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 | 8 |
| Details | binding site for residue 55D A 301 |
| Chain | Residue |
| A | ASN54 |
| A | GLU58 |
| A | ASP81 |
| A | ARG84 |
| A | ILE86 |
| A | HOH412 |
| A | HOH431 |
| A | HOH473 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | HOH406 |
| A | HOH426 |
| A | HOH443 |
| A | HOH450 |
| A | HOH466 |
| A | GLU50 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 303 |
| Chain | Residue |
| A | VAL88 |
| A | ARG144 |
| A | ASN145 |
| A | HOH499 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MPD A 304 |
| Chain | Residue |
| A | THR80 |
| A | ASP81 |
| A | ASN82 |
| A | HIS143 |
| A | THR171 |
| A | HOH462 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MPD A 305 |
| Chain | Residue |
| A | GLY24 |
| A | VAL28 |
| A | TYR35 |
| A | SER128 |
| A | LEU205 |
| A | LYS207 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue 55D B 301 |
| Chain | Residue |
| B | ASN54 |
| B | GLU58 |
| B | ASP81 |
| B | ARG84 |
| B | GLY85 |
| B | ILE86 |
| B | PRO87 |
| B | HOH421 |
| B | HOH492 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | GLU164 |
| B | GLU219 |
| B | HOH411 |
| B | HOH441 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 303 |
| Chain | Residue |
| B | LYS163 |
| B | TYR192 |
| B | GLU193 |
| B | ARG217 |
| B | HOH483 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 304 |
| Chain | Residue |
| B | ASP81 |
| B | LYS170 |
| B | MPD305 |
| B | MPD306 |
| B | HOH513 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MPD B 305 |
| Chain | Residue |
| B | HIS143 |
| B | GLU186 |
| B | THR187 |
| B | MPD304 |
| B | HOH439 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue MPD B 306 |
| Chain | Residue |
| B | GLN66 |
| B | GLU68 |
| B | MPD304 |
Functional Information from PROSITE/UniProt
| site_id | PS00154 |
| Number of Residues | 7 |
| Details | ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTVI |
| Chain | Residue | Details |
| A | ASP169-ILE175 | |
