5C8D
Crystal structure of full-length Thermus thermophilus CarH bound to adenosylcobalamin (dark state)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0031419 | molecular_function | cobalamin binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0031419 | molecular_function | cobalamin binding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003700 | molecular_function | DNA-binding transcription factor activity |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0031419 | molecular_function | cobalamin binding |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0003677 | molecular_function | DNA binding |
| F | 0003700 | molecular_function | DNA-binding transcription factor activity |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0031419 | molecular_function | cobalamin binding |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0003677 | molecular_function | DNA binding |
| G | 0003700 | molecular_function | DNA-binding transcription factor activity |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0031419 | molecular_function | cobalamin binding |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0003677 | molecular_function | DNA binding |
| H | 0003700 | molecular_function | DNA-binding transcription factor activity |
| H | 0006355 | biological_process | regulation of DNA-templated transcription |
| H | 0031419 | molecular_function | cobalamin binding |
| H | 0042802 | molecular_function | identical protein binding |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue B12 A 300 |
| Chain | Residue |
| A | GLU117 |
| A | ARG176 |
| A | HIS177 |
| A | GLU178 |
| A | ILE179 |
| A | GLY180 |
| A | VAL220 |
| A | SER222 |
| A | VAL224 |
| A | LEU225 |
| A | GLY247 |
| A | LEU121 |
| A | GLY248 |
| A | GLN249 |
| A | MET264 |
| A | ASP266 |
| A | LEU267 |
| A | 5AD301 |
| A | LEU124 |
| A | GLY128 |
| A | GLU141 |
| A | HIS142 |
| A | SER145 |
| A | GLY174 |
| A | GLU175 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue 5AD A 301 |
| Chain | Residue |
| A | TRP131 |
| A | VAL138 |
| A | GLU141 |
| A | HIS142 |
| A | B12300 |
| B | ASP201 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue B12 B 300 |
| Chain | Residue |
| B | LEU121 |
| B | LEU124 |
| B | ARG125 |
| B | GLY128 |
| B | TRP131 |
| B | HIS132 |
| B | GLU141 |
| B | HIS142 |
| B | SER145 |
| B | ARG149 |
| B | GLY174 |
| B | GLU175 |
| B | ARG176 |
| B | HIS177 |
| B | GLU178 |
| B | ILE179 |
| B | GLY180 |
| B | VAL220 |
| B | SER222 |
| B | VAL224 |
| B | LEU225 |
| B | GLY247 |
| B | GLY248 |
| B | GLN249 |
| B | MET264 |
| B | ASP266 |
| B | LEU267 |
| B | 5AD301 |
| H | ALA231 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue 5AD B 301 |
| Chain | Residue |
| A | ASP201 |
| A | PRO203 |
| B | TRP131 |
| B | VAL138 |
| B | GLU141 |
| B | HIS142 |
| B | B12300 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | binding site for residue B12 C 300 |
| Chain | Residue |
| C | GLU117 |
| C | LEU121 |
| C | LEU124 |
| C | ARG125 |
| C | GLY128 |
| C | GLU129 |
| C | TRP131 |
| C | HIS132 |
| C | GLU141 |
| C | HIS142 |
| C | SER145 |
| C | GLY174 |
| C | GLU175 |
| C | ARG176 |
| C | HIS177 |
| C | GLU178 |
| C | ILE179 |
| C | GLY180 |
| C | LEU183 |
| C | VAL220 |
| C | SER222 |
| C | VAL224 |
| C | LEU225 |
| C | GLY247 |
| C | GLY248 |
| C | GLN249 |
| C | MET264 |
| C | ASP266 |
| C | LEU267 |
| C | 5AD301 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue 5AD C 301 |
| Chain | Residue |
| C | GLU141 |
| C | HIS142 |
| C | B12300 |
| D | ASP201 |
| D | PRO203 |
| C | TRP131 |
| C | VAL138 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | binding site for residue B12 D 300 |
| Chain | Residue |
| D | LEU121 |
| D | LEU124 |
| D | ARG125 |
| D | GLY128 |
| D | TRP131 |
| D | HIS132 |
| D | GLU141 |
| D | HIS142 |
| D | SER145 |
| D | ARG149 |
| D | GLY174 |
| D | GLU175 |
| D | ARG176 |
| D | HIS177 |
| D | GLU178 |
| D | ILE179 |
| D | GLY180 |
| D | VAL220 |
| D | SER222 |
| D | VAL224 |
| D | LEU225 |
| D | GLY247 |
| D | GLY248 |
| D | GLN249 |
| D | MET264 |
| D | ASP266 |
| D | LEU267 |
| D | 5AD301 |
| F | ARG230 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue 5AD D 301 |
| Chain | Residue |
| C | ASP201 |
| C | PRO203 |
| D | TRP131 |
| D | VAL138 |
| D | GLU141 |
| D | HIS142 |
| D | B12300 |
| site_id | AC9 |
| Number of Residues | 26 |
| Details | binding site for residue B12 E 300 |
| Chain | Residue |
| E | LEU121 |
| E | LEU124 |
| E | ARG125 |
| E | GLY128 |
| E | TRP131 |
| E | GLU141 |
| E | HIS142 |
| E | SER145 |
| E | GLY174 |
| E | GLU175 |
| E | ARG176 |
| E | HIS177 |
| E | GLU178 |
| E | ILE179 |
| E | GLY180 |
| E | VAL220 |
| E | SER222 |
| E | VAL224 |
| E | LEU225 |
| E | GLY247 |
| E | GLY248 |
| E | GLN249 |
| E | MET264 |
| E | ASP266 |
| E | LEU267 |
| E | 5AD301 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue 5AD E 301 |
| Chain | Residue |
| E | TRP131 |
| E | VAL138 |
| E | GLU141 |
| E | HIS142 |
| E | B12300 |
| F | ASP201 |
| site_id | AD2 |
| Number of Residues | 30 |
| Details | binding site for residue B12 F 300 |
| Chain | Residue |
| D | ALA231 |
| F | LEU121 |
| F | LEU124 |
| F | ARG125 |
| F | GLY128 |
| F | TRP131 |
| F | HIS132 |
| F | GLU141 |
| F | HIS142 |
| F | SER145 |
| F | ARG149 |
| F | GLY174 |
| F | GLU175 |
| F | ARG176 |
| F | HIS177 |
| F | GLU178 |
| F | ILE179 |
| F | GLY180 |
| F | LEU183 |
| F | VAL220 |
| F | SER222 |
| F | VAL224 |
| F | LEU225 |
| F | GLY247 |
| F | GLY248 |
| F | GLN249 |
| F | MET264 |
| F | ASP266 |
| F | LEU267 |
| F | 5AD301 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue 5AD F 301 |
| Chain | Residue |
| E | ASP201 |
| E | PRO203 |
| F | TRP131 |
| F | VAL138 |
| F | GLU141 |
| F | HIS142 |
| F | B12300 |
| site_id | AD4 |
| Number of Residues | 27 |
| Details | binding site for residue B12 G 300 |
| Chain | Residue |
| G | LEU121 |
| G | LEU124 |
| G | ARG125 |
| G | GLY128 |
| G | TRP131 |
| G | HIS132 |
| G | GLU141 |
| G | HIS142 |
| G | SER145 |
| G | GLY174 |
| G | GLU175 |
| G | ARG176 |
| G | HIS177 |
| G | GLU178 |
| G | ILE179 |
| G | GLY180 |
| G | VAL220 |
| G | LEU221 |
| G | SER222 |
| G | VAL224 |
| G | LEU225 |
| G | GLY247 |
| G | GLY248 |
| G | GLN249 |
| G | MET264 |
| G | LEU267 |
| G | 5AD301 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue 5AD G 301 |
| Chain | Residue |
| G | TRP131 |
| G | VAL138 |
| G | GLU141 |
| G | HIS142 |
| G | B12300 |
| H | ASP201 |
| H | PRO203 |
| site_id | AD6 |
| Number of Residues | 28 |
| Details | binding site for residue B12 H 300 |
| Chain | Residue |
| H | LEU121 |
| H | LEU124 |
| H | ARG125 |
| H | GLY128 |
| H | TRP131 |
| H | HIS132 |
| H | GLU141 |
| H | HIS142 |
| H | SER145 |
| H | GLY174 |
| H | GLU175 |
| H | ARG176 |
| H | HIS177 |
| H | GLU178 |
| H | ILE179 |
| H | GLY180 |
| H | LEU183 |
| H | VAL220 |
| H | SER222 |
| H | VAL224 |
| H | LEU225 |
| H | GLY247 |
| H | GLY248 |
| H | GLN249 |
| H | MET264 |
| H | ASP266 |
| H | LEU267 |
| H | 5AD301 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue 5AD H 301 |
| Chain | Residue |
| G | ASP201 |
| G | PRO203 |
| H | TRP131 |
| H | VAL138 |
| H | GLU141 |
| H | HIS142 |
| H | B12300 |
