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 501 |
Chain | Residue |
A | ASN91 |
A | ADP502 |
A | HOH601 |
A | HOH633 |
A | HOH635 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ADP A 502 |
Chain | Residue |
A | ILE125 |
A | ILE141 |
A | PHE142 |
A | SER148 |
A | SER149 |
A | ASN150 |
A | GLY161 |
A | ARG162 |
A | ASN163 |
A | GLY164 |
A | TYR165 |
A | GLY166 |
A | ALA167 |
A | LYS168 |
A | MG501 |
A | HOH601 |
A | HOH635 |
B | TYR34 |
A | ASN91 |
A | ASN95 |
A | ARG98 |
A | ASN120 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 503 |
Chain | Residue |
A | TYR50 |
A | LYS83 |
A | ASN163 |
A | TYR165 |
A | GLY166 |
A | LYS378 |
A | HOH635 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 501 |
Chain | Residue |
B | ASN91 |
B | ADP503 |
B | HOH644 |
B | HOH645 |
B | HOH646 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 B 502 |
Chain | Residue |
B | GLU87 |
B | ARG162 |
B | ASN163 |
B | GLY164 |
B | TYR165 |
B | GLY166 |
B | LYS378 |
B | ADP503 |
B | HOH645 |
site_id | AC6 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE ADP B 503 |
Chain | Residue |
A | TYR34 |
B | ASN91 |
B | ASN95 |
B | ASN120 |
B | ILE125 |
B | ILE141 |
B | PHE142 |
B | SER148 |
B | SER149 |
B | ASN150 |
B | GLY161 |
B | ARG162 |
B | ASN163 |
B | GLY164 |
B | TYR165 |
B | GLY166 |
B | ALA167 |
B | LYS168 |
B | MG501 |
B | SO4502 |
B | HOH603 |
B | HOH606 |
B | HOH612 |
B | HOH645 |
B | HOH646 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 501 |
Chain | Residue |
C | ASN91 |
C | ADP502 |
C | HOH602 |
C | HOH607 |
C | HOH638 |
site_id | AC8 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE ADP C 502 |
Chain | Residue |
C | HOH610 |
C | HOH638 |
D | TYR34 |
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 |
C | LYS168 |
C | MG501 |
C | SO4503 |
C | HOH603 |
C | HOH607 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 C 503 |
Chain | Residue |
C | GLU87 |
C | ASN163 |
C | TYR165 |
C | GLY166 |
C | LYS378 |
C | ADP502 |
C | HOH607 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 501 |
Chain | Residue |
D | ASN91 |
D | ADP503 |
D | HOH609 |
D | HOH610 |
D | HOH611 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 D 502 |
Chain | Residue |
D | GLU87 |
D | ARG162 |
D | ASN163 |
D | GLY164 |
D | TYR165 |
D | GLY166 |
D | LYS378 |
D | ADP503 |
D | HOH611 |
site_id | BC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ADP D 503 |
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 | MG501 |
D | SO4502 |
D | HOH610 |
D | HOH611 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 44 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"16100112","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25202966","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"16100112","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25202966","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 36 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Region: {"description":"Interaction with DNA","evidences":[{"source":"PubMed","id":"23022727","evidenceCode":"ECO:0000305"}]} |