3NUH
A domain insertion in E. coli GyrB adopts a novel fold that plays a critical role in gyrase function
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 | 0006259 | biological_process | DNA metabolic process |
| 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 |
Functional Information from PROSITE/UniProt
| site_id | PS00177 |
| Number of Residues | 9 |
| Details | TOPOISOMERASE_II DNA topoisomerase II signature. LVEGDSAGG |
| Chain | Residue | Details |
| B | LEU422-GLY430 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"O-(5'-phospho-DNA)-tyrosine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01897","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3031051","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01898","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12051843","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18642932","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 745 |
| Chain | Residue | Details |
| A | GLY40 | electrostatic stabiliser |
| A | VAL90 | proton acceptor |
| A | VAL146 | metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
