5Z72
Crystal structure of CcpC regulatory domain in complex with citrate from Bacillus amyloliquefaciens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0003700 | molecular_function | DNA-binding transcription factor activity |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 301 |
| Chain | Residue |
| A | SER129 |
| A | SER130 |
| A | ASP190 |
| A | SER191 |
| A | FLC303 |
| A | HOH469 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | HOH406 |
| A | HOH415 |
| A | PHE187 |
| A | TYR193 |
| A | ILE233 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue FLC A 303 |
| Chain | Residue |
| A | ALA98 |
| A | SER99 |
| A | ILE100 |
| A | TRP128 |
| A | SER129 |
| A | ARG147 |
| A | PHE187 |
| A | SER189 |
| A | SER191 |
| A | ARG260 |
| A | NA301 |
| A | HOH402 |
| A | HOH408 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 301 |
| Chain | Residue |
| B | ASP168 |
| B | THR169 |
| B | ARG182 |
| B | ALA225 |
| B | GLY228 |
| B | GLY230 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 302 |
| Chain | Residue |
| B | ARG147 |
| B | MET160 |
| B | THR161 |
| B | ASP162 |
| B | ARG260 |
| B | THR262 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue NA B 303 |
| Chain | Residue |
| B | TRP128 |
| B | SER129 |
| B | SER130 |
| B | ASP190 |
| B | SER191 |
| B | FLC304 |
| B | HOH464 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue FLC B 304 |
| Chain | Residue |
| B | ALA98 |
| B | SER99 |
| B | ILE100 |
| B | TRP128 |
| B | SER129 |
| B | ARG147 |
| B | PHE187 |
| B | SER189 |
| B | SER191 |
| B | ILE218 |
| B | ARG260 |
| B | NA303 |
| B | HOH403 |
| B | HOH419 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue NA C 301 |
| Chain | Residue |
| C | TRP128 |
| C | SER129 |
| C | SER130 |
| C | ASP190 |
| C | SER191 |
| C | FLC303 |
| C | HOH454 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 302 |
| Chain | Residue |
| C | ASP168 |
| C | THR169 |
| C | ARG182 |
| C | ALA225 |
| C | GLY228 |
| C | GLY230 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue FLC C 303 |
| Chain | Residue |
| C | ALA98 |
| C | SER99 |
| C | ILE100 |
| C | TRP128 |
| C | SER129 |
| C | ARG147 |
| C | PHE187 |
| C | SER189 |
| C | SER191 |
| C | ARG260 |
| C | NA301 |
| C | HOH411 |
| C | HOH426 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue NA D 301 |
| Chain | Residue |
| D | ASP168 |
| D | THR169 |
| D | ARG182 |
| D | ALA225 |
| D | GLY228 |
| D | GLY230 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue NA D 302 |
| Chain | Residue |
| D | PHE184 |
| D | LYS210 |
| D | GLN211 |
| D | THR212 |
| D | ILE213 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue NA D 303 |
| Chain | Residue |
| D | TRP200 |
| D | GLN203 |
| D | LYS204 |
| D | HOH418 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue NA D 304 |
| Chain | Residue |
| D | GLN217 |
| D | ILE218 |
| D | FLC305 |
| D | HOH422 |
| D | ILE100 |
| site_id | AD6 |
| Number of Residues | 11 |
| Details | binding site for residue FLC D 305 |
| Chain | Residue |
| D | SER99 |
| D | ILE100 |
| D | GLY127 |
| D | TRP128 |
| D | SER129 |
| D | ARG147 |
| D | PHE187 |
| D | SER189 |
| D | SER191 |
| D | ARG260 |
| D | NA304 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue NA E 301 |
| Chain | Residue |
| E | GLN217 |
| E | ILE218 |
| E | FLC302 |
| E | HOH418 |
| site_id | AD8 |
| Number of Residues | 12 |
| Details | binding site for residue FLC E 302 |
| Chain | Residue |
| E | ALA98 |
| E | SER99 |
| E | ILE100 |
| E | TRP128 |
| E | SER129 |
| E | ARG147 |
| E | PHE187 |
| E | SER189 |
| E | ASP190 |
| E | SER191 |
| E | ILE218 |
| E | NA301 |
