6ENG
Crystal structure of the 43K ATPase domain of Escherichia coli gyrase B in complex with an aminocoumarin
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 | 3 |
| Details | binding site for residue PO4 A 401 |
| Chain | Residue |
| A | ARG192 |
| A | TYR228 |
| A | LYS231 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 402 |
| Chain | Residue |
| A | HIS64 |
| A | ARG168 |
| A | LYS208 |
| A | HOH514 |
| A | HOH531 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue PG4 A 403 |
| Chain | Residue |
| A | ASN265 |
| A | ILE266 |
| A | TYR267 |
| A | CYS268 |
| A | ARG276 |
| A | LEU282 |
| A | HOH557 |
| A | GLU264 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 404 |
| Chain | Residue |
| A | ARG204 |
| A | HIS215 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 405 |
| Chain | Residue |
| A | ILE273 |
| A | PRO274 |
| A | THR336 |
| A | LYS337 |
| A | ASP338 |
| A | HOH695 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue K A 406 |
| Chain | Residue |
| A | GLY102 |
| A | LYS103 |
| A | ASP105 |
| A | HOH543 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue K A 407 |
| Chain | Residue |
| A | ASN271 |
| A | ILE273 |
| A | HOH589 |
| A | HOH599 |
| A | HOH621 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue K A 408 |
| Chain | Residue |
| A | TYR242 |
| A | HOH640 |
| A | HOH682 |
| A | HOH689 |
| site_id | AC9 |
| Number of Residues | 33 |
| Details | binding site for residue BHW B 401 |
| Chain | Residue |
| A | ASN46 |
| A | GLU50 |
| A | VAL71 |
| A | ASP73 |
| A | ARG76 |
| A | GLY77 |
| A | ILE78 |
| A | ILE94 |
| A | GLY101 |
| A | PHE104 |
| A | ASP105 |
| A | LYS110 |
| A | VAL120 |
| A | ARG136 |
| B | VAL43 |
| B | ASN46 |
| B | GLU50 |
| B | VAL71 |
| B | ASP73 |
| B | ARG76 |
| B | GLY77 |
| B | ILE78 |
| B | ILE94 |
| B | GLY101 |
| B | PHE104 |
| B | ASP105 |
| B | LYS110 |
| B | VAL120 |
| B | ARG136 |
| B | THR165 |
| B | HOH524 |
| B | HOH557 |
| B | HOH608 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 B 402 |
| Chain | Residue |
| B | ARG192 |
| B | TYR228 |
| B | LYS231 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 B 403 |
| Chain | Residue |
| B | HIS64 |
| B | ARG168 |
| B | LYS208 |
| B | HOH506 |
| B | HOH548 |
| B | HOH560 |
| B | HOH603 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 B 404 |
| Chain | Residue |
| B | LYS223 |
| B | TYR242 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 405 |
| Chain | Residue |
| B | ARG204 |
| B | HIS215 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| 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_FI2 |
| 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_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25849408","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"9657678","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 171 |
| Details | Region: {"description":"Transducer domain","evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1646964","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
