1RJD
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 | 7 |
Details | BINDING SITE FOR RESIDUE SO4 C 335 |
Chain | Residue |
C | ARG192 |
C | SER224 |
C | HIS330 |
C | HIS331 |
C | HIS332 |
C | HIS333 |
C | HIS334 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE SAM A 801 |
Chain | Residue |
A | THR8 |
A | ASP9 |
A | ALA12 |
A | ARG81 |
A | GLY105 |
A | CYS106 |
A | GLY107 |
A | ASP128 |
A | TYR129 |
A | CYS174 |
A | ASP175 |
A | LEU176 |
A | ASN177 |
A | GLU201 |
A | CYS202 |
A | LEU203 |
A | HOH810 |
A | HOH811 |
A | HOH838 |
A | HOH864 |
A | HOH913 |
A | HOH1010 |
A | ILE5 |
A | GLN6 |
site_id | AC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE SAM B 802 |
Chain | Residue |
B | ILE5 |
B | GLN6 |
B | THR8 |
B | ASP9 |
B | ALA12 |
B | ARG81 |
B | GLY105 |
B | CYS106 |
B | GLY107 |
B | ASP128 |
B | TYR129 |
B | CYS174 |
B | ASP175 |
B | LEU176 |
B | ASN177 |
B | GLU201 |
B | CYS202 |
B | LEU203 |
B | TYR206 |
B | HOH809 |
B | HOH811 |
B | HOH823 |
B | HOH847 |
B | HOH863 |
B | HOH877 |
site_id | AC4 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE SAM C 803 |
Chain | Residue |
C | ILE5 |
C | GLN6 |
C | THR8 |
C | ALA12 |
C | ARG81 |
C | GLY105 |
C | CYS106 |
C | GLY107 |
C | ASP128 |
C | TYR129 |
C | CYS174 |
C | ASP175 |
C | LEU176 |
C | ASN177 |
C | GLU201 |
C | CYS202 |
C | LEU203 |
C | TYR206 |
C | HOH824 |
C | HOH826 |
C | HOH846 |
C | HOH869 |
C | HOH912 |
C | HOH949 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME A 804 |
Chain | Residue |
A | CYS202 |
A | TYR206 |
A | PRO233 |
A | MET259 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME B 805 |
Chain | Residue |
B | CYS202 |
B | TYR206 |
B | PRO233 |
B | HOH978 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME C 806 |
Chain | Residue |
C | CYS202 |
C | TYR206 |
C | PRO233 |
C | MET259 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME A 807 |
Chain | Residue |
A | SER14 |
A | CYS15 |
A | ALA66 |
A | SER70 |
A | HOH960 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME B 808 |
Chain | Residue |
B | SER70 |
B | MET74 |
B | CYS15 |
B | ALA66 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME C 809 |
Chain | Residue |
C | CYS15 |
C | ALA66 |
C | SER70 |
C | MET74 |
C | HOH1026 |
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 |