6XGT
Crystal structure of cyanase from the thermophilic fungus Thermomyces lanuginosus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0008824 | molecular_function | cyanate hydratase activity |
| A | 0009440 | biological_process | cyanate catabolic process |
| B | 0003677 | molecular_function | DNA binding |
| B | 0008824 | molecular_function | cyanate hydratase activity |
| B | 0009440 | biological_process | cyanate catabolic process |
| C | 0003677 | molecular_function | DNA binding |
| C | 0008824 | molecular_function | cyanate hydratase activity |
| C | 0009440 | biological_process | cyanate catabolic process |
| D | 0003677 | molecular_function | DNA binding |
| D | 0008824 | molecular_function | cyanate hydratase activity |
| D | 0009440 | biological_process | cyanate catabolic process |
| E | 0003677 | molecular_function | DNA binding |
| E | 0008824 | molecular_function | cyanate hydratase activity |
| E | 0009440 | biological_process | cyanate catabolic process |
| F | 0003677 | molecular_function | DNA binding |
| F | 0008824 | molecular_function | cyanate hydratase activity |
| F | 0009440 | biological_process | cyanate catabolic process |
| G | 0003677 | molecular_function | DNA binding |
| G | 0008824 | molecular_function | cyanate hydratase activity |
| G | 0009440 | biological_process | cyanate catabolic process |
| H | 0003677 | molecular_function | DNA binding |
| H | 0008824 | molecular_function | cyanate hydratase activity |
| H | 0009440 | biological_process | cyanate catabolic process |
| I | 0003677 | molecular_function | DNA binding |
| I | 0008824 | molecular_function | cyanate hydratase activity |
| I | 0009440 | biological_process | cyanate catabolic process |
| J | 0003677 | molecular_function | DNA binding |
| J | 0008824 | molecular_function | cyanate hydratase activity |
| J | 0009440 | biological_process | cyanate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue FMT E 201 |
| Chain | Residue |
| E | SER127 |
| E | ALA128 |
| E | ILE129 |
| F | ARG101 |
| I | FMT201 |
| J | ARG101 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue MLI G 201 |
| Chain | Residue |
| F | ALA128 |
| F | ILE129 |
| F | LEU156 |
| G | ILE125 |
| G | SER127 |
| G | ALA128 |
| G | ILE129 |
| G | LEU156 |
| H | ARG101 |
| E | ARG101 |
| F | ILE125 |
| F | SER127 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue MLI A 201 |
| Chain | Residue |
| A | ILE125 |
| A | SER127 |
| A | ALA128 |
| A | ILE129 |
| A | LEU156 |
| D | ARG101 |
| G | ARG101 |
| H | ILE125 |
| H | SER127 |
| H | ALA128 |
| H | ILE129 |
| H | LEU156 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue MLI D 201 |
| Chain | Residue |
| A | ARG101 |
| B | ILE125 |
| B | SER127 |
| B | ALA128 |
| B | LEU156 |
| C | ARG101 |
| D | ILE125 |
| D | SER127 |
| D | ALA128 |
| D | ILE129 |
| D | LEU156 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue FMT I 201 |
| Chain | Residue |
| E | FMT201 |
| F | ARG101 |
| I | SER127 |
| I | ALA128 |
| I | ILE129 |
| I | LEU156 |
| J | ARG101 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue FMT J 201 |
| Chain | Residue |
| B | ARG101 |
| C | FMT201 |
| I | ARG101 |
| J | ILE125 |
| J | SER127 |
| J | ALA128 |
| J | ILE129 |
| J | LEU156 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue FMT C 201 |
| Chain | Residue |
| B | ARG101 |
| C | ILE125 |
| C | SER127 |
| C | ALA128 |
| C | LEU156 |
| I | ARG101 |
| J | FMT201 |
