3LBF
Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004719 | molecular_function | protein-L-isoaspartate (D-aspartate) O-methyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030091 | biological_process | protein repair |
| A | 0032259 | biological_process | methylation |
| A | 0036211 | biological_process | protein modification process |
| B | 0004719 | molecular_function | protein-L-isoaspartate (D-aspartate) O-methyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030091 | biological_process | protein repair |
| B | 0032259 | biological_process | methylation |
| B | 0036211 | biological_process | protein modification process |
| C | 0004719 | molecular_function | protein-L-isoaspartate (D-aspartate) O-methyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030091 | biological_process | protein repair |
| C | 0032259 | biological_process | methylation |
| C | 0036211 | biological_process | protein modification process |
| D | 0004719 | molecular_function | protein-L-isoaspartate (D-aspartate) O-methyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030091 | biological_process | protein repair |
| D | 0032259 | biological_process | methylation |
| D | 0036211 | biological_process | protein modification process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE SAH A 300 |
| Chain | Residue |
| A | GLN56 |
| A | GLU104 |
| A | ARG105 |
| A | ILE106 |
| A | LEU109 |
| A | GLY130 |
| A | ASP131 |
| A | GLY132 |
| A | THR148 |
| A | LEU202 |
| A | VAL203 |
| A | THR57 |
| A | HOH219 |
| A | HOH236 |
| A | HOH251 |
| A | HOH272 |
| A | HOH273 |
| A | GLY83 |
| A | THR84 |
| A | GLY85 |
| A | SER86 |
| A | TYR88 |
| A | GLN89 |
| A | VAL103 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 209 |
| Chain | Residue |
| A | LYS107 |
| A | HIS129 |
| A | HOH234 |
| C | SER126 |
| C | ARG139 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 210 |
| Chain | Residue |
| A | PO4211 |
| A | HOH260 |
| A | HOH429 |
| B | LYS107 |
| B | HIS129 |
| B | PO4210 |
| C | TRP111 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 211 |
| Chain | Residue |
| A | HIS99 |
| A | SER126 |
| A | ARG139 |
| A | PO4210 |
| B | LYS107 |
| B | GLN110 |
| B | ARG128 |
| B | HIS129 |
| B | HOH221 |
| B | HOH246 |
| B | HOH380 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 212 |
| Chain | Residue |
| A | PRO152 |
| A | GLU153 |
| A | HOH223 |
| A | HOH285 |
| B | TRP133 |
| B | PRO155 |
| B | THR156 |
| B | ALA157 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE SAH B 300 |
| Chain | Residue |
| B | GLN56 |
| B | THR57 |
| B | GLY83 |
| B | THR84 |
| B | GLY85 |
| B | SER86 |
| B | TYR88 |
| B | GLN89 |
| B | VAL103 |
| B | GLU104 |
| B | ARG105 |
| B | ILE106 |
| B | LEU109 |
| B | GLY130 |
| B | ASP131 |
| B | GLY132 |
| B | THR148 |
| B | PRO201 |
| B | LEU202 |
| B | VAL203 |
| B | HOH212 |
| B | HOH215 |
| B | HOH250 |
| B | HOH252 |
| B | HOH288 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 209 |
| Chain | Residue |
| A | TRP136 |
| A | ALA138 |
| A | ARG139 |
| B | LYS107 |
| B | ARG114 |
| B | PO4210 |
| C | LYS107 |
| C | PO4209 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 210 |
| Chain | Residue |
| A | PO4210 |
| B | LYS107 |
| B | PO4209 |
| C | LYS107 |
| C | ARG114 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE SAH C 300 |
| Chain | Residue |
| C | TYR88 |
| C | GLN89 |
| C | VAL103 |
| C | GLU104 |
| C | ARG105 |
| C | ILE106 |
| C | LEU109 |
| C | GLY130 |
| C | ASP131 |
| C | GLY132 |
| C | THR148 |
| C | VAL200 |
| C | PRO201 |
| C | LEU202 |
| C | VAL203 |
| C | HOH212 |
| C | HOH214 |
| C | HOH221 |
| C | HOH243 |
| C | GLN56 |
| C | THR57 |
| C | GLY83 |
| C | THR84 |
| C | GLY85 |
| C | SER86 |
| site_id | BC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SAH D 300 |
| Chain | Residue |
| D | GLN56 |
| D | GLY83 |
| D | THR84 |
| D | GLY85 |
| D | SER86 |
| D | TYR88 |
| D | GLN89 |
| D | GLU104 |
| D | ARG105 |
| D | ILE106 |
| D | GLY130 |
| D | ASP131 |
| D | GLY132 |
| D | TRP133 |
| D | THR148 |
| D | VAL200 |
| D | LEU202 |
| D | VAL203 |
| D | HOH237 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 C 209 |
| Chain | Residue |
| A | ARG128 |
| A | TRP136 |
| A | ALA138 |
| A | HOH270 |
| B | TRP111 |
| B | PO4209 |
| C | LYS107 |
| C | HIS129 |
| C | HOH215 |
| C | HOH397 |
Functional Information from PROSITE/UniProt
| site_id | PS01279 |
| Number of Residues | 16 |
| Details | PCMT Protein-L-isoaspartate(D-aspartate) O-methyltransferase signature. GDGwqGWqarAPFDaI |
| Chain | Residue | Details |
| A | GLY130-ILE145 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
