7CRC
Cryo-EM structure of plant NLR RPP1 tetramer in complex with ATR1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006950 | biological_process | response to stress |
| A | 0006952 | biological_process | defense response |
| A | 0007165 | biological_process | signal transduction |
| A | 0043531 | molecular_function | ADP binding |
| B | 0006950 | biological_process | response to stress |
| B | 0006952 | biological_process | defense response |
| B | 0007165 | biological_process | signal transduction |
| B | 0043531 | molecular_function | ADP binding |
| C | 0006950 | biological_process | response to stress |
| C | 0006952 | biological_process | defense response |
| C | 0007165 | biological_process | signal transduction |
| C | 0043531 | molecular_function | ADP binding |
| D | 0006950 | biological_process | response to stress |
| D | 0006952 | biological_process | defense response |
| D | 0007165 | biological_process | signal transduction |
| D | 0043531 | molecular_function | ADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue ADP A 1301 |
| Chain | Residue |
| A | GLY258 |
| A | THR294 |
| A | THR295 |
| A | ILE427 |
| A | PRO457 |
| A | LYS461 |
| A | LEU259 |
| A | VAL260 |
| A | MET262 |
| A | PRO289 |
| A | GLY290 |
| A | ILE291 |
| A | GLY292 |
| A | LYS293 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue ADP B 1301 |
| Chain | Residue |
| A | GLU328 |
| B | LEU259 |
| B | VAL260 |
| B | PRO289 |
| B | GLY290 |
| B | GLY292 |
| B | LYS293 |
| B | THR294 |
| B | THR295 |
| B | ILE427 |
| B | PRO457 |
| B | LYS461 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue ATP B 1302 |
| Chain | Residue |
| A | PHE177 |
| A | ILE221 |
| A | ALA222 |
| A | GLY223 |
| A | HIS225 |
| B | PHE91 |
| B | HIS92 |
| B | GLY93 |
| B | ILE127 |
| B | LEU131 |
| B | SER152 |
| B | TRP154 |
| B | GLU158 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue ADP C 1301 |
| Chain | Residue |
| C | LEU259 |
| C | VAL260 |
| C | MET262 |
| C | PRO289 |
| C | GLY290 |
| C | ILE291 |
| C | GLY292 |
| C | LYS293 |
| C | THR294 |
| C | THR295 |
| C | ILE427 |
| C | PRO457 |
| C | LYS461 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue ADP D 1301 |
| Chain | Residue |
| D | LEU259 |
| D | VAL260 |
| D | PRO289 |
| D | GLY290 |
| D | GLY292 |
| D | LYS293 |
| D | THR294 |
| D | THR295 |
| D | ILE427 |
| D | PRO457 |
| D | LEU458 |
| D | LYS461 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue ATP D 1302 |
| Chain | Residue |
| C | PHE177 |
| C | ILE221 |
| C | ALA222 |
| C | GLY223 |
| C | HIS225 |
| D | PHE91 |
| D | GLY93 |
| D | ARG97 |
| D | TRP154 |
| D | CYS155 |
| D | GLU158 |
