1MX0
Structure of topoisomerase subunit
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| 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 | 0003676 | molecular_function | nucleic acid binding |
| 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 | 0003676 | molecular_function | nucleic acid binding |
| 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 | 0003676 | molecular_function | nucleic acid binding |
| 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 |
| E | 0003676 | molecular_function | nucleic acid binding |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006265 | biological_process | DNA topological change |
| F | 0003676 | molecular_function | nucleic acid binding |
| F | 0003677 | molecular_function | DNA binding |
| F | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006265 | biological_process | DNA topological change |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | ASN42 |
| A | ANP900 |
| A | HOH913 |
| A | HOH915 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 501 |
| Chain | Residue |
| B | ASN42 |
| B | ANP910 |
| B | HOH949 |
| B | HOH985 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 501 |
| Chain | Residue |
| C | ANP920 |
| C | HOH948 |
| C | HOH1048 |
| C | ASN42 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 501 |
| Chain | Residue |
| D | ASN42 |
| D | ANP930 |
| D | HOH932 |
| D | HOH1045 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG E 501 |
| Chain | Residue |
| E | ASN42 |
| E | ANP940 |
| E | HOH976 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG F 501 |
| Chain | Residue |
| F | ASN42 |
| F | ANP950 |
| F | HOH982 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 901 |
| Chain | Residue |
| D | VAL259 |
| D | PHE262 |
| D | ILE265 |
| D | HOH954 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ANP A 900 |
| Chain | Residue |
| A | GLU38 |
| A | ASN42 |
| A | ALA46 |
| A | ASP76 |
| A | GLY80 |
| A | ILE81 |
| A | ALA89 |
| A | SER96 |
| A | SER97 |
| A | LYS98 |
| A | GLY106 |
| A | MSE107 |
| A | TYR108 |
| A | GLY109 |
| A | LEU110 |
| A | GLY111 |
| A | VAL112 |
| A | LYS113 |
| A | LYS427 |
| A | MG501 |
| A | HOH905 |
| A | HOH912 |
| A | HOH915 |
| A | HOH969 |
| B | PHE7 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ANP B 910 |
| Chain | Residue |
| A | PHE7 |
| B | ASN42 |
| B | ALA46 |
| B | ASP76 |
| B | GLY80 |
| B | ILE81 |
| B | ALA89 |
| B | SER96 |
| B | SER97 |
| B | LYS98 |
| B | GLY106 |
| B | MSE107 |
| B | TYR108 |
| B | GLY109 |
| B | LEU110 |
| B | GLY111 |
| B | VAL112 |
| B | LYS113 |
| B | THR170 |
| B | LYS427 |
| B | MG501 |
| B | HOH911 |
| B | HOH922 |
| B | HOH978 |
| B | HOH985 |
| site_id | BC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ANP C 920 |
| Chain | Residue |
| C | HOH948 |
| C | HOH980 |
| C | HOH982 |
| C | HOH1048 |
| D | PHE7 |
| C | GLU38 |
| C | ASN42 |
| C | ALA46 |
| C | ASP76 |
| C | ILE81 |
| C | ALA89 |
| C | PHE90 |
| C | SER96 |
| C | SER97 |
| C | LYS98 |
| C | GLY106 |
| C | MSE107 |
| C | TYR108 |
| C | GLY109 |
| C | LEU110 |
| C | GLY111 |
| C | VAL112 |
| C | LYS113 |
| C | THR170 |
| C | LYS427 |
| C | MG501 |
| C | HOH924 |
| C | HOH931 |
| site_id | BC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ANP D 930 |
| Chain | Residue |
| C | PHE7 |
| D | GLU38 |
| D | ASN42 |
| D | ALA46 |
| D | ASP76 |
| D | ILE81 |
| D | ALA89 |
| D | SER96 |
| D | SER97 |
| D | LYS98 |
| D | GLY106 |
| D | MSE107 |
| D | TYR108 |
| D | GLY109 |
| D | LEU110 |
| D | GLY111 |
| D | VAL112 |
| D | LYS113 |
| D | LYS427 |
| D | MG501 |
| D | HOH932 |
| D | HOH934 |
| D | HOH938 |
| D | HOH940 |
| D | HOH943 |
| D | HOH1045 |
| site_id | BC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ANP E 940 |
| Chain | Residue |
| E | GLU38 |
| E | ASN42 |
| E | ALA46 |
| E | ASP76 |
| E | ILE81 |
| E | ALA89 |
| E | SER96 |
| E | SER97 |
| E | LYS98 |
| E | GLY106 |
| E | MSE107 |
| E | TYR108 |
| E | GLY109 |
| E | LEU110 |
| E | GLY111 |
| E | VAL112 |
| E | LYS113 |
| E | THR170 |
| E | LYS427 |
| E | MG501 |
| E | HOH941 |
| E | HOH943 |
| E | HOH949 |
| E | HOH961 |
| E | HOH976 |
| F | PHE7 |
| site_id | BC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ANP F 950 |
| Chain | Residue |
| E | PHE7 |
| F | ASN42 |
| F | SER43 |
| F | ALA46 |
| F | ASP76 |
| F | GLY80 |
| F | ILE81 |
| F | ALA89 |
| F | TYR95 |
| F | SER96 |
| F | SER97 |
| F | LYS98 |
| F | GLY106 |
| F | MSE107 |
| F | TYR108 |
| F | GLY109 |
| F | LEU110 |
| F | GLY111 |
| F | VAL112 |
| F | LYS113 |
| F | LYS427 |
| F | MG501 |
| F | HOH951 |
| F | HOH979 |
| F | HOH982 |
| F | HOH998 |
| F | HOH1017 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12505993","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15939019","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z59","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z5A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z5B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z5C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12505993","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15939019","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z5A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z5B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z5C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12505993","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MX0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






