1RJF
Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005575 | cellular_component | cellular_component |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0010506 | biological_process | regulation of autophagy |
| A | 0018423 | molecular_function | protein C-terminal leucine carboxyl O-methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0065003 | biological_process | protein-containing complex assembly |
| B | 0005575 | cellular_component | cellular_component |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0010506 | biological_process | regulation of autophagy |
| B | 0018423 | molecular_function | protein C-terminal leucine carboxyl O-methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0065003 | biological_process | protein-containing complex assembly |
| C | 0005575 | cellular_component | cellular_component |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0010506 | biological_process | regulation of autophagy |
| C | 0018423 | molecular_function | protein C-terminal leucine carboxyl O-methyltransferase activity |
| C | 0032259 | biological_process | methylation |
| C | 0065003 | biological_process | protein-containing complex assembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 335 |
| Chain | Residue |
| A | CYS202 |
| A | PRO233 |
| A | TYR321 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME B 335 |
| Chain | Residue |
| B | CYS202 |
| B | PRO233 |
| B | TYR321 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME C 335 |
| Chain | Residue |
| C | CYS202 |
| C | TYR206 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME A 336 |
| Chain | Residue |
| A | SER14 |
| A | CYS15 |
| A | ALA66 |
| A | SER70 |
| A | MET74 |
| A | HOH357 |
| A | HOH381 |
| A | ASP11 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME B 336 |
| Chain | Residue |
| B | CYS15 |
| B | ALA66 |
| B | SER70 |
| B | MET74 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME C 336 |
| Chain | Residue |
| C | SER14 |
| C | CYS15 |
| C | ALA66 |
| C | SER70 |
| C | MET74 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 337 |
| Chain | Residue |
| A | MET74 |
| A | ARG81 |
| A | TYR231 |
| A | GLN318 |
| A | TYR321 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 338 |
| Chain | Residue |
| A | HIS121 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 15 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG81 | |
| B | GLU201 | |
| C | ARG81 | |
| C | GLY105 | |
| C | ASP128 | |
| C | ASP175 | |
| C | GLU201 | |
| A | GLY105 | |
| A | ASP128 | |
| A | ASP175 | |
| A | GLU201 | |
| B | ARG81 | |
| B | GLY105 | |
| B | ASP128 | |
| B | ASP175 |
