3VW1
Crystal Strucuture of the Crystal Violet-Bound Form of RamR (Transcriptional Regurator of TetR Family) from Salmonella Typhimurium
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000976 | molecular_function | transcription cis-regulatory region binding |
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 | 0000976 | molecular_function | transcription cis-regulatory region binding |
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 | 0000976 | molecular_function | transcription cis-regulatory region binding |
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 | 0000976 | molecular_function | transcription cis-regulatory region binding |
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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 201 |
Chain | Residue |
A | GLN19 |
A | HIS99 |
A | PRO100 |
A | ALA101 |
A | ARG102 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 202 |
Chain | Residue |
A | ARG35 |
D | LYS51 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CVI B 301 |
Chain | Residue |
B | CYS67 |
B | MET70 |
B | ILE88 |
B | SER91 |
B | TYR92 |
B | ILE106 |
B | LEU130 |
B | PHE155 |
B | HOH410 |
B | TYR59 |
B | LEU66 |
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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 201 |
Chain | Residue |
C | GLN19 |
C | HIS99 |
C | PRO100 |
C | ALA101 |
C | ARG102 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CVI D 301 |
Chain | Residue |
D | TYR59 |
D | CYS67 |
D | MET70 |
D | ILE88 |
D | SER91 |
D | ILE106 |
D | PHE127 |
D | LEU130 |
D | CYS134 |
D | VAL138 |
D | PHE155 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 D 302 |
Chain | Residue |
D | GLN19 |
D | ASN98 |
D | HIS99 |
D | PRO100 |
D | ALA101 |
D | ARG102 |
D | HOH414 |
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 |