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 |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 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 | 0006265 | biological_process | DNA topological change |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 900 |
| Chain | Residue |
| A | ASN91 |
| A | ADP901 |
| A | HOH902 |
| A | HOH958 |
| A | HOH960 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 902 |
| Chain | Residue |
| B | HOH981 |
| B | ASN91 |
| B | ADP903 |
| B | HOH979 |
| B | HOH980 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 904 |
| Chain | Residue |
| C | ASN91 |
| C | ADP905 |
| C | HOH908 |
| C | HOH919 |
| C | HOH975 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 906 |
| Chain | Residue |
| D | ASN91 |
| D | ADP907 |
| D | HOH940 |
| D | HOH941 |
| D | HOH942 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 D 908 |
| Chain | Residue |
| D | GLU87 |
| D | ARG162 |
| D | ASN163 |
| D | GLY164 |
| D | TYR165 |
| D | GLY166 |
| D | LYS378 |
| D | ADP907 |
| D | HOH942 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 909 |
| Chain | Residue |
| B | GLU87 |
| B | ASN163 |
| B | GLY164 |
| B | TYR165 |
| B | GLY166 |
| B | ADP903 |
| B | HOH980 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP A 901 |
| Chain | Residue |
| A | ASN91 |
| A | ASN95 |
| A | ARG98 |
| A | ASN120 |
| A | ILE125 |
| A | ILE141 |
| A | SER148 |
| A | SER149 |
| A | ASN150 |
| A | GLY161 |
| A | ARG162 |
| A | ASN163 |
| A | GLY164 |
| A | TYR165 |
| A | GLY166 |
| A | ALA167 |
| A | LYS168 |
| A | MG900 |
| A | HOH902 |
| A | HOH905 |
| A | HOH911 |
| A | HOH960 |
| B | TYR34 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ADP B 903 |
| Chain | Residue |
| B | ASN91 |
| B | ASN95 |
| B | ASN120 |
| B | ILE125 |
| B | ILE141 |
| B | SER148 |
| B | SER149 |
| B | ASN150 |
| B | GLY161 |
| B | ARG162 |
| B | ASN163 |
| B | GLY164 |
| B | TYR165 |
| B | GLY166 |
| B | ALA167 |
| B | LYS168 |
| B | THR215 |
| B | MG902 |
| B | SO4909 |
| B | HOH912 |
| B | HOH916 |
| B | HOH924 |
| B | HOH980 |
| B | HOH981 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP C 905 |
| Chain | Residue |
| C | LYS168 |
| C | MG904 |
| C | HOH906 |
| C | HOH909 |
| C | HOH919 |
| C | HOH922 |
| C | HOH975 |
| C | ASN91 |
| C | ASN95 |
| C | ASN120 |
| C | ILE125 |
| C | ILE141 |
| C | PHE142 |
| C | SER148 |
| C | SER149 |
| C | ASN150 |
| C | GLY161 |
| C | ARG162 |
| C | ASN163 |
| C | GLY164 |
| C | TYR165 |
| C | GLY166 |
| C | ALA167 |
| site_id | BC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP D 907 |
| Chain | Residue |
| C | TYR34 |
| D | ASN91 |
| D | ASN95 |
| D | ASN120 |
| D | ILE125 |
| D | ILE141 |
| D | PHE142 |
| D | SER148 |
| D | SER149 |
| D | ASN150 |
| D | GLY161 |
| D | ARG162 |
| D | ASN163 |
| D | GLY164 |
| D | TYR165 |
| D | GLY166 |
| D | ALA167 |
| D | LYS168 |
| D | MG906 |
| D | SO4908 |
| D | HOH941 |
| D | HOH942 |
| D | HOH943 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 599 |
| Chain | Residue |
| A | TYR50 |
| A | LYS83 |
| A | ASN163 |
| A | TYR165 |
| A | GLY166 |
| A | GLN376 |
| A | HOH960 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| C | ASN91 | |
| C | ASN120 | |
| C | SER148 | |
| C | GLY161 | |
| D | ASN91 | |
| D | ASN120 | |
| D | SER148 | |
| D | GLY161 | |
| A | ASN91 | |
| A | ASN120 | |
| A | SER148 | |
| A | GLY161 | |
| B | ASN91 | |
| B | ASN120 | |
| B | SER148 | |
| B | GLY161 | |
| Chain | Residue | Details |
| A | GLN376 | |
| B | GLN376 | |
| C | GLN376 | |
| D | GLN376 | |
| Chain | Residue | Details |
| A | THR282 | |
| B | THR282 | |
| C | THR282 | |
| D | THR282 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 40 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS352 | |
| A | LYS386 | |
| A | LYS397 | |
| A | LYS416 | |
| A | LYS418 | |
| A | LYS425 | |
| B | LYS156 | |
| B | LYS157 | |
| B | LYS261 | |
| B | LYS352 | |
| B | LYS386 | |
| B | LYS397 | |
| B | LYS416 | |
| B | LYS418 | |
| B | LYS425 | |
| C | LYS156 | |
| C | LYS157 | |
| C | LYS261 | |
| C | LYS352 | |
| C | LYS386 | |
| C | LYS397 | |
| C | LYS416 | |
| C | LYS418 | |
| C | LYS425 | |
| D | LYS156 | |
| D | LYS157 | |
| D | LYS261 | |
| D | LYS352 | |
| D | LYS386 | |
| D | LYS397 | |
| D | LYS416 | |
| D | LYS418 | |
| D | LYS425 | |
| A | LYS156 | |
| A | LYS157 | |
| A | LYS261 | |
