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 |
| 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 | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue ANP A 501 |
| Chain | Residue |
| A | GLU47 |
| A | TYR113 |
| A | GLY118 |
| A | LEU119 |
| A | HIS120 |
| A | GLY121 |
| A | VAL122 |
| A | GLY123 |
| A | SER124 |
| A | THR172 |
| A | LYS344 |
| A | ASN51 |
| A | MG502 |
| B | TYR11 |
| B | ILE16 |
| A | GLU55 |
| A | ASP78 |
| A | ILE98 |
| A | ALA104 |
| A | GLY105 |
| A | GLY106 |
| A | LYS107 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | GLU47 |
| A | ASN51 |
| A | ANP501 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue ANP B 501 |
| Chain | Residue |
| A | TYR11 |
| A | ILE16 |
| B | ASN51 |
| B | GLU55 |
| B | ASP78 |
| B | MET83 |
| B | ILE98 |
| B | ALA104 |
| B | GLY106 |
| B | LYS107 |
| B | TYR113 |
| B | GLY118 |
| B | LEU119 |
| B | HIS120 |
| B | GLY121 |
| B | VAL122 |
| B | GLY123 |
| B | SER124 |
| B | THR172 |
| B | LYS344 |
| B | MG502 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | ASN51 |
| B | ANP501 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | binding site for residue ANP C 501 |
| Chain | Residue |
| C | GLU47 |
| C | ASN51 |
| C | GLU55 |
| C | ASP78 |
| C | MET83 |
| C | ILE98 |
| C | ALA104 |
| C | GLY105 |
| C | GLY106 |
| C | LYS107 |
| C | TYR113 |
| C | GLY118 |
| C | LEU119 |
| C | HIS120 |
| C | GLY121 |
| C | VAL122 |
| C | GLY123 |
| C | SER124 |
| C | SER125 |
| C | LYS344 |
| C | MG502 |
| D | TYR11 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue MG C 502 |
| Chain | Residue |
| C | GLU47 |
| C | ASN51 |
| C | ANP501 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | binding site for residue ANP D 501 |
| Chain | Residue |
| C | TYR11 |
| D | GLU47 |
| D | ASN51 |
| D | GLU55 |
| D | ASP78 |
| D | MET83 |
| D | ILE98 |
| D | GLY105 |
| D | GLY106 |
| D | LYS107 |
| D | TYR113 |
| D | GLY118 |
| D | LEU119 |
| D | HIS120 |
| D | GLY121 |
| D | VAL122 |
| D | GLY123 |
| D | SER124 |
| D | THR172 |
| D | MG502 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue MG D 502 |
| Chain | Residue |
| D | ASN51 |
| D | ANP501 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ANP F 101 |
| Chain | Residue |
| F | DT4 |
| B | ASP269 |
| E | DA11 |
| E | DT12 |
| F | DA3 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | TYR11 | |
| B | LYS344 | |
| C | TYR11 | |
| C | ASN51 | |
| C | ASP78 | |
| C | GLY118 | |
| C | LYS344 | |
| D | TYR11 | |
| D | ASN51 | |
| D | ASP78 | |
| D | GLY118 | |
| A | ASN51 | |
| D | LYS344 | |
| A | ASP78 | |
| A | GLY118 | |
| A | LYS344 | |
| B | TYR11 | |
| B | ASN51 | |
| B | ASP78 | |
| B | GLY118 | |
