1T7P
T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004527 | molecular_function | exonuclease activity |
| A | 0004529 | molecular_function | DNA exonuclease activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006260 | biological_process | DNA replication |
| A | 0006261 | biological_process | DNA-templated DNA replication |
| A | 0008152 | biological_process | metabolic process |
| A | 0008408 | molecular_function | 3'-5' exonuclease activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0039693 | biological_process | viral DNA genome replication |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0090592 | biological_process | DNA synthesis involved in DNA replication |
| A | 0097681 | biological_process | double-strand break repair via alternative nonhomologous end joining |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0015035 | molecular_function | protein-disulfide reductase activity |
| B | 0015036 | molecular_function | disulfide oxidoreductase activity |
| B | 0030337 | molecular_function | DNA polymerase processivity factor activity |
| B | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 4001 |
| Chain | Residue |
| A | ASP475 |
| A | ALA476 |
| A | ASP654 |
| P | DG323 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 4002 |
| Chain | Residue |
| P | HOH3180 |
| A | ASP475 |
| A | ASP654 |
| A | HOH3195 |
| P | 2DA22 |
| P | DG323 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 4003 |
| Chain | Residue |
| A | ASP5 |
| A | HOH3532 |
| A | HOH3533 |
| A | HOH3534 |
| A | HOH3535 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE DG3 P 23 |
| Chain | Residue |
| A | ARG429 |
| A | ASP475 |
| A | ALA476 |
| A | SER477 |
| A | GLY478 |
| A | LEU479 |
| A | GLU480 |
| A | HIS506 |
| A | ARG518 |
| A | LYS522 |
| A | TYR526 |
| A | TYR530 |
| A | ASP654 |
| A | HOH3486 |
| A | MG4001 |
| A | MG4002 |
| P | 2DA22 |
| P | HOH3107 |
| P | HOH3405 |
| T | DC4 |
| T | DT5 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| B | CYS32 | |
| B | CYS35 | |
| A | ALA180 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | SITE: Deprotonates C-terminal active site Cys |
| Chain | Residue | Details |
| B | ASP26 | |
| A | ARG482 | |
| A | CYS660 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Contributes to redox potential value |
| Chain | Residue | Details |
| B | GLY33 | |
| B | PRO34 | |
| A | PHE528 | |
| A | ALA532 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| B | LYS69 |
