR94 |
B | ARG101 |
B | TYR116 |
site_id | CC4 |
Number of Residues | 7 |
Details |
Chain | Residue |
A | LYS114 |
A | SER117 |
B | ASP110 |
B | TRP111 |
B | GLU174 |
B | PEG304 |
B | HOH431 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | GLY11 | |
B | GLY11 |