2J87
Structure of vaccinia virus thymidine kinase in complex with dTTP: insights for drug design
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004797 | molecular_function | thymidine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0009157 | biological_process | deoxyribonucleoside monophosphate biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0046104 | biological_process | thymidine metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071897 | biological_process | DNA biosynthetic process |
| B | 0004797 | molecular_function | thymidine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0009157 | biological_process | deoxyribonucleoside monophosphate biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0046104 | biological_process | thymidine metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071897 | biological_process | DNA biosynthetic process |
| C | 0004797 | molecular_function | thymidine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0009157 | biological_process | deoxyribonucleoside monophosphate biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0046104 | biological_process | thymidine metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071897 | biological_process | DNA biosynthetic process |
| D | 0004797 | molecular_function | thymidine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0009157 | biological_process | deoxyribonucleoside monophosphate biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0046104 | biological_process | thymidine metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0071897 | biological_process | DNA biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 400 |
| Chain | Residue |
| A | CYS138 |
| A | CYS141 |
| A | CYS170 |
| A | CYS173 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 500 |
| Chain | Residue |
| A | PHE14 |
| A | TTP300 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 400 |
| Chain | Residue |
| B | CYS173 |
| B | CYS138 |
| B | CYS141 |
| B | CYS170 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 500 |
| Chain | Residue |
| B | MET13 |
| B | PHE14 |
| B | TTP300 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 400 |
| Chain | Residue |
| C | CYS138 |
| C | CYS141 |
| C | CYS170 |
| C | CYS173 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 500 |
| Chain | Residue |
| C | MET13 |
| C | TTP300 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 400 |
| Chain | Residue |
| D | CYS138 |
| D | CYS141 |
| D | CYS170 |
| D | CYS173 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG D 500 |
| Chain | Residue |
| D | TTP300 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE TTP A 300 |
| Chain | Residue |
| A | PRO12 |
| A | MET13 |
| A | PHE14 |
| A | SER15 |
| A | GLY16 |
| A | LYS17 |
| A | SER18 |
| A | ASP82 |
| A | GLU83 |
| A | PHE86 |
| A | LEU109 |
| A | PHE113 |
| A | ILE157 |
| A | GLU158 |
| A | ILE159 |
| A | ILE160 |
| A | GLY161 |
| A | TYR166 |
| A | MG500 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE TTP B 300 |
| Chain | Residue |
| B | MET13 |
| B | PHE14 |
| B | SER15 |
| B | GLY16 |
| B | LYS17 |
| B | SER18 |
| B | ASN42 |
| B | ASP82 |
| B | GLU83 |
| B | PHE86 |
| B | THR112 |
| B | PHE113 |
| B | PHE118 |
| B | ILE157 |
| B | GLU158 |
| B | ILE159 |
| B | ILE160 |
| B | GLY161 |
| B | TYR166 |
| B | MG500 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE TTP C 300 |
| Chain | Residue |
| C | PRO12 |
| C | MET13 |
| C | PHE14 |
| C | SER15 |
| C | GLY16 |
| C | LYS17 |
| C | SER18 |
| C | ASP82 |
| C | GLU83 |
| C | PHE86 |
| C | LEU109 |
| C | PHE113 |
| C | ARG150 |
| C | ILE157 |
| C | GLU158 |
| C | ILE159 |
| C | ILE160 |
| C | GLY161 |
| C | TYR166 |
| C | MG500 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TTP D 300 |
| Chain | Residue |
| D | ILE159 |
| D | ILE160 |
| D | GLY161 |
| D | TYR166 |
| D | MG500 |
| D | PRO12 |
| D | MET13 |
| D | PHE14 |
| D | SER15 |
| D | GLY16 |
| D | LYS17 |
| D | SER18 |
| D | ASP82 |
| D | GLU83 |
| D | PHE86 |
| D | LEU109 |
| D | THR112 |
| D | PHE113 |
| D | PHE118 |
| D | ILE157 |
| D | GLU158 |
Functional Information from PROSITE/UniProt
| site_id | PS00603 |
| Number of Residues | 14 |
| Details | TK_CELLULAR_TYPE Thymidine kinase cellular-type signature. GgnDmYqSvCRkCY |
| Chain | Residue | Details |
| A | GLY161-TYR174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:17062140, ECO:0007744|PDB:2J87 |
| Chain | Residue | Details |
| A | GLU83 | |
| B | GLU83 | |
| C | GLU83 | |
| D | GLU83 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17062140, ECO:0007744|PDB:2J87 |
| Chain | Residue | Details |
| A | GLY11 | |
| B | CYS138 | |
| B | CYS141 | |
| B | ILE157 | |
| B | CYS170 | |
| B | CYS173 | |
| C | GLY11 | |
| C | PHE113 | |
| C | CYS138 | |
| C | CYS141 | |
| C | ILE157 | |
| A | PHE113 | |
| C | CYS170 | |
| C | CYS173 | |
| D | GLY11 | |
| D | PHE113 | |
| D | CYS138 | |
| D | CYS141 | |
| D | ILE157 | |
| D | CYS170 | |
| D | CYS173 | |
| A | CYS138 | |
| A | CYS141 | |
| A | ILE157 | |
| A | CYS170 | |
| A | CYS173 | |
| B | GLY11 | |
| B | PHE113 |
