Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0000234 | molecular_function | phosphoethanolamine N-methyltransferase activity | 
| A | 0008168 | molecular_function | methyltransferase activity | 
| A | 0016740 | molecular_function | transferase activity | 
| A | 0032259 | biological_process | methylation | 
| B | 0000234 | molecular_function | phosphoethanolamine N-methyltransferase activity | 
| B | 0008168 | molecular_function | methyltransferase activity | 
| B | 0016740 | molecular_function | transferase activity | 
| B | 0032259 | biological_process | methylation | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 20 | 
| Details | BINDING SITE FOR RESIDUE SAM A 301 | 
| Chain | Residue | 
| A | TYR16 | 
| A | ARG124 | 
| A | ASP125 | 
| A | SER126 | 
| A | HIS129 | 
| A | HOH410 | 
| A | HOH412 | 
| A | HOH423 | 
| A | HOH593 | 
| A | HOH598 | 
| A | HOH611 | 
| A | ILE33 | 
| A | HOH619 | 
| A | SER34 | 
| A | GLY60 | 
| A | ASP82 | 
| A | ILE83 | 
| A | MET87 | 
| A | ASP107 | 
| A | ILE108 | 
| site_id | AC2 | 
| Number of Residues | 9 | 
| Details | BINDING SITE FOR RESIDUE PO4 A 302 | 
| Chain | Residue | 
| A | GLN15 | 
| A | TYR24 | 
| A | TYR157 | 
| A | TYR172 | 
| A | ARG176 | 
| A | TYR178 | 
| A | LYS244 | 
| A | HOH426 | 
| A | HOH454 | 
| site_id | AC3 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE BME A 303 | 
| Chain | Residue | 
| A | TYR16 | 
| A | GLN49 | 
| A | CYS84 | 
| A | HOH598 | 
| site_id | AC4 | 
| Number of Residues | 20 | 
| Details | BINDING SITE FOR RESIDUE SAM B 301 | 
| Chain | Residue | 
| B | TYR16 | 
| B | ILE33 | 
| B | SER34 | 
| B | GLY60 | 
| B | ASP82 | 
| B | ILE83 | 
| B | CYS84 | 
| B | MET87 | 
| B | ASP107 | 
| B | ILE108 | 
| B | ARG124 | 
| B | ASP125 | 
| B | SER126 | 
| B | HIS129 | 
| B | LEU130 | 
| B | BME304 | 
| B | HOH402 | 
| B | HOH404 | 
| B | HOH413 | 
| B | HOH427 | 
| site_id | AC5 | 
| Number of Residues | 9 | 
| Details | BINDING SITE FOR RESIDUE PO4 B 302 | 
| Chain | Residue | 
| B | GLN15 | 
| B | TYR24 | 
| B | TYR157 | 
| B | TYR172 | 
| B | ARG176 | 
| B | TYR178 | 
| B | LYS244 | 
| B | HOH417 | 
| B | HOH425 | 
| site_id | AC6 | 
| Number of Residues | 16 | 
| Details | BINDING SITE FOR RESIDUE CQA B 303 | 
| Chain | Residue | 
| B | SER3 | 
| B | GLU4 | 
| B | PHE28 | 
| B | GLY29 | 
| B | GLY36 | 
| B | ILE39 | 
| B | TYR132 | 
| B | GLU185 | 
| B | GLU209 | 
| B | LEU210 | 
| B | LEU213 | 
| B | GLU214 | 
| B | LYS217 | 
| B | HOH418 | 
| B | HOH546 | 
| B | HOH662 | 
| site_id | AC7 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE BME B 304 | 
| Chain | Residue | 
| B | ILE8 | 
| B | LEU11 | 
| B | GLU12 | 
| B | TYR16 | 
| B | ILE83 | 
| B | CYS84 | 
| B | SAM301 | 
Functional Information from PROSITE/UniProt
| site_id | PS00107 | 
| Number of Residues | 34 | 
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGLGGGCKyInekygahvhgvdicekmvTIAK | 
| Chain | Residue | Details | 
| A | ILE59-LYS92 |  |