2AJQ
Structure of replicative DNA polymerase provides insigts into the mechanisms for processivity, frameshifting and editing
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 | 0006259 | biological_process | DNA metabolic process |
| A | 0006260 | biological_process | DNA replication |
| A | 0006261 | biological_process | DNA-templated DNA replication |
| A | 0006302 | biological_process | double-strand break repair |
| 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 | 0034061 | molecular_function | DNA polymerase 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 |
| 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 | 0030337 | molecular_function | DNA polymerase processivity factor activity |
| B | 0045454 | biological_process | cell redox homeostasis |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003676 | molecular_function | nucleic acid binding |
| F | 0003677 | molecular_function | DNA binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
| F | 0004518 | molecular_function | nuclease activity |
| F | 0004527 | molecular_function | exonuclease activity |
| F | 0004529 | molecular_function | DNA exonuclease activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0006259 | biological_process | DNA metabolic process |
| F | 0006260 | biological_process | DNA replication |
| F | 0006261 | biological_process | DNA-templated DNA replication |
| F | 0006302 | biological_process | double-strand break repair |
| F | 0008408 | molecular_function | 3'-5' exonuclease activity |
| F | 0016740 | molecular_function | transferase activity |
| F | 0016779 | molecular_function | nucleotidyltransferase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0034061 | molecular_function | DNA polymerase activity |
| F | 0039693 | biological_process | viral DNA genome replication |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0090592 | biological_process | DNA synthesis involved in DNA replication |
| I | 0005515 | molecular_function | protein binding |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0005829 | cellular_component | cytosol |
| I | 0015035 | molecular_function | protein-disulfide reductase activity |
| I | 0030337 | molecular_function | DNA polymerase processivity factor activity |
| I | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 372 |
| Details | Region: {"description":"3'-5'exonuclease","evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9440688","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 502 |
| Details | Region: {"description":"Polymerase","evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9440688","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 76 |
| Details | Region: {"description":"Binding to host TrxA","evidences":[{"source":"PubMed","id":"15795374","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15292168","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9440688","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9440688","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9914251","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9914251","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Deprotonates C-terminal active site Cys"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Site: {"description":"Contributes to redox potential value"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| B | PRO34 | |
| B | CYS35 | |
| B | CYS32 | |
| B | GLY33 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| I | PRO34 | |
| I | CYS35 | |
| I | CYS32 | |
| I | GLY33 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| B | CYS35 | |
| B | CYS32 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| I | CYS35 | |
| I | CYS32 |
