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 | 0005694 | cellular_component | chromosome |
| A | 0006259 | biological_process | DNA metabolic process |
| 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 | 0005694 | cellular_component | chromosome |
| B | 0006259 | biological_process | DNA metabolic process |
| B | 0006265 | biological_process | DNA topological change |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006265 | biological_process | DNA topological change |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006265 | biological_process | DNA topological change |
Functional Information from PDB Data
| site_id | 1 |
| Number of Residues | |
| Details | |
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NFX F 0 |
| Chain | Residue |
| B | GLY77 |
| B | ASP78 |
| B | SER79 |
| F | DA1 |
| H | DT4 |
| H | DA5 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NFX H 0 |
| Chain | Residue |
| F | DA5 |
| H | DG1 |
| A | SER79 |
| A | SER80 |
| F | DC4 |
Functional Information from PROSITE/UniProt
| site_id | PS00177 |
| Number of Residues | 9 |
| Details | TOPOISOMERASE_II DNA topoisomerase II signature. LVEGDSAGG |
| Chain | Residue | Details |
| C | LEU431-GLY439 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| C | GLU433 | |
| C | ASP506 | |
| C | ASP508 | |
| D | GLU433 | |
| D | ASP506 | |
| D | ASP508 | |
| Chain | Residue | Details |
| C | LYS458 | |
| B | LYS93 | |
| C | ASN461 | |
| C | HIS513 | |
| C | ARG629 | |
| D | LYS458 | |
| D | ASN461 | |
| D | HIS513 | |
| D | ARG629 | |
| B | ARG87 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | ARG117 | |
| B | ARG117 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ab4 |
| Chain | Residue | Details |
| A | TYR118 | |
| A | ARG28 | |
| A | HIS74 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ab4 |
| Chain | Residue | Details |
| B | TYR118 | |
| B | ARG28 | |
| B | HIS74 | |
