Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0006259 | biological_process | DNA metabolic process |
b | 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 | 0006259 | biological_process | DNA metabolic process |
B | 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 | 0006259 | biological_process | DNA metabolic process |
d | 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 | 0006259 | biological_process | DNA metabolic process |
D | 0006265 | biological_process | DNA topological change |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MN B 1501 |
Chain | Residue |
B | ASP508 |
B | ASP510 |
B | HOH1724 |
B | HOH1840 |
B | HOH1990 |
E | HOH132 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue 94H B 1502 |
Chain | Residue |
B | MET1027 |
B | MET1179 |
B | ARG1342 |
B | PRO1343 |
B | HOH1683 |
B | HOH1926 |
B | HOH1952 |
B | HOH1970 |
B | HOH2016 |
D | HOH1611 |
B | ARG630 |
B | GLU634 |
B | ALA637 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL B 1503 |
Chain | Residue |
B | ARG458 |
B | HOH1602 |
B | HOH1870 |
E | DG-1 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL B 1504 |
Chain | Residue |
B | GLY446 |
B | ARG447 |
B | TRP592 |
B | HOH1613 |
B | HOH1978 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL B 1505 |
Chain | Residue |
B | MET1113 |
B | GLY1115 |
B | GLN1267 |
B | VAL1268 |
E | DC-5 |
E | HOH143 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue 94H B 1506 |
Chain | Residue |
B | ILE1386 |
B | ASP1389 |
B | HIS1390 |
B | GLU1393 |
B | ARG1414 |
b | ARG468 |
e | DA-8 |
e | 9JN101 |
f | DT12 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MN D 1501 |
Chain | Residue |
D | ASP508 |
D | ASP510 |
D | HOH1632 |
D | HOH1961 |
D | HOH1968 |
F | HOH106 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue GOL D 1502 |
Chain | Residue |
D | SER445 |
D | GLY446 |
D | ASP589 |
D | TRP592 |
D | HOH1636 |
D | HOH2005 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue 94H D 1503 |
Chain | Residue |
D | ARG630 |
D | GLU634 |
D | ALA637 |
D | MET1027 |
D | MET1179 |
D | ARG1342 |
D | PRO1343 |
D | HOH1656 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue GOL D 1504 |
Chain | Residue |
B | LYS1066 |
B | ARG1122 |
B | HOH1781 |
D | PRO1080 |
D | HIS1081 |
D | GLY1082 |
D | HOH1658 |
D | HOH1680 |
D | HOH1916 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue GOL D 1505 |
Chain | Residue |
D | PRO1044 |
D | ARG1047 |
D | PRO1157 |
D | HOH1775 |
D | HOH1783 |
D | HOH1867 |
D | HOH1937 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue GOL D 1506 |
Chain | Residue |
D | TYR1051 |
D | GLU1055 |
D | TYR1078 |
D | GLU1154 |
D | ARG1155 |
D | HOH1606 |
D | HOH1794 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue CL D 1507 |
Chain | Residue |
D | HIS1390 |
D | HOH2114 |
f | DA-8 |
f | HOH110 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue MN b 1501 |
Chain | Residue |
b | ASP508 |
b | ASP510 |
b | HOH1641 |
b | HOH1935 |
b | HOH1962 |
e | HOH224 |
site_id | AD6 |
Number of Residues | 14 |
Details | binding site for residue 94H b 1502 |
Chain | Residue |
b | MET1027 |
b | MET1179 |
b | ARG1342 |
b | PRO1343 |
b | HOH1802 |
b | HOH1845 |
b | HOH1903 |
b | HOH1986 |
b | HOH2017 |
d | GLU1235 |
d | HOH1609 |
b | ARG630 |
b | GLU634 |
b | ALA637 |
site_id | AD7 |
Number of Residues | 9 |
Details | binding site for residue GOL b 1503 |
Chain | Residue |
b | MET1075 |
b | PRO1080 |
b | HIS1081 |
b | HOH1653 |
b | HOH1697 |
b | HOH1772 |
b | HOH1841 |
d | ARG1122 |
d | PHE1123 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue GOL b 1504 |
Chain | Residue |
b | PRO1044 |
b | ARG1047 |
b | HOH1634 |
b | HOH1656 |
b | HOH1666 |
b | HOH1758 |
b | HOH1820 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for residue GOL b 1505 |
Chain | Residue |
b | ARG1122 |
b | PHE1123 |
b | HOH1655 |
b | HOH1660 |
b | HOH1706 |
d | MET1075 |
d | PRO1080 |
d | HIS1081 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue SO4 b 1506 |
Chain | Residue |
b | ARG1429 |
b | HOH1627 |
b | HOH1973 |
d | ARG1429 |
d | ARG1432 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue NA b 1507 |
Chain | Residue |
b | TYR1322 |
b | LYS1323 |
b | THR1325 |
b | GLN1328 |
b | HOH1991 |
b | HOH2074 |
site_id | AE3 |
Number of Residues | 12 |
Details | binding site for residue 9JN b 1508 |
Chain | Residue |
B | ARG468 |
B | HOH2073 |
E | DA-8 |
F | DT12 |
b | ARG1385 |
b | ILE1386 |
b | ASP1389 |
b | HIS1390 |
b | GLU1393 |
b | ARG1414 |
b | LYS1416 |
b | 94H1509 |
site_id | AE4 |
Number of Residues | 13 |
Details | binding site for residue 94H b 1509 |
Chain | Residue |
B | ARG468 |
B | HOH2073 |
E | DA-8 |
F | DT12 |
b | ILE1386 |
b | ASP1389 |
b | HIS1390 |
b | GLU1393 |
b | ARG1414 |
b | PHE1415 |
b | LYS1416 |
b | 9JN1508 |
b | HOH1718 |
site_id | AE5 |
Number of Residues | 6 |
Details | binding site for residue MN d 1501 |
Chain | Residue |
d | ASP508 |
d | ASP510 |
d | HOH1649 |
d | HOH1843 |
d | HOH1879 |
f | HOH131 |
site_id | AE6 |
Number of Residues | 9 |
Details | binding site for residue 94H d 1502 |
Chain | Residue |
d | ARG630 |
d | ILE633 |
d | GLU634 |
d | ALA637 |
d | MET1027 |
d | MET1179 |
d | ARG1342 |
d | PRO1343 |
d | HOH1840 |
site_id | AE7 |
Number of Residues | 4 |
Details | binding site for residue GOL d 1503 |
Chain | Residue |
d | GLY446 |
d | ARG447 |
d | ASP589 |
d | HOH1607 |
site_id | AE8 |
Number of Residues | 7 |
Details | binding site for residue GOL d 1504 |
Chain | Residue |
d | PRO1044 |
d | ARG1047 |
d | ARG1048 |
d | GLU1156 |
d | HOH1601 |
d | HOH1653 |
d | HOH1676 |
site_id | AE9 |
Number of Residues | 2 |
Details | binding site for residue MN d 1505 |
Chain | Residue |
F | DA-8 |
d | HIS1390 |
site_id | AF1 |
Number of Residues | 11 |
Details | binding site for residue 9JN e 101 |
Chain | Residue |
B | ARG1385 |
B | ILE1386 |
B | ASP1389 |
B | HIS1390 |
B | GLU1393 |
B | ARG1414 |
B | 94H1506 |
B | HOH1852 |
b | ARG468 |
e | DA-8 |
f | DT12 |
site_id | AF2 |
Number of Residues | 9 |
Details | binding site for residue GOL e 102 |
Chain | Residue |
b | ARG458 |
b | GLY459 |
e | DG-1 |
e | DG1 |
e | DT2 |
e | HOH203 |
e | HOH222 |
f | DA3 |
f | DC4 |
site_id | AF3 |
Number of Residues | 12 |
Details | binding site for Di-peptide GLN b 1413 and ARG b 1414 |
Chain | Residue |
b | GLU1393 |
b | THR1397 |
b | GLU1409 |
b | SER1410 |
b | LEU1411 |
b | GLN1412 |
b | PHE1415 |
b | LYS1416 |
b | 9JN1508 |
b | 94H1509 |
b | HOH1741 |
b | HOH2094 |
site_id | AF4 |
Number of Residues | 12 |
Details | binding site for Di-peptide GLN b 1413 and ARG b 1414 |
Chain | Residue |
b | GLU1393 |
b | THR1397 |
b | GLU1409 |
b | SER1410 |
b | LEU1411 |
b | GLN1412 |
b | PHE1415 |
b | LYS1416 |
b | 9JN1508 |
b | 94H1509 |
b | HOH1741 |
b | HOH2094 |
Functional Information from PROSITE/UniProt
site_id | PS00177 |
Number of Residues | 9 |
Details | TOPOISOMERASE_II DNA topoisomerase II signature. LVEGDSAGG |
Chain | Residue | Details |
B | LEU433-GLY441 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | GLU435 | |
d | GLU435 | |
d | ASP508 | |
d | ASP510 | |
B | ASP508 | |
B | ASP510 | |
D | GLU435 | |
D | ASP508 | |
D | ASP510 | |
b | GLU435 | |
b | ASP508 | |
b | ASP510 | |
Chain | Residue | Details |
B | LYS460 | |
B | ASN463 | |
D | LYS460 | |
D | ASN463 | |
b | LYS460 | |
b | ASN463 | |
d | LYS460 | |
d | ASN463 | |
Chain | Residue | Details |
B | PHE1123 | |
D | PHE1123 | |
b | PHE1123 | |
d | PHE1123 | |