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 | 6 |
| Details | binding site for residue MPD A 301 |
| Chain | Residue |
| A | ASP81 |
| A | LYS170 |
| A | THR171 |
| A | MPD302 |
| A | HOH409 |
| A | HOH483 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MPD A 302 |
| Chain | Residue |
| A | TYR141 |
| A | HIS143 |
| A | MPD301 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue 57W A 303 |
| Chain | Residue |
| A | ASN54 |
| A | SER55 |
| A | GLU58 |
| A | VAL79 |
| A | ASP81 |
| A | ARG84 |
| A | GLY85 |
| A | ILE86 |
| A | PRO87 |
| A | ILE102 |
| A | ARG144 |
| A | THR173 |
| A | HOH422 |
| A | HOH450 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 304 |
| Chain | Residue |
| A | GLU50 |
| A | HOH416 |
| A | HOH477 |
| A | HOH487 |
| A | HOH532 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MPD B 301 |
| Chain | Residue |
| B | THR80 |
| B | ASP81 |
| B | HIS143 |
| B | LYS170 |
| B | THR171 |
| B | GLY172 |
| B | MPD302 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MPD B 302 |
| Chain | Residue |
| B | TYR141 |
| B | HIS143 |
| B | GLU186 |
| B | MPD301 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | binding site for residue 57W B 303 |
| Chain | Residue |
| A | THR185 |
| B | ASN54 |
| B | SER55 |
| B | GLU58 |
| B | VAL79 |
| B | ASP81 |
| B | ARG84 |
| B | GLY85 |
| B | ILE86 |
| B | PRO87 |
| B | ILE102 |
| B | ARG144 |
| B | THR173 |
| B | HOH458 |
| B | HOH493 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 304 |
| Chain | Residue |
| B | ASP53 |
| B | ASP57 |
| B | HOH406 |
| B | HOH426 |
| B | HOH447 |
| B | HOH501 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 305 |
| Chain | Residue |
| B | GLU164 |
| B | GLU219 |
| B | HOH512 |
| B | HOH531 |
| B | HOH538 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 306 |
| Chain | Residue |
| A | HOH419 |
| A | HOH521 |
| B | LEU60 |
| B | HOH503 |
| B | HOH505 |
| B | HOH565 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 307 |
| Chain | Residue |
| B | ASN54 |
| B | MG310 |
| B | HOH421 |
| B | HOH429 |
| B | HOH506 |
| B | HOH542 |
| B | HOH562 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 308 |
| Chain | Residue |
| B | ASN82 |
| B | GLY83 |
| B | THR171 |
| B | HOH479 |
| B | HOH504 |
| B | HOH514 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 309 |
| Chain | Residue |
| B | GLY208 |
| B | HIS228 |
| B | HOH478 |
| B | HOH519 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 310 |
| Chain | Residue |
| B | ASP53 |
| B | MG307 |
| B | HOH406 |
| B | HOH421 |
| B | HOH429 |
| B | HOH432 |
| B | HOH562 |
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 | |
