1EI1
DIMERIZATION OF E. COLI DNA GYRASE B PROVIDES A STRUCTURAL MECHANISM FOR ACTIVATING THE ATPASE CATALYTIC CENTER
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006265 | biological_process | DNA topological change |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006265 | biological_process | DNA topological change |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1081 |
| Chain | Residue |
| A | PRO79 |
| A | THR80 |
| A | GLY81 |
| A | ARG136 |
| B | SER405 |
| B | ASP406 |
| B | SER407 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2081 |
| Chain | Residue |
| A | HOH4050 |
| B | GLY481 |
| B | LYS704 |
| B | HOH4108 |
| A | ASP6 |
| A | SER7 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2101 |
| Chain | Residue |
| B | ARG691 |
| B | ALA695 |
| B | LYS699 |
| B | ALA758 |
| B | HOH2536 |
| B | HOH2537 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ANP A 394 |
| Chain | Residue |
| A | GLU42 |
| A | ASN46 |
| A | GLU50 |
| A | ASP73 |
| A | ILE78 |
| A | ALA100 |
| A | GLY101 |
| A | GLY102 |
| A | LYS103 |
| A | TYR109 |
| A | GLY114 |
| A | LEU115 |
| A | HIS116 |
| A | GLY117 |
| A | VAL118 |
| A | GLY119 |
| A | VAL120 |
| A | SER121 |
| A | THR165 |
| A | LYS337 |
| A | HOH1510 |
| A | HOH1560 |
| A | HOH1579 |
| A | HOH1601 |
| A | HOH1616 |
| A | GOL2031 |
| site_id | AC5 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE ANP B 794 |
| Chain | Residue |
| B | GLU442 |
| B | ASN446 |
| B | GLU450 |
| B | ASP473 |
| B | ILE478 |
| B | ILE494 |
| B | ALA500 |
| B | GLY501 |
| B | GLY502 |
| B | LYS503 |
| B | TYR509 |
| B | GLY514 |
| B | LEU515 |
| B | HIS516 |
| B | GLY517 |
| B | VAL518 |
| B | GLY519 |
| B | VAL520 |
| B | THR565 |
| B | GLN735 |
| B | LYS737 |
| B | GOL1031 |
| B | HOH2510 |
| B | HOH2529 |
| B | HOH2560 |
| B | HOH2579 |
| B | HOH2601 |
| B | HOH2616 |
| B | HOH4060 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 1031 |
| Chain | Residue |
| A | SER5 |
| A | SER9 |
| B | GLU450 |
| B | ARG476 |
| B | GLY477 |
| B | PRO479 |
| B | GLY502 |
| B | SER508 |
| B | TYR509 |
| B | ARG536 |
| B | ANP794 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL A 2031 |
| Chain | Residue |
| A | GLU50 |
| A | ARG76 |
| A | GLY77 |
| A | PRO79 |
| A | GLY102 |
| A | SER108 |
| A | TYR109 |
| A | ARG136 |
| A | ANP394 |
| B | SER405 |
| B | SER409 |
| B | ILE410 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 436 |
| Details | Region: {"description":"ATPase domain","evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1646964","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 342 |
| Details | Region: {"description":"Transducer domain","evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1646964","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor (ATPase activity)","evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8248233","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25202966","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25849408","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25202966","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25849408","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25849408","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25849408","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"9657678","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
