5HEV
Crystal Structure of the beryllofluoride-activated LiaR from Enterococcus faecium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000160 | biological_process | phosphorelay signal transduction system |
| A | 0003677 | molecular_function | DNA binding |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0000160 | biological_process | phosphorelay signal transduction system |
| B | 0003677 | molecular_function | DNA binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0000160 | biological_process | phosphorelay signal transduction system |
| C | 0003677 | molecular_function | DNA binding |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0000160 | biological_process | phosphorelay signal transduction system |
| F | 0003677 | molecular_function | DNA binding |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | ASP8 |
| A | ASP9 |
| A | ASP54 |
| A | VAL56 |
| A | MET57 |
| A | BEF302 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue BEF A 302 |
| Chain | Residue |
| A | THR82 |
| A | SER83 |
| A | PHE84 |
| A | LYS104 |
| A | MG301 |
| A | ASP54 |
| A | LEU55 |
| A | VAL56 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG F 301 |
| Chain | Residue |
| F | ASP8 |
| F | ASP9 |
| F | ASP54 |
| F | VAL56 |
| F | MET57 |
| F | BEF302 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue BEF F 302 |
| Chain | Residue |
| F | ASP9 |
| F | ASP54 |
| F | LEU55 |
| F | VAL56 |
| F | THR82 |
| F | SER83 |
| F | PHE84 |
| F | LYS104 |
| F | MG301 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | ASP9 |
| B | ASP54 |
| B | VAL56 |
| B | BEF302 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue BEF B 302 |
| Chain | Residue |
| B | ASP9 |
| B | ASP54 |
| B | LEU55 |
| B | VAL56 |
| B | THR82 |
| B | SER83 |
| B | LYS104 |
| B | MG301 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 301 |
| Chain | Residue |
| C | ASP8 |
| C | ASP9 |
| C | ASP54 |
| C | VAL56 |
| C | BEF302 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue BEF C 302 |
| Chain | Residue |
| C | ASP9 |
| C | ASP54 |
| C | VAL56 |
| C | THR82 |
| C | SER83 |
| C | PHE84 |
| C | LYS104 |
| C | MG301 |
Functional Information from PROSITE/UniProt
| site_id | PS00622 |
| Number of Residues | 28 |
| Details | HTH_LUXR_1 LuxR-type HTH domain signature. GksNqeIAdeLfItlkTVktHvsNIlaK |
| Chain | Residue | Details |
| A | GLY163-LYS190 |
