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 MG A 301 |
| Chain | Residue |
| A | ASP53 |
| A | ASN54 |
| A | ASP57 |
| A | MG302 |
| A | HOH409 |
| A | HOH470 |
| A | HOH503 |
| A | HOH521 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | MG301 |
| A | HOH449 |
| A | HOH470 |
| A | HOH503 |
| A | HOH521 |
| A | GLU50 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 303 |
| Chain | Residue |
| A | ASP57 |
| A | ASP57 |
| A | HOH409 |
| A | HOH409 |
| A | HOH524 |
| A | HOH524 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 304 |
| Chain | Residue |
| A | GLY208 |
| A | HIS228 |
| A | HOH505 |
| A | HOH506 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | VAL88 |
| A | ARG144 |
| A | ASN145 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue 57Y A 306 |
| Chain | Residue |
| A | ILE51 |
| A | ASN54 |
| A | SER55 |
| A | GLU58 |
| A | VAL79 |
| A | ASP81 |
| A | ARG84 |
| A | GLY85 |
| A | ILE86 |
| A | PRO87 |
| A | ARG144 |
| A | THR173 |
| A | ILE175 |
| A | HOH406 |
| A | HOH406 |
| A | HOH408 |
| A | HOH432 |
| A | HOH443 |
| A | HOH537 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | ASN54 |
| B | HOH409 |
| B | HOH429 |
| B | HOH506 |
| B | HOH533 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | GLY208 |
| B | HIS228 |
| B | HOH490 |
| B | HOH496 |
| B | HOH534 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 303 |
| Chain | Residue |
| B | GLU164 |
| B | GLU219 |
| B | HOH461 |
| B | HOH487 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 304 |
| Chain | Residue |
| B | ASN82 |
| B | GLY83 |
| B | THR171 |
| B | HOH467 |
| B | HOH520 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MPD B 305 |
| Chain | Residue |
| B | HIS143 |
| B | VAL174 |
| B | GLU186 |
| B | HOH485 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 306 |
| Chain | Residue |
| B | VAL88 |
| B | ASP89 |
| B | ARG144 |
| B | ASN145 |
| site_id | AD4 |
| Number of Residues | 25 |
| Details | binding site for residue 57Y B 307 |
| Chain | Residue |
| A | THR185 |
| A | GLU186 |
| A | HOH450 |
| B | ASN54 |
| B | SER55 |
| B | GLU58 |
| B | VAL79 |
| B | ASP81 |
| B | ARG84 |
| B | GLY85 |
| B | ILE86 |
| B | PRO87 |
| B | ARG144 |
| B | THR173 |
| B | ILE175 |
| B | HOH401 |
| B | HOH402 |
| B | HOH403 |
| B | HOH404 |
| B | HOH413 |
| B | HOH432 |
| B | HOH434 |
| B | HOH454 |
| B | HOH509 |
| B | HOH510 |
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 | |
