6N9U
Structure of bacteriophage T7 lagging-strand DNA polymerase (D5A/E7A) interacting with primase domains of two gp4 subunits bound to an RNA/DNA hybrid and dTTP (from LagS1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003678 | molecular_function | DNA helicase activity |
| E | 0003697 | molecular_function | single-stranded DNA binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| E | 0004386 | molecular_function | helicase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006260 | biological_process | DNA replication |
| E | 0006269 | biological_process | DNA replication, synthesis of primer |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016779 | molecular_function | nucleotidyltransferase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0039693 | biological_process | viral DNA genome replication |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0043139 | molecular_function | 5'-3' DNA helicase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003677 | molecular_function | DNA binding |
| F | 0003678 | molecular_function | DNA helicase activity |
| F | 0003697 | molecular_function | single-stranded DNA binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| F | 0004386 | molecular_function | helicase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006260 | biological_process | DNA replication |
| F | 0006269 | biological_process | DNA replication, synthesis of primer |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0016740 | molecular_function | transferase activity |
| F | 0016779 | molecular_function | nucleotidyltransferase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0039693 | biological_process | viral DNA genome replication |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0043139 | molecular_function | 5'-3' DNA helicase activity |
| F | 0046872 | molecular_function | metal ion binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0003676 | molecular_function | nucleic acid binding |
| H | 0003677 | molecular_function | DNA binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
| H | 0004518 | molecular_function | nuclease activity |
| H | 0004527 | molecular_function | exonuclease activity |
| H | 0004529 | molecular_function | DNA exonuclease activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0006259 | biological_process | DNA metabolic process |
| H | 0006260 | biological_process | DNA replication |
| H | 0006261 | biological_process | DNA-templated DNA replication |
| H | 0006302 | biological_process | double-strand break repair |
| H | 0008408 | molecular_function | 3'-5' exonuclease activity |
| H | 0016740 | molecular_function | transferase activity |
| H | 0016779 | molecular_function | nucleotidyltransferase activity |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0034061 | molecular_function | DNA polymerase activity |
| H | 0039693 | biological_process | viral DNA genome replication |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0090592 | biological_process | DNA synthesis involved in DNA replication |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN E 601 |
| Chain | Residue |
| E | CYS17 |
| E | CYS20 |
| E | CYS36 |
| E | CYS39 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue TTP H 801 |
| Chain | Residue |
| H | HIS506 |
| H | ARG518 |
| H | LYS522 |
| H | TYR526 |
| H | ASP654 |
| H | MG802 |
| P | DOC6 |
| T | DA2004 |
| T | DG2005 |
| H | ASP475 |
| H | ALA476 |
| H | GLY478 |
| H | LEU479 |
| H | GLU480 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG H 802 |
| Chain | Residue |
| H | ASP475 |
| H | ALA476 |
| H | ASP654 |
| H | TTP801 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue MG H 803 |
| Chain | Residue |
| H | HIS59 |
Functional Information from PROSITE/UniProt
| site_id | PS00447 |
| Number of Residues | 20 |
| Details | DNA_POLYMERASE_A DNA polymerase family A signature. RdnAKtfiYGflYgaGdekI |
| Chain | Residue | Details |
| H | ARG518-ILE537 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Zinc finger: {"description":"C4-like; zinc ribbon fold","evidences":[{"source":"HAMAP-Rule","id":"MF_04154","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10200256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12769857","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2829184","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04154","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12769857","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04154","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12769857","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 87 |
| Details | Domain: {"description":"Toprim","evidences":[{"source":"PROSITE-ProRule","id":"PRU00995","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| 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_FI6 |
| Number of Residues | 3 |
| 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_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9914251","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |






