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 | 14 |
Details | binding site for residue N1N A 301 |
Chain | Residue |
A | ASN54 |
A | ALA98 |
A | ARG144 |
A | HOH407 |
A | HOH420 |
A | HOH428 |
A | SER55 |
A | GLU58 |
A | ASP81 |
A | ARG84 |
A | ARG84 |
A | GLY85 |
A | ILE86 |
A | PRO87 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | ARG200 |
A | PHE204 |
A | HOH406 |
A | HOH427 |
B | GLY95 |
B | ARG96 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MPD A 303 |
Chain | Residue |
A | THR80 |
A | ASP81 |
A | HIS143 |
A | LYS170 |
A | MPD304 |
A | HOH445 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue MPD A 304 |
Chain | Residue |
A | TYR141 |
A | HIS143 |
A | MPD303 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue MPD A 305 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CL A 306 |
Chain | Residue |
A | VAL88 |
A | ASP89 |
A | ARG144 |
A | ASN145 |
site_id | AC7 |
Number of Residues | 18 |
Details | binding site for residue N1N B 301 |
Chain | Residue |
A | THR185 |
A | GLU186 |
A | HOH409 |
B | ASN54 |
B | SER55 |
B | GLU58 |
B | ASP81 |
B | ARG84 |
B | GLY85 |
B | ILE86 |
B | PRO87 |
B | ARG144 |
B | THR173 |
B | ILE175 |
B | HOH411 |
B | HOH427 |
B | HOH440 |
B | HOH484 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue MPD B 302 |
Chain | Residue |
B | THR80 |
B | ASP81 |
B | HIS143 |
B | LYS170 |
B | THR171 |
B | MPD303 |
B | HOH441 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MPD B 303 |
Chain | Residue |
B | HIS143 |
B | GLU186 |
B | THR187 |
B | VAL189 |
B | MPD302 |
B | HOH441 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue IMD B 304 |
Chain | Residue |
B | LEU162 |
B | HOH426 |
B | HOH438 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue CL B 305 |
Chain | Residue |
B | VAL88 |
B | ASP89 |
B | ARG144 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CA B 306 |
Chain | Residue |
A | GLU224 |
A | HOH413 |
B | GLU224 |
B | HOH432 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue DMS B 307 |
Chain | Residue |
B | ASP74 |
B | ASN75 |
B | GLY166 |
B | THR167 |
B | THR188 |
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 | |