2ORV
human Thymidine Kinase 1 in complex with TP4A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004797 | molecular_function | thymidine kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009157 | biological_process | deoxyribonucleoside monophosphate biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046104 | biological_process | thymidine metabolic process |
| A | 0046105 | biological_process | thymidine biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0071897 | biological_process | DNA biosynthetic process |
| A | 1904860 | biological_process | DNA synthesis involved in mitotic DNA replication |
| B | 0004797 | molecular_function | thymidine kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009157 | biological_process | deoxyribonucleoside monophosphate biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046104 | biological_process | thymidine metabolic process |
| B | 0046105 | biological_process | thymidine biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0071897 | biological_process | DNA biosynthetic process |
| B | 1904860 | biological_process | DNA synthesis involved in mitotic DNA replication |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 235 |
| Chain | Residue |
| A | CYS153 |
| A | CYS156 |
| A | CYS185 |
| A | CYS188 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 235 |
| Chain | Residue |
| B | CYS153 |
| B | CYS156 |
| B | CYS185 |
| B | CYS188 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE 4TA A 801 |
| Chain | Residue |
| A | PHE29 |
| A | SER30 |
| A | GLY31 |
| A | LYS32 |
| A | SER33 |
| A | ASP58 |
| A | ARG60 |
| A | ASP97 |
| A | GLU98 |
| A | GLN100 |
| A | PHE101 |
| A | LEU124 |
| A | THR127 |
| A | PHE128 |
| A | PHE133 |
| A | VAL172 |
| A | GLU173 |
| A | VAL174 |
| A | ILE175 |
| A | GLY176 |
| A | TYR181 |
| A | HOH806 |
| A | HOH810 |
| A | HOH823 |
| A | HOH831 |
| A | HOH846 |
| A | HOH863 |
| A | HOH868 |
| A | HOH880 |
| A | MET28 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE 4TA B 802 |
| Chain | Residue |
| B | MET28 |
| B | PHE29 |
| B | SER30 |
| B | GLY31 |
| B | LYS32 |
| B | SER33 |
| B | ASP58 |
| B | ASP97 |
| B | GLU98 |
| B | GLN100 |
| B | PHE101 |
| B | LEU124 |
| B | THR127 |
| B | PHE128 |
| B | PHE133 |
| B | THR163 |
| B | ARG165 |
| B | VAL172 |
| B | GLU173 |
| B | VAL174 |
| B | ILE175 |
| B | GLY176 |
| B | TYR181 |
| B | HOH808 |
| B | HOH821 |
| B | HOH834 |
| B | HOH872 |
Functional Information from PROSITE/UniProt
| site_id | PS00603 |
| Number of Residues | 14 |
| Details | TK_CELLULAR_TYPE Thymidine kinase cellular-type signature. GgaDkYhSvCRlCY |
| Chain | Residue | Details |
| A | GLY176-TYR189 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255 |
| Chain | Residue | Details |
| A | GLU98 | |
| B | GLU98 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15611477, ECO:0000269|PubMed:15733844, ECO:0000269|PubMed:17407781, ECO:0000269|PubMed:22385435, ECO:0007744|PDB:1W4R, ECO:0007744|PDB:1XBT, ECO:0007744|PDB:2ORV, ECO:0007744|PDB:2WVJ |
| Chain | Residue | Details |
| A | GLY26 | |
| B | CYS156 | |
| B | CYS185 | |
| B | CYS188 | |
| A | PHE128 | |
| A | CYS153 | |
| A | CYS156 | |
| A | CYS185 | |
| A | CYS188 | |
| B | GLY26 | |
| B | PHE128 | |
| B | CYS153 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15611477, ECO:0000269|PubMed:15733844, ECO:0000269|PubMed:22385435, ECO:0007744|PDB:1W4R, ECO:0007744|PDB:1XBT, ECO:0007744|PDB:2WVJ |
| Chain | Residue | Details |
| A | ASP58 | |
| A | VAL172 | |
| B | ASP58 | |
| B | VAL172 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15733844, ECO:0000269|PubMed:22385435, ECO:0007744|PDB:1W4R, ECO:0007744|PDB:2WVJ |
| Chain | Residue | Details |
| A | ASP97 | |
| B | ASP97 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15611477, ECO:0000269|PubMed:15733844, ECO:0000269|PubMed:17407781, ECO:0000269|PubMed:22385435, ECO:0007744|PDB:1W4R, ECO:0007744|PDB:1XBT, ECO:0007744|PDB:2ORV |
| Chain | Residue | Details |
| A | TYR181 | |
| B | TYR181 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:14697231, ECO:0000269|PubMed:9575153, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER13 | |
| B | SER13 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| A | SER231 | |
| B | SER231 |
