4R6X
Plasmodium falciparum phosphoethanolamine methyltransferase D128A mutant in complex with S-adenosylhomocysteine and phosphoethanolamine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000139 | cellular_component | Golgi membrane |
| A | 0000234 | molecular_function | phosphoethanolamine N-methyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0032259 | biological_process | methylation |
| A | 0052667 | molecular_function | phosphomethylethanolamine N-methyltransferase activity |
| B | 0000139 | cellular_component | Golgi membrane |
| B | 0000234 | molecular_function | phosphoethanolamine N-methyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008654 | biological_process | phospholipid biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0032259 | biological_process | methylation |
| B | 0052667 | molecular_function | phosphomethylethanolamine N-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OPE A 501 |
| Chain | Residue |
| A | GLN18 |
| A | HOH624 |
| A | TYR27 |
| A | ILE36 |
| A | TYR160 |
| A | TYR175 |
| A | ARG179 |
| A | TYR181 |
| A | LYS247 |
| A | HOH616 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SAH A 502 |
| Chain | Residue |
| A | LEU14 |
| A | TYR19 |
| A | TYR35 |
| A | ILE36 |
| A | SER37 |
| A | GLY63 |
| A | SER64 |
| A | ASP85 |
| A | ILE86 |
| A | CYS87 |
| A | ILE90 |
| A | ASN109 |
| A | ASP110 |
| A | ILE111 |
| A | ARG127 |
| A | ALA128 |
| A | ALA129 |
| A | HIS132 |
| A | LEU133 |
| A | HOH604 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OPE B 501 |
| Chain | Residue |
| B | GLN18 |
| B | TYR27 |
| B | ILE36 |
| B | TYR160 |
| B | TYR175 |
| B | ARG179 |
| B | TYR181 |
| B | LYS247 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAH B 502 |
| Chain | Residue |
| B | LEU14 |
| B | TYR19 |
| B | TYR35 |
| B | ILE36 |
| B | SER37 |
| B | GLY63 |
| B | SER64 |
| B | GLY65 |
| B | ASP85 |
| B | ILE86 |
| B | CYS87 |
| B | ASP110 |
| B | ILE111 |
| B | ARG127 |
| B | ALA128 |
| B | ALA129 |
| B | HIS132 |
| B | LEU133 |
| B | HOH602 |
| B | HOH614 |
| B | HOH625 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:22117061 |
| Chain | Residue | Details |
| A | TYR19 | |
| A | HIS132 | |
| B | TYR19 | |
| B | HIS132 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22117061, ECO:0000269|PubMed:25288796, ECO:0007744|PDB:3UJ9, ECO:0007744|PDB:3UJA, ECO:0007744|PDB:3UJB, ECO:0007744|PDB:3UJC, ECO:0007744|PDB:3UJD, ECO:0007744|PDB:4R6W |
| Chain | Residue | Details |
| A | GLN18 | |
| B | TYR160 | |
| B | TYR175 | |
| B | ARG179 | |
| B | TYR181 | |
| B | LYS247 | |
| A | TYR27 | |
| A | TYR160 | |
| A | TYR175 | |
| A | ARG179 | |
| A | TYR181 | |
| A | LYS247 | |
| B | GLN18 | |
| B | TYR27 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22117061, ECO:0000269|PubMed:22771008, ECO:0000269|PubMed:25288796, ECO:0007744|PDB:3UJ6, ECO:0007744|PDB:3UJ7, ECO:0007744|PDB:3UJB, ECO:0007744|PDB:4FGZ, ECO:0007744|PDB:4R6W, ECO:0007744|PDB:4R6X |
| Chain | Residue | Details |
| A | ILE36 | |
| B | SER37 | |
| B | GLY63 | |
| B | ASP85 | |
| B | ILE86 | |
| B | ASP110 | |
| B | ILE111 | |
| B | ARG127 | |
| A | SER37 | |
| A | GLY63 | |
| A | ASP85 | |
| A | ILE86 | |
| A | ASP110 | |
| A | ILE111 | |
| A | ARG127 | |
| B | ILE36 |
