3VVZ
Crystal Strucuture of The Rhodamine 6G-Bound Form of RamR (Transcriptional Regurator of TetR Family) from Salmonella Typhimurium
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 | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| 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 | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE RHQ A 301 |
| Chain | Residue |
| A | LEU66 |
| A | MET143 |
| A | ARG148 |
| A | GLY151 |
| A | ASP152 |
| A | PHE155 |
| A | THR85 |
| A | ILE88 |
| A | TRP89 |
| A | ILE106 |
| A | ASP124 |
| A | CYS134 |
| A | HIS135 |
| A | PHE142 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | GLN19 |
| A | HIS99 |
| A | PRO100 |
| A | ALA101 |
| A | ARG102 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE RHQ B 301 |
| Chain | Residue |
| B | LEU66 |
| B | THR85 |
| B | ILE88 |
| B | TRP89 |
| B | ILE106 |
| B | ASP124 |
| B | LEU130 |
| B | ARG131 |
| B | CYS134 |
| B | HIS135 |
| B | PHE142 |
| B | ARG148 |
| B | GLY151 |
| B | ASP152 |
| B | PHE155 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 302 |
| Chain | Residue |
| B | GLN19 |
| B | HIS99 |
| B | PRO100 |
| B | ALA101 |
| B | ARG102 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE RHQ C 301 |
| Chain | Residue |
| C | THR85 |
| C | ILE88 |
| C | TRP89 |
| C | ASP124 |
| C | LEU130 |
| C | CYS134 |
| C | HIS135 |
| C | PHE142 |
| C | MET143 |
| C | ARG148 |
| C | GLY151 |
| C | ASP152 |
| C | PHE155 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 302 |
| Chain | Residue |
| C | GLN19 |
| C | HIS99 |
| C | PRO100 |
| C | ALA101 |
| C | ARG102 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE RHQ D 301 |
| Chain | Residue |
| D | LYS63 |
| D | THR85 |
| D | TRP89 |
| D | ILE106 |
| D | ASP124 |
| D | LEU130 |
| D | CYS134 |
| D | HIS135 |
| D | PHE142 |
| D | ARG148 |
| D | GLY151 |
| D | ASP152 |
| D | PHE155 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 302 |
| Chain | Residue |
| D | GLN19 |
| D | HIS99 |
| D | PRO100 |
| D | ALA101 |
| D | ARG102 |
Functional Information from PROSITE/UniProt
| site_id | PS01081 |
| Number of Residues | 31 |
| Details | HTH_TETR_1 TetR-type HTH domain signature. GIaa.STavIarnagVAeGtLFrYFaTKdelI |
| Chain | Residue | Details |
| A | GLY25-ILE55 |
