Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003916 | molecular_function | DNA topoisomerase activity |
A | 0003917 | molecular_function | DNA topoisomerase type I (single strand cut, ATP-independent) activity |
A | 0006265 | biological_process | DNA topological change |
A | 0046872 | molecular_function | metal ion binding |
A | 0140226 | molecular_function | RNA topoisomerase activity |
B | 0003677 | molecular_function | DNA binding |
B | 0003916 | molecular_function | DNA topoisomerase activity |
B | 0003917 | molecular_function | DNA topoisomerase type I (single strand cut, ATP-independent) activity |
B | 0006265 | biological_process | DNA topological change |
B | 0046872 | molecular_function | metal ion binding |
B | 0140226 | molecular_function | RNA topoisomerase activity |
Functional Information from PROSITE/UniProt
site_id | PS00396 |
Number of Residues | 23 |
Details | TOPO_IA_1 Topoisomerase (Topo) IA-type active site signature. QqLYEgvetkdghiaf.ITYmRTD |
Chain | Residue | Details |
A | GLN270-ASP292 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 42 |
Details | ZN_FING: C4-type |
Chain | Residue | Details |
A | CYS559-CYS580 | |
B | CYS559-CYS580 | |
Chain | Residue | Details |
A | TYR288 | |
B | TYR288 | |
Chain | Residue | Details |
A | GLU12 | |
A | ASP84 | |
B | GLU12 | |
B | ASP84 | |
Chain | Residue | Details |
A | HIS36 | |
B | ARG140 | |
B | ARG141 | |
B | ASP144 | |
B | TYR149 | |
B | TRP156 | |
B | ARG290 | |
B | ARG475 | |
A | ARG140 | |
A | ARG141 | |
A | ASP144 | |
A | TYR149 | |
A | TRP156 | |
A | ARG290 | |
A | ARG475 | |
B | HIS36 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ecl |
Chain | Residue | Details |
A | HIS334 | |
A | ASP84 | |
A | TYR288 | |
A | GLU12 | |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ecl |
Chain | Residue | Details |
B | HIS334 | |
B | ASP84 | |
B | TYR288 | |
B | GLU12 | |