1XXB
C-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR/ L-ARGININE COMPLEX
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 | 10 |
| Details | BINDING SITE FOR RESIDUE ARG A 1 |
| Chain | Residue |
| A | GLN106 |
| D | ASP128 |
| A | ASP113 |
| A | THR124 |
| A | ILE125 |
| A | ALA126 |
| C | GLY127 |
| C | ASP128 |
| C | ASP129 |
| C | THR130 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ARG A 157 |
| Chain | Residue |
| A | GLY127 |
| A | ASP128 |
| A | ASP129 |
| A | THR130 |
| A | HOH158 |
| A | HOH175 |
| B | GLN106 |
| B | ALA109 |
| B | ASP113 |
| B | THR124 |
| B | ALA126 |
| F | ARG1 |
| F | PRO102 |
| F | ASP128 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ARG C 1 |
| Chain | Residue |
| B | GLY127 |
| B | ASP128 |
| B | ASP129 |
| B | THR130 |
| C | GLN106 |
| C | ALA109 |
| C | ASP113 |
| C | THR124 |
| C | ALA126 |
| E | ASP128 |
| F | ARG157 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ARG F 1 |
| Chain | Residue |
| A | PRO102 |
| A | GLY103 |
| A | ASP128 |
| A | ARG157 |
| D | GLN106 |
| D | ASP113 |
| D | THR124 |
| D | ALA126 |
| F | GLY127 |
| F | ASP128 |
| F | ASP129 |
| F | THR130 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ARG E 1 |
| Chain | Residue |
| C | ASP128 |
| D | GLY127 |
| D | ASP128 |
| D | ASP129 |
| D | THR130 |
| E | GLN106 |
| E | ALA109 |
| E | ASP113 |
| E | THR124 |
| E | ALA126 |
| E | HOH165 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ARG F 157 |
| Chain | Residue |
| B | GLY103 |
| B | ASP128 |
| C | ARG1 |
| E | GLY127 |
| E | ASP128 |
| E | ASP129 |
| E | THR130 |
| F | GLN106 |
| F | ALA109 |
| F | ARG110 |
| F | ASP113 |
| F | THR124 |
| F | ILE125 |
| F | ALA126 |
