5WP5
Arabidopsis thaliana phosphoethanolamine N-methyltransferase 2 (AtPMT2) in complex with SAH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000234 | molecular_function | phosphoethanolamine N-methyltransferase activity |
| A | 0003729 | molecular_function | mRNA binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008170 | molecular_function | N-methyltransferase activity |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| B | 0000234 | molecular_function | phosphoethanolamine N-methyltransferase activity |
| B | 0003729 | molecular_function | mRNA binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008170 | molecular_function | N-methyltransferase activity |
| B | 0008654 | biological_process | phospholipid biosynthetic process |
| 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 SAH A 501 |
| Chain | Residue |
| A | VAL263 |
| A | CYS339 |
| A | ARG355 |
| A | ASP356 |
| A | THR357 |
| A | HIS360 |
| A | HOH663 |
| A | HOH750 |
| A | HOH787 |
| A | HOH795 |
| A | HOH851 |
| A | SER264 |
| A | HOH855 |
| A | GLY290 |
| A | GLY292 |
| A | ASP312 |
| A | LEU313 |
| A | MET317 |
| A | ALA337 |
| A | ASP338 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue SAH A 502 |
| Chain | Residue |
| A | ARG9 |
| A | TRP16 |
| A | GLY61 |
| A | GLY63 |
| A | ARG66 |
| A | PHE67 |
| A | ASP82 |
| A | PHE83 |
| A | ILE84 |
| A | ALA106 |
| A | ASP107 |
| A | VAL108 |
| A | ASN126 |
| A | TRP127 |
| A | HOH622 |
| A | HOH653 |
| A | HOH749 |
| A | HOH849 |
| A | HOH934 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue SAH B 701 |
| Chain | Residue |
| B | ARG9 |
| B | TRP16 |
| B | GLY61 |
| B | GLY63 |
| B | ARG66 |
| B | PHE67 |
| B | ASP82 |
| B | PHE83 |
| B | ILE84 |
| B | ALA106 |
| B | ASP107 |
| B | VAL108 |
| B | ASN126 |
| B | TRP127 |
| B | HOH845 |
| B | HOH849 |
| B | HOH921 |
| B | HOH993 |
| B | HOH1062 |
| B | HOH1141 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue SAH B 702 |
| Chain | Residue |
| B | VAL263 |
| B | SER264 |
| B | GLY290 |
| B | GLY292 |
| B | ASP312 |
| B | LEU313 |
| B | MET317 |
| B | ALA337 |
| B | ASP338 |
| B | CYS339 |
| B | ARG355 |
| B | ASP356 |
| B | THR357 |
| B | HIS360 |
| B | ILE361 |
| B | HOH878 |
| B | HOH949 |
| B | HOH994 |
| B | HOH1013 |
| B | HOH1060 |
| B | HOH1061 |
| B | HOH1085 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 26 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29084845, ECO:0007744|PDB:5WP5 |
| Chain | Residue | Details |
| A | GLY61 | |
| A | ASP312 | |
| A | ASP338 | |
| A | CYS339 | |
| A | THR357 | |
| B | GLY61 | |
| B | ARG66 | |
| B | ASP82 | |
| B | ASP107 | |
| B | VAL108 | |
| B | ASN126 | |
| A | ARG66 | |
| B | VAL263 | |
| B | SER264 | |
| B | GLY290 | |
| B | ASP312 | |
| B | ASP338 | |
| B | CYS339 | |
| B | THR357 | |
| A | ASP82 | |
| A | ASP107 | |
| A | VAL108 | |
| A | ASN126 | |
| A | VAL263 | |
| A | SER264 | |
| A | GLY290 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9FR44 |
| Chain | Residue | Details |
| A | SER159 | |
| A | TYR406 | |
| A | LYS472 | |
| B | SER159 | |
| B | SER164 | |
| B | GLY165 | |
| B | ARG169 | |
| B | TYR176 | |
| B | TYR254 | |
| B | TYR386 | |
| B | TYR400 | |
| A | SER164 | |
| B | ARG404 | |
| B | TYR406 | |
| B | LYS472 | |
| A | GLY165 | |
| A | ARG169 | |
| A | TYR176 | |
| A | TYR254 | |
| A | TYR386 | |
| A | TYR400 | |
| A | ARG404 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q22993 |
| Chain | Residue | Details |
| A | GLN245 | |
| A | ARG355 | |
| B | GLN245 | |
| B | ARG355 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:Q9FR44 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
