7DMW
Crystal structure of CcpC regulatory domain in complex with citrate from Bacillus amyloliquefaciens
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000976 | molecular_function | transcription cis-regulatory region 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 | 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 | 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 | 0003700 | molecular_function | DNA-binding transcription factor activity |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0000976 | molecular_function | transcription cis-regulatory region binding |
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 | 12 |
Details | binding site for residue FLC A 300 |
Chain | Residue |
A | ALA98 |
A | ARG260 |
A | HOH403 |
A | HOH415 |
A | SER99 |
A | ILE100 |
A | TRP128 |
A | SER129 |
A | ARG147 |
A | PHE187 |
A | SER189 |
A | SER191 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue FLC B 301 |
Chain | Residue |
B | ALA98 |
B | SER99 |
B | ILE100 |
B | TRP128 |
B | SER129 |
B | ARG147 |
B | PHE187 |
B | SER189 |
B | SER191 |
B | ARG260 |
B | HOH418 |
B | HOH422 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue FLC C 301 |
Chain | Residue |
C | ALA98 |
C | SER99 |
C | ILE100 |
C | TRP128 |
C | SER129 |
C | ARG147 |
C | PHE187 |
C | SER189 |
C | SER191 |
C | GLN217 |
C | ARG260 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue FLC D 301 |
Chain | Residue |
D | ALA98 |
D | SER99 |
D | ILE100 |
D | TRP128 |
D | SER129 |
D | ARG147 |
D | PHE187 |
D | SER189 |
D | SER191 |
D | GLN217 |
D | ARG260 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue FLC E 301 |
Chain | Residue |
E | ALA98 |
E | SER99 |
E | ILE100 |
E | SER129 |
E | ARG147 |
E | PHE187 |
E | SER189 |
E | SER191 |
E | TYR193 |
E | ARG260 |