4PDK
FadR, Fatty Acid Responsive Transcription Factor from Vibrio cholerae, in Complex with oleoyl-CoA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000062 | molecular_function | fatty-acyl-CoA binding |
A | 0003677 | molecular_function | DNA binding |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0019217 | biological_process | regulation of fatty acid metabolic process |
A | 0071072 | biological_process | negative regulation of phospholipid biosynthetic process |
B | 0000062 | molecular_function | fatty-acyl-CoA binding |
B | 0003677 | molecular_function | DNA binding |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0019217 | biological_process | regulation of fatty acid metabolic process |
B | 0071072 | biological_process | negative regulation of phospholipid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | binding site for residue 3VV A 301 |
Chain | Residue |
A | LEU101 |
A | SER151 |
A | PRO152 |
A | ASP185 |
A | LEU208 |
A | TYR212 |
A | GLY216 |
A | TYR219 |
A | PHE220 |
A | ARG253 |
A | GLY256 |
A | LEU102 |
A | SER259 |
A | GLY260 |
A | TRP263 |
B | TYR115 |
B | LYS118 |
B | ARG245 |
A | ALA103 |
A | ARG105 |
A | THR106 |
A | ILE108 |
A | SER134 |
A | ALA137 |
A | ALA150 |
site_id | AC2 |
Number of Residues | 14 |
Details | binding site for residue 3VV A 302 |
Chain | Residue |
A | ASN130 |
A | SER134 |
A | TYR153 |
A | LYS156 |
A | TYR184 |
A | ARG191 |
A | PHE194 |
A | HIS195 |
A | ILE200 |
A | GLY207 |
B | TRP21 |
B | PRO27 |
B | ILE82 |
B | 3VV302 |
site_id | AC3 |
Number of Residues | 19 |
Details | binding site for residue 3VV B 301 |
Chain | Residue |
A | ILE111 |
A | ARG114 |
A | TYR115 |
A | ILE204 |
A | ARG245 |
B | LEU101 |
B | LEU102 |
B | ALA104 |
B | ARG105 |
B | THR106 |
B | ILE108 |
B | PHE205 |
B | TYR212 |
B | TYR219 |
B | ARG253 |
B | GLY256 |
B | ILE257 |
B | SER259 |
B | GLY260 |
site_id | AC4 |
Number of Residues | 14 |
Details | binding site for residue 3VV B 302 |
Chain | Residue |
A | PRO27 |
A | MET75 |
A | 3VV302 |
B | ARG126 |
B | ASN130 |
B | SER134 |
B | TYR153 |
B | TYR184 |
B | ARG191 |
B | PHE194 |
B | HIS195 |
B | GLN199 |
B | ILE204 |
B | LEU208 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 38 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00696 |
Chain | Residue | Details |
A | GLU34-GLN53 | |
B | GLU34-GLN53 |