3CAG
Crystal structure of the oligomerization domain hexamer of the arginine repressor protein from Mycobacterium tuberculosis in complex with 9 arginines.
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 |
| A | 0034618 | molecular_function | arginine binding |
| A | 0051259 | biological_process | protein complex oligomerization |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0034618 | molecular_function | arginine binding |
| B | 0051259 | biological_process | protein complex oligomerization |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0034618 | molecular_function | arginine binding |
| C | 0051259 | biological_process | protein complex oligomerization |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0034618 | molecular_function | arginine binding |
| D | 0051259 | biological_process | protein complex oligomerization |
| E | 0003700 | molecular_function | DNA-binding transcription factor activity |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0034618 | molecular_function | arginine binding |
| E | 0051259 | biological_process | protein complex oligomerization |
| F | 0003700 | molecular_function | DNA-binding transcription factor activity |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0034618 | molecular_function | arginine binding |
| F | 0051259 | biological_process | protein complex oligomerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ARG A 300 |
| Chain | Residue |
| A | HIS125 |
| C | ASP147 |
| C | THR148 |
| F | PRO121 |
| F | GLY122 |
| F | ASP146 |
| A | ALA128 |
| A | SER129 |
| A | ASP132 |
| A | THR142 |
| A | ILE143 |
| A | ALA144 |
| C | GLY145 |
| C | ASP146 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ARG B 300 |
| Chain | Residue |
| A | GLY145 |
| A | ASP146 |
| A | ASP147 |
| A | THR148 |
| B | HIS125 |
| B | ALA128 |
| B | ASP132 |
| B | THR142 |
| B | ILE143 |
| B | ALA144 |
| E | PRO121 |
| E | ASP146 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ARG C 300 |
| Chain | Residue |
| B | GLY145 |
| B | ASP146 |
| B | ASP147 |
| B | THR148 |
| C | HIS125 |
| C | ALA128 |
| C | ASP132 |
| C | THR142 |
| C | ILE143 |
| C | ALA144 |
| D | PRO121 |
| D | GLY122 |
| D | ASP146 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ARG D 300 |
| Chain | Residue |
| C | ASP146 |
| D | HIS125 |
| D | ALA128 |
| D | ASP132 |
| D | THR142 |
| D | ILE143 |
| D | ALA144 |
| F | GLY145 |
| F | ASP146 |
| F | ASP147 |
| F | THR148 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ARG E 300 |
| Chain | Residue |
| B | PRO121 |
| B | ASP146 |
| D | GLY145 |
| D | ASP146 |
| D | ASP147 |
| D | THR148 |
| E | HIS125 |
| E | ALA128 |
| E | SER129 |
| E | ASP132 |
| E | THR142 |
| E | ILE143 |
| E | ALA144 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ARG F 300 |
| Chain | Residue |
| A | PRO121 |
| A | ASP146 |
| E | GLY145 |
| E | ASP146 |
| E | ASP147 |
| E | THR148 |
| F | HIS125 |
| F | ALA128 |
| F | ASP132 |
| F | THR142 |
| F | ILE143 |
| F | ALA144 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ARG A 400 |
| Chain | Residue |
| A | GLY122 |
| A | ALA124 |
| A | HIS125 |
| A | GLY145 |
| A | ASP146 |
| B | GLY122 |
| B | HIS125 |
| E | GLY122 |
| E | ALA124 |
| E | HIS125 |
| E | GLY145 |
| E | ASP146 |
| F | GLY122 |
| F | HIS125 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ARG B 400 |
| Chain | Residue |
| D | GLY145 |
| D | ASP146 |
| E | GLY122 |
| E | HIS125 |
| B | GLY122 |
| B | ALA124 |
| B | HIS125 |
| B | GLY145 |
| B | ASP146 |
| C | GLY122 |
| C | HIS125 |
| D | GLY122 |
| D | ALA124 |
| D | HIS125 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ARG C 400 |
| Chain | Residue |
| A | GLY122 |
| A | HIS125 |
| C | GLY122 |
| C | ALA123 |
| C | ALA124 |
| C | HIS125 |
| C | GLY145 |
| C | ASP146 |
| D | HIS125 |
| F | GLY122 |
| F | ALA124 |
| F | HIS125 |
| F | GLY145 |
| F | ASP146 |
