6Z1B
Structure of K52-acetylated RutR in complex with uracil.
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 | 0005515 | molecular_function | protein binding |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
A | 0045893 | biological_process | positive 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 | 0005515 | molecular_function | protein binding |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue URA A 301 |
Chain | Residue |
A | LEU74 |
A | TRP77 |
A | LYS101 |
A | PHE115 |
A | TRP167 |
A | GLN171 |
A | HOH409 |
B | PHE176 |
B | GLN179 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | LYS19 |
A | ALA48 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | PHE36 |
A | TYR66 |
A | GLU118 |
A | PRO124 |
A | HOH449 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | TYR57 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue URA B 301 |
Chain | Residue |
A | PHE176 |
A | GLN179 |
B | LEU74 |
B | TRP77 |
B | LEU78 |
B | LYS101 |
B | TRP167 |
B | GLN171 |
B | HOH405 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 38 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00335 |
Chain | Residue | Details |
A | THR39-TYR58 | |
B | THR39-TYR58 |