8OFB
Crystal Structure of T. maritima reverse gyrase with a minimal latch, hexagonal form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003916 | molecular_function | DNA topoisomerase activity |
| A | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006265 | biological_process | DNA topological change |
| A | 0006268 | biological_process | DNA unwinding involved in DNA replication |
| A | 0008094 | molecular_function | ATP-dependent activity, acting on DNA |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0160097 | molecular_function | reverse gyrase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00572 |
| Number of Residues | 9 |
| Details | GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LLVLENGVN |
| Chain | Residue | Details |
| A | LEU717-ASN725 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 38 |
| Details | ZN_FING: RG N-terminal-type => ECO:0000255|PROSITE-ProRule:PRU01380, ECO:0000269|PubMed:23209025 |
| Chain | Residue | Details |
| A | MET1-SER39 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 27 |
| Details | ZN_FING: RG C-terminal-type => ECO:0000255|PROSITE-ProRule:PRU01381, ECO:0000269|PubMed:23209025 |
| Chain | Residue | Details |
| A | ASP618-LYS645 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255|PROSITE-ProRule:PRU01383, ECO:0000305|PubMed:18614530 |
| Chain | Residue | Details |
| A | GLY851 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01125, ECO:0000269|PubMed:23209025, ECO:0000312|PDB:7FSE, ECO:0000312|PDB:7FSF, ECO:0000312|PDB:8OFB, ECO:0007744|PDB:4DDT, ECO:0007744|PDB:4DDU, ECO:0007744|PDB:4DDV, ECO:0007744|PDB:4DDW, ECO:0007744|PDB:4DDX |
| Chain | Residue | Details |
| A | CYS11 | |
| A | CYS14 | |
| A | CYS29 | |
| A | CYS32 | |
| A | GLN621 | |
| A | LEU624 | |
| A | MET635 | |
| A | ILE638 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21627332, ECO:0007744|PDB:3P4X |
| Chain | Residue | Details |
| A | PHE75 | |
| A | ASP78 | |
| A | GLY103 | |
| A | GLY105 | |
| A | LYS106 | |
| A | THR107 | |
| A | THR108 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01125 |
| Chain | Residue | Details |
| A | GLN83 | |
| A | ALA100 | |
| A | GLY548 | |
| A | ASP668 |
