Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006260 | biological_process | DNA replication |
| B | 0003677 | molecular_function | DNA binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006260 | biological_process | DNA replication |
| C | 0003677 | molecular_function | DNA binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006260 | biological_process | DNA replication |
| D | 0003677 | molecular_function | DNA binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006260 | biological_process | DNA replication |
| E | 0003677 | molecular_function | DNA binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006260 | biological_process | DNA replication |
| F | 0003677 | molecular_function | DNA binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006260 | biological_process | DNA replication |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 700 |
| Chain | Residue |
| A | CYS302 |
| A | CYS305 |
| A | HIS313 |
| A | HIS317 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 700 |
| Chain | Residue |
| B | CYS302 |
| B | CYS305 |
| B | HIS313 |
| B | HIS317 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 700 |
| Chain | Residue |
| C | CYS305 |
| C | HIS313 |
| C | HIS317 |
| C | CYS302 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 700 |
| Chain | Residue |
| D | CYS302 |
| D | CYS305 |
| D | HIS313 |
| D | HIS317 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 700 |
| Chain | Residue |
| E | CYS302 |
| E | CYS305 |
| E | HIS313 |
| E | HIS317 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 700 |
| Chain | Residue |
| F | CYS302 |
| F | CYS305 |
| F | HIS313 |
| F | HIS317 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 750 |
| Chain | Residue |
| A | THR433 |
| A | GLU473 |
| A | ATP800 |
| A | HOH802 |
| A | HOH935 |
| A | HOH936 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 750 |
| Chain | Residue |
| B | THR433 |
| B | ATP800 |
| B | HOH937 |
| B | HOH938 |
| B | HOH939 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 750 |
| Chain | Residue |
| C | THR433 |
| C | ATP800 |
| C | HOH803 |
| C | HOH811 |
| C | HOH926 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 750 |
| Chain | Residue |
| D | THR433 |
| D | ATP800 |
| D | HOH801 |
| D | HOH921 |
| D | HOH922 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG E 750 |
| Chain | Residue |
| D | HOH823 |
| E | THR433 |
| E | GLU473 |
| E | ASP474 |
| E | ATP800 |
| E | HOH957 |
| E | HOH958 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 750 |
| Chain | Residue |
| F | THR433 |
| F | ATP800 |
| F | HOH805 |
| F | HOH808 |
| F | HOH922 |
| site_id | BC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ATP A 800 |
| Chain | Residue |
| A | LEU397 |
| A | ILE428 |
| A | ASP429 |
| A | SER430 |
| A | GLY431 |
| A | LYS432 |
| A | THR433 |
| A | THR434 |
| A | ASP474 |
| A | ASN529 |
| A | ARG548 |
| A | PRO549 |
| A | LYS550 |
| A | LEU553 |
| A | LEU557 |
| A | LEU564 |
| A | MG750 |
| A | HOH802 |
| A | HOH910 |
| A | HOH935 |
| A | HOH936 |
| F | LYS418 |
| F | ARG540 |
| F | HOH846 |
| F | HOH921 |
| site_id | BC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ATP B 800 |
| Chain | Residue |
| B | LEU557 |
| B | LEU564 |
| B | MG750 |
| B | HOH804 |
| B | HOH813 |
| B | HOH893 |
| B | HOH937 |
| B | HOH938 |
| B | HOH939 |
| B | HOH940 |
| A | LYS418 |
| A | ARG540 |
| A | HOH837 |
| B | LEU397 |
| B | ILE428 |
| B | ASP429 |
| B | SER430 |
| B | GLY431 |
| B | LYS432 |
| B | THR433 |
| B | THR434 |
| B | ASP474 |
| B | ASN529 |
| B | ARG548 |
| B | PRO549 |
| B | LYS550 |
| B | LEU553 |
| site_id | BC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ATP C 800 |
| Chain | Residue |
| B | LYS418 |
| B | ARG540 |
| B | HOH827 |
| C | LEU397 |
| C | ILE428 |
| C | ASP429 |
| C | SER430 |
| C | GLY431 |
| C | LYS432 |
| C | THR433 |
| C | THR434 |
| C | ASP474 |
| C | ASN529 |
| C | ARG548 |
| C | PRO549 |
| C | LYS550 |
| C | LEU553 |
| C | LEU557 |
| C | LEU564 |
| C | MG750 |
| C | HOH803 |
| C | HOH811 |
| C | HOH822 |
| C | HOH860 |
| C | HOH862 |
| C | HOH925 |
| site_id | BC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ATP D 800 |
| Chain | Residue |
| C | LYS418 |
| C | ARG540 |
| C | HOH812 |
| C | HOH927 |
| D | LEU397 |
| D | ILE428 |
| D | ASP429 |
| D | SER430 |
| D | GLY431 |
| D | LYS432 |
| D | THR433 |
| D | THR434 |
| D | ASP474 |
| D | ASN529 |
| D | ARG548 |
| D | PRO549 |
| D | LYS550 |
| D | LEU553 |
| D | LEU557 |
| D | LEU564 |
| D | MG750 |
| D | HOH801 |
| D | HOH831 |
| D | HOH843 |
| D | HOH921 |
| site_id | BC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ATP E 800 |
| Chain | Residue |
| D | LYS418 |
| D | ARG540 |
| D | HOH823 |
| D | HOH923 |
| E | LEU397 |
| E | ILE428 |
| E | ASP429 |
| E | SER430 |
| E | GLY431 |
| E | LYS432 |
| E | THR433 |
| E | THR434 |
| E | ASP474 |
| E | ASN529 |
| E | ARG548 |
| E | PRO549 |
| E | LYS550 |
| E | LEU553 |
| E | LEU557 |
| E | LEU564 |
| E | MG750 |
| E | HOH886 |
| E | HOH916 |
| E | HOH950 |
| E | HOH958 |
| E | HOH959 |
| site_id | BC9 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ATP F 800 |
| Chain | Residue |
| E | LYS418 |
| E | ARG540 |
| E | HOH849 |
| E | HOH866 |
| E | HOH868 |
| F | LEU397 |
| F | ILE428 |
| F | ASP429 |
| F | SER430 |
| F | GLY431 |
| F | LYS432 |
| F | THR433 |
| F | THR434 |
| F | ASP474 |
| F | ASN529 |
| F | ARG548 |
| F | PRO549 |
| F | LYS550 |
| F | LEU553 |
| F | LEU557 |
| F | LEU564 |
| F | MG750 |
| F | HOH805 |
| F | HOH808 |
| F | HOH815 |
| F | HOH818 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 960 |
| Details | Domain: {"description":"SF3 helicase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00551","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1188 |
| Details | Region: {"description":"ATPase activity"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00671","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 42 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00551","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 184 |
| Details | Zinc finger: {"description":"T-ag D1-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00671","evidenceCode":"ECO:0000255"}]} |