Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0006259 | biological_process | DNA metabolic process |
| B | 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 | 0006259 | biological_process | DNA metabolic process |
| D | 0006265 | biological_process | DNA topological change |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue 31N F 101 |
| Chain | Residue |
| B | ALA1068 |
| F | DC11 |
| F | HOH204 |
| B | GLY1072 |
| B | ASP1083 |
| B | MET1121 |
| D | ALA1068 |
| D | ASP1083 |
| E | DG10 |
| E | DC11 |
| F | DG10 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 1501 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 1502 |
| Chain | Residue |
| B | GLU435 |
| B | ASP508 |
| B | HOH1625 |
| B | HOH1626 |
| E | DG8 |
| E | DG9 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 1501 |
| Chain | Residue |
| B | ARG1429 |
| D | ARG1429 |
| D | ARG1432 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 1502 |
| Chain | Residue |
| D | ARG1256 |
| D | THR1290 |
| D | ARG1309 |
| D | LYS1310 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MN D 1503 |
| Chain | Residue |
| D | GLU435 |
| D | ASP508 |
| D | HOH1619 |
| D | HOH1620 |
| F | DG8 |
| F | DG9 |
Functional Information from PROSITE/UniProt
| site_id | PS00177 |
| Number of Residues | 9 |
| Details | TOPOISOMERASE_II DNA topoisomerase II signature. LVEGDSAGG |
| Chain | Residue | Details |
| B | LEU433-GLY441 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| B | GLU435 | |
| B | ASP508 | |
| B | ASP510 | |
| D | GLU435 | |
| D | ASP508 | |
| D | ASP510 | |
| Chain | Residue | Details |
| B | LYS460 | |
| B | ASN463 | |
| D | LYS460 | |
| D | ASN463 | |
| Chain | Residue | Details |
| B | PHE1123 | |
| D | PHE1123 | |
