5LRR
The Transcriptional Regulator PrfA from Listeria Monocytogenes in complex with glutathione
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003700 | molecular_function | DNA-binding transcription factor activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0003677 | molecular_function | DNA binding |
| F | 0003700 | molecular_function | DNA-binding transcription factor activity |
| F | 0005829 | cellular_component | cytosol |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0003677 | molecular_function | DNA binding |
| G | 0003700 | molecular_function | DNA-binding transcription factor activity |
| G | 0005829 | cellular_component | cytosol |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
| H | 0003677 | molecular_function | DNA binding |
| H | 0003700 | molecular_function | DNA-binding transcription factor activity |
| H | 0005829 | cellular_component | cytosol |
| H | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue GSH A 301 |
| Chain | Residue |
| A | GLN61 |
| A | ILE149 |
| A | VAL153 |
| A | TYR154 |
| A | HOH416 |
| A | HOH421 |
| A | HOH449 |
| A | HOH453 |
| A | TYR62 |
| A | TYR63 |
| A | LYS64 |
| A | GLY65 |
| A | ALA66 |
| A | PHE67 |
| A | LYS122 |
| A | TYR126 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | PHE29 |
| A | GLN35 |
| A | GLU36 |
| A | TYR37 |
| A | SER71 |
| A | HOH441 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 303 |
| Chain | Residue |
| A | HIS182 |
| A | SER183 |
| A | SER184 |
| A | HOH434 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue GSH B 301 |
| Chain | Residue |
| B | TYR62 |
| B | TYR63 |
| B | LYS64 |
| B | GLY65 |
| B | ALA66 |
| B | PHE67 |
| B | LYS122 |
| B | TYR126 |
| B | ILE149 |
| B | VAL153 |
| B | TYR154 |
| B | HOH415 |
| B | HOH418 |
| B | HOH449 |
| B | HOH454 |
| B | HOH461 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 302 |
| Chain | Residue |
| B | GLN172 |
| B | HIS182 |
| B | SER183 |
| B | HOH412 |
| B | HOH420 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 B 303 |
| Chain | Residue |
| B | GLY138 |
| B | LYS139 |
| F | TRP32 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | binding site for residue GSH C 301 |
| Chain | Residue |
| C | GLN61 |
| C | TYR62 |
| C | TYR63 |
| C | LYS64 |
| C | GLY65 |
| C | ALA66 |
| C | PHE67 |
| C | LYS122 |
| C | TYR126 |
| C | ILE149 |
| C | VAL153 |
| C | TYR154 |
| C | HOH420 |
| C | HOH422 |
| C | HOH432 |
| C | HOH433 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for residue GSH D 301 |
| Chain | Residue |
| D | GLN61 |
| D | TYR62 |
| D | TYR63 |
| D | LYS64 |
| D | GLY65 |
| D | ALA66 |
| D | PHE67 |
| D | LYS122 |
| D | TYR126 |
| D | ILE149 |
| D | TYR154 |
| D | HOH403 |
| D | HOH405 |
| D | HOH411 |
| D | HOH432 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue NA D 302 |
| Chain | Residue |
| D | PHE29 |
| D | GLN35 |
| D | SER71 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue GSH E 301 |
| Chain | Residue |
| E | TYR63 |
| E | LYS64 |
| E | ALA66 |
| E | PHE67 |
| E | ILE149 |
| E | CYS229 |
| E | HOH455 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue NA E 302 |
| Chain | Residue |
| E | ASN30 |
| E | ASP33 |
| E | GLU36 |
| E | HOH407 |
| E | HOH412 |
| E | HOH419 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue GSH F 301 |
| Chain | Residue |
| F | TYR63 |
| F | LYS64 |
| F | GLY65 |
| F | ALA66 |
| F | PHE67 |
| F | LYS122 |
| F | TYR126 |
| F | ILE149 |
| F | HOH433 |
| F | GLN61 |
| F | TYR62 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue NA F 302 |
| Chain | Residue |
| F | PHE29 |
| F | GLN35 |
| F | TYR37 |
| F | SER71 |
| F | HOH407 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue GSH G 301 |
| Chain | Residue |
| G | TYR63 |
| G | LYS64 |
| G | ALA66 |
| G | TYR126 |
| G | GLN146 |
| G | ILE149 |
| G | CYS229 |
| G | HOH426 |
| site_id | AD6 |
| Number of Residues | 12 |
| Details | binding site for residue GSH H 301 |
| Chain | Residue |
| H | GLN61 |
| H | TYR62 |
| H | TYR63 |
| H | LYS64 |
| H | GLY65 |
| H | ALA66 |
| H | PHE67 |
| H | TYR126 |
| H | GLN146 |
| H | ILE149 |
| H | HOH401 |
| H | HOH403 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue NA H 302 |
| Chain | Residue |
| C | ARG188 |
| H | ASN30 |
| H | GLN31 |
| H | ASP33 |
| H | HOH411 |
| H | HOH421 |
Functional Information from PROSITE/UniProt
| site_id | PS00042 |
| Number of Residues | 25 |
| Details | HTH_CRP_1 Crp-type HTH domain signature. LTMqeLGySSGiAhsSavSRiIskL |
| Chain | Residue | Details |
| A | LEU169-LEU193 |
