4KRI
Haemonchus contortus Phospholethanolamine N-methyltransferase 2 in complex with phosphomonomethylethanolamine and S-adenosylhomocysteine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000234 | molecular_function | phosphoethanolamine N-methyltransferase activity |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent 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 | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| C | 0000234 | molecular_function | phosphoethanolamine N-methyltransferase activity |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0032259 | biological_process | methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH A 701 |
| Chain | Residue |
| A | TYR183 |
| A | MET255 |
| A | CYS276 |
| A | ASP277 |
| A | ALA278 |
| A | ARG294 |
| A | CYS296 |
| A | HIS299 |
| A | ILE300 |
| A | 1SH702 |
| A | HOH806 |
| A | ILE200 |
| A | HOH809 |
| A | HOH815 |
| A | HOH817 |
| A | SER201 |
| A | GLY228 |
| A | VAL229 |
| A | GLY230 |
| A | ASP250 |
| A | LEU251 |
| A | SER252 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 1SH A 702 |
| Chain | Residue |
| A | GLN182 |
| A | TYR183 |
| A | TYR191 |
| A | ILE200 |
| A | ASP295 |
| A | GLN298 |
| A | TYR325 |
| A | TYR339 |
| A | ARG343 |
| A | TYR345 |
| A | LYS411 |
| A | SAH701 |
| A | HOH862 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH B 701 |
| Chain | Residue |
| B | PHE174 |
| B | ILE200 |
| B | SER201 |
| B | GLY228 |
| B | VAL229 |
| B | GLY230 |
| B | ASP250 |
| B | LEU251 |
| B | SER252 |
| B | MET255 |
| B | CYS276 |
| B | ASP277 |
| B | ALA278 |
| B | ARG294 |
| B | CYS296 |
| B | HIS299 |
| B | ILE300 |
| B | 1SH702 |
| B | HOH802 |
| B | HOH812 |
| B | HOH824 |
| B | HOH863 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 1SH B 702 |
| Chain | Residue |
| B | GLN182 |
| B | TYR183 |
| B | TYR191 |
| B | ILE200 |
| B | ASP295 |
| B | GLN298 |
| B | TYR325 |
| B | TYR339 |
| B | ARG343 |
| B | TYR345 |
| B | LYS411 |
| B | SAH701 |
| B | HOH815 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAH C 701 |
| Chain | Residue |
| C | PHE174 |
| C | ILE200 |
| C | SER201 |
| C | GLY228 |
| C | VAL229 |
| C | GLY230 |
| C | ASP250 |
| C | LEU251 |
| C | SER252 |
| C | MET255 |
| C | CYS276 |
| C | ASP277 |
| C | ALA278 |
| C | ARG294 |
| C | CYS296 |
| C | HIS299 |
| C | 1SH702 |
| C | HOH803 |
| C | HOH810 |
| C | HOH813 |
| C | HOH831 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1SH C 702 |
| Chain | Residue |
| C | TYR345 |
| C | LYS411 |
| C | SAH701 |
| C | HOH843 |
| C | GLN182 |
| C | TYR183 |
| C | TYR191 |
| C | ILE200 |
| C | ASP295 |
| C | TYR325 |
| C | TYR339 |
| C | ARG343 |
