Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
| A | 0006281 | biological_process | DNA repair |
| A | 0006303 | biological_process | double-strand break repair via nonhomologous end joining |
| A | 0006974 | biological_process | DNA damage response |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0034061 | molecular_function | DNA polymerase activity |
| A | 0044423 | cellular_component | virion component |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071897 | biological_process | DNA biosynthetic process |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
| B | 0006281 | biological_process | DNA repair |
| B | 0006303 | biological_process | double-strand break repair via nonhomologous end joining |
| B | 0006974 | biological_process | DNA damage response |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0034061 | molecular_function | DNA polymerase activity |
| B | 0044423 | cellular_component | virion component |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071897 | biological_process | DNA biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue DGT A 201 |
| Chain | Residue |
| A | GLY38 |
| A | VAL120 |
| A | MN202 |
| A | MN203 |
| A | HOH302 |
| C | DG9 |
| D | DA9 |
| A | SER39 |
| A | ARG42 |
| A | ASN48 |
| A | ASP49 |
| A | ASP51 |
| A | PHE115 |
| A | PHE116 |
| A | THR117 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MN A 202 |
| Chain | Residue |
| A | ASP49 |
| A | ASP51 |
| A | DGT201 |
| A | HOH301 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 203 |
| Chain | Residue |
| A | ASP49 |
| A | ASP51 |
| A | ASP100 |
| A | DGT201 |
| A | HOH302 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue DGT B 201 |
| Chain | Residue |
| B | GLY38 |
| B | SER39 |
| B | ARG42 |
| B | ASN48 |
| B | ASP49 |
| B | ASP51 |
| B | PHE115 |
| B | PHE116 |
| B | THR117 |
| B | VAL120 |
| B | MN202 |
| B | MN203 |
| F | DG9 |
| G | DA9 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MN B 202 |
| Chain | Residue |
| B | SER39 |
| B | ASP49 |
| B | ASP51 |
| B | DGT201 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MN B 203 |
| Chain | Residue |
| B | ASP49 |
| B | ASP51 |
| B | ASP100 |
| B | DGT201 |
Functional Information from PROSITE/UniProt
| site_id | PS00522 |
| Number of Residues | 20 |
| Details | DNA_POLYMERASE_X DNA polymerase family X signature. GSLrREekmLnDVDLLIivP |
| Chain | Residue | Details |
| A | GLY38-PRO57 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Region: {"description":"Involved in ssDNA binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11685239","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28245220","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Stabilizes dGTP in a syn conformation to overcome the Watson-Crick base pairing constraint","evidences":[{"source":"PubMed","id":"24617852","evidenceCode":"ECO:0000269"}]} |
