2O59
Structure of E. coli topoisomerase III in complex with an 8-base single stranded oligonucleotide. Frozen in glycerol pH 8.0
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0005515 | molecular_function | protein binding |
| A | 0006261 | biological_process | DNA-templated DNA replication |
| A | 0006265 | biological_process | DNA topological change |
| A | 0006281 | biological_process | DNA repair |
| A | 0006310 | biological_process | DNA recombination |
| A | 0043597 | cellular_component | cytoplasmic replication fork |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051304 | biological_process | chromosome separation |
| A | 0098847 | molecular_function | sequence-specific single stranded DNA binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0005515 | molecular_function | protein binding |
| B | 0006261 | biological_process | DNA-templated DNA replication |
| B | 0006265 | biological_process | DNA topological change |
| B | 0006281 | biological_process | DNA repair |
| B | 0006310 | biological_process | DNA recombination |
| B | 0043597 | cellular_component | cytoplasmic replication fork |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051304 | biological_process | chromosome separation |
| B | 0098847 | molecular_function | sequence-specific single stranded DNA binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 800 |
| Chain | Residue |
| A | ARG60 |
| A | TRP61 |
| B | ARG185 |
| C | DC1 |
| D | DC1 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 801 |
| Chain | Residue |
| D | DC1 |
| A | ARG185 |
| B | ARG60 |
| B | TRP61 |
| C | DC1 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACY B 803 |
| Chain | Residue |
| B | ARG408 |
| B | GLN409 |
Functional Information from PROSITE/UniProt
| site_id | PS00396 |
| Number of Residues | 16 |
| Details | TOPO_IA_1 Topoisomerase (Topo) IA-type active site signature. QkLYEthkl........ITYpRSD |
| Chain | Residue | Details |
| A | GLN317-ASP332 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255|PROSITE-ProRule:PRU01383, ECO:0000269|PubMed:10574789 |
| Chain | Residue | Details |
| A | TYR328 | |
| B | TYR328 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00953 |
| Chain | Residue | Details |
| A | GLU7 | |
| A | ASP103 | |
| A | ASP105 | |
| B | GLU7 | |
| B | ASP103 | |
| B | ASP105 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | SITE: Interaction with DNA |
| Chain | Residue | Details |
| A | TRP61 | |
| B | ARG330 | |
| A | TRP170 | |
| A | ARG178 | |
| A | ARG185 | |
| A | ARG330 | |
| B | TRP61 | |
| B | TRP170 | |
| B | ARG178 | |
| B | ARG185 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ecl |
| Chain | Residue | Details |
| A | ASP103 | |
| A | TYR328 | |
| A | GLU7 | |
| A | HIS381 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ecl |
| Chain | Residue | Details |
| B | ASP103 | |
| B | TYR328 | |
| B | GLU7 | |
| B | HIS381 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ecl |
| Chain | Residue | Details |
| A | TYR328 | |
| A | LYS8 | |
| A | GLU7 | |
| A | ARG330 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ecl |
| Chain | Residue | Details |
| B | TYR328 | |
| B | LYS8 | |
| B | GLU7 | |
| B | ARG330 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 64 |
| Chain | Residue | Details |
| A | GLU7 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | LYS8 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP103 | metal ligand |
| A | ASP105 | metal ligand |
| A | TYR328 | hydrogen bond acceptor, nucleofuge, nucleophile |
| A | ARG330 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 64 |
| Chain | Residue | Details |
| B | GLU7 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| B | LYS8 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP103 | metal ligand |
| B | ASP105 | metal ligand |
| B | TYR328 | hydrogen bond acceptor, nucleofuge, nucleophile |
| B | ARG330 | electrostatic stabiliser, hydrogen bond donor |
