2GXA
Crystal structure of papillomavirus E1 hexameric helicase with ssDNA and MgADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003678 | molecular_function | DNA helicase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006260 | biological_process | DNA replication |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003678 | molecular_function | DNA helicase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006260 | biological_process | DNA replication |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003678 | molecular_function | DNA helicase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006260 | biological_process | DNA replication |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003678 | molecular_function | DNA helicase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006260 | biological_process | DNA replication |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003678 | molecular_function | DNA helicase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006260 | biological_process | DNA replication |
| F | 0003677 | molecular_function | DNA binding |
| F | 0003678 | molecular_function | DNA helicase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006260 | biological_process | DNA replication |
| G | 0003677 | molecular_function | DNA binding |
| G | 0003678 | molecular_function | DNA helicase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006260 | biological_process | DNA replication |
| H | 0003677 | molecular_function | DNA binding |
| H | 0003678 | molecular_function | DNA helicase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0006260 | biological_process | DNA replication |
| I | 0003677 | molecular_function | DNA binding |
| I | 0003678 | molecular_function | DNA helicase activity |
| I | 0005524 | molecular_function | ATP binding |
| I | 0006260 | biological_process | DNA replication |
| J | 0003677 | molecular_function | DNA binding |
| J | 0003678 | molecular_function | DNA helicase activity |
| J | 0005524 | molecular_function | ATP binding |
| J | 0006260 | biological_process | DNA replication |
| K | 0003677 | molecular_function | DNA binding |
| K | 0003678 | molecular_function | DNA helicase activity |
| K | 0005524 | molecular_function | ATP binding |
| K | 0006260 | biological_process | DNA replication |
| L | 0003677 | molecular_function | DNA binding |
| L | 0003678 | molecular_function | DNA helicase activity |
| L | 0005524 | molecular_function | ATP binding |
| L | 0006260 | biological_process | DNA replication |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 21 |
| Chain | Residue |
| A | ADP1 |
| A | SER440 |
| A | ASP479 |
| A | HOH578 |
| A | HOH579 |
| B | HOH3 |
| B | ARG538 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 22 |
| Chain | Residue |
| B | HOH6 |
| B | SER440 |
| B | ASP479 |
| C | HOH5 |
| C | ARG538 |
| B | ADP2 |
| B | HOH4 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG C 23 |
| Chain | Residue |
| C | ADP3 |
| C | HOH7 |
| C | HOH8 |
| C | SER440 |
| C | ASP479 |
| D | HOH9 |
| D | ARG538 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 24 |
| Chain | Residue |
| D | ADP4 |
| D | SER440 |
| D | ASP479 |
| E | TYR534 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG E 25 |
| Chain | Residue |
| E | ADP5 |
| E | SER440 |
| E | ASP479 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG G 27 |
| Chain | Residue |
| G | ADP7 |
| G | HOH10 |
| G | HOH11 |
| G | HOH12 |
| G | SER440 |
| G | ASP479 |
| H | ARG538 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG H 28 |
| Chain | Residue |
| H | ADP8 |
| H | HOH13 |
| H | HOH14 |
| H | CL48 |
| H | SER440 |
| H | ASP479 |
| I | HOH15 |
| I | ARG538 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG I 29 |
| Chain | Residue |
| I | SER440 |
| I | ASP479 |
| J | ADP9 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG J 30 |
| Chain | Residue |
| J | SER440 |
| J | ASP479 |
| K | ADP10 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG K 31 |
| Chain | Residue |
| K | SER440 |
| K | ASP479 |
| L | ADP11 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 41 |
| Chain | Residue |
| A | ADP1 |
| A | LYS439 |
| B | ARG538 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 42 |
| Chain | Residue |
| B | ADP2 |
| B | LYS439 |
| B | ASN523 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL H 48 |
| Chain | Residue |
| H | ADP8 |
| H | MG28 |
| H | PRO435 |
| H | LYS439 |
| H | ASP479 |
| H | ASN523 |
| site_id | BC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP A 1 |
| Chain | Residue |
| A | MG21 |
| A | CL41 |
| A | ASN436 |
| A | THR437 |
| A | GLY438 |
| A | LYS439 |
| A | SER440 |
| A | MET441 |
| A | ASN558 |
| A | HOH578 |
| A | HOH579 |
| B | ILE423 |
| B | PRO424 |
| B | LYS425 |
| B | LYS426 |
| B | TYR499 |
| site_id | BC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP B 2 |
| Chain | Residue |
| B | HOH4 |
| B | MG22 |
| B | CL42 |
| B | ASN436 |
| B | THR437 |
| B | GLY438 |
| B | LYS439 |
| B | SER440 |
| B | MET441 |
| B | ASN558 |
| C | HOH5 |
| C | PRO424 |
| C | LYS425 |
| C | LYS426 |
| C | TYR499 |
| site_id | BC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP C 3 |
| Chain | Residue |
| C | THR437 |
| C | GLY438 |
| C | LYS439 |
| C | SER440 |
| C | MET441 |
| C | THR549 |
| C | ASN558 |
| D | PRO424 |
| D | LYS425 |
| D | TYR499 |
| C | HOH7 |
| C | HOH8 |
| C | MG23 |
| C | ASN436 |
| site_id | BC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP D 4 |
| Chain | Residue |
| D | MG24 |
| D | ASN436 |
| D | THR437 |
| D | GLY438 |
| D | LYS439 |
| D | SER440 |
| D | THR549 |
| D | GLN555 |
| E | TYR499 |
| E | TYR534 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ADP E 5 |
| Chain | Residue |
| E | MG25 |
| E | ASN436 |
| E | THR437 |
| E | GLY438 |
| E | LYS439 |
| E | SER440 |
| E | MET441 |
| F | TYR499 |
| site_id | CC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP F 6 |
| Chain | Residue |
| F | PRO435 |
| F | ASN436 |
| F | THR437 |
| F | GLY438 |
| F | LYS439 |
| F | SER440 |
| F | MET441 |
| F | ASP479 |
| F | ASN523 |
| F | CYS548 |
| F | PHE557 |
| site_id | CC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP G 7 |
| Chain | Residue |
| G | HOH10 |
| G | HOH11 |
| G | MG27 |
| G | ASN436 |
| G | THR437 |
| G | GLY438 |
| G | LYS439 |
| G | SER440 |
| G | MET441 |
| G | ASN558 |
| H | LYS425 |
| H | TYR499 |
| site_id | CC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP H 8 |
| Chain | Residue |
| H | HOH14 |
| H | MG28 |
| H | CL48 |
| H | ASN436 |
| H | THR437 |
| H | GLY438 |
| H | LYS439 |
| H | SER440 |
| H | MET441 |
| H | ASN558 |
| I | PRO424 |
| I | LYS425 |
| I | TYR499 |
| site_id | CC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ADP J 9 |
| Chain | Residue |
| I | MG29 |
| I | ASN436 |
| I | THR437 |
| I | GLY438 |
| I | LYS439 |
| I | SER440 |
| I | MET441 |
| I | GLN555 |
| J | TYR499 |
| site_id | CC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP K 10 |
| Chain | Residue |
| J | MG30 |
| J | ASN436 |
| J | THR437 |
| J | GLY438 |
| J | LYS439 |
| J | SER440 |
| J | MET441 |
| J | CYS548 |
| J | ASP550 |
| K | ASP497 |
| K | TYR499 |
| site_id | CC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP L 11 |
| Chain | Residue |
| K | MG31 |
| K | PRO435 |
| K | ASN436 |
| K | THR437 |
| K | GLY438 |
| K | LYS439 |
| K | SER440 |
| K | ASP479 |
| L | ASP489 |
| L | THR490 |
| L | ARG493 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1800 |
| Details | Domain: {"description":"SF3 helicase","evidences":[{"source":"HAMAP-Rule","id":"MF_04000","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 84 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04000","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"HAMAP-Rule","id":"MF_04000","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11005821","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






