4R6W
Plasmodium falciparum phosphoethanolamine methyltransferase D128A mutant in complex with S-adenosylhomocysteine and phosphocholine
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 | 0009058 | biological_process | biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0032259 | biological_process | methylation |
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 | 0009058 | biological_process | biosynthetic process |
B | 0016020 | cellular_component | membrane |
B | 0032259 | biological_process | methylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PC A 301 |
Chain | Residue |
A | GLN18 |
A | LYS247 |
A | SAH302 |
A | HOH437 |
A | TYR19 |
A | TYR27 |
A | ILE36 |
A | ALA128 |
A | TYR160 |
A | TYR175 |
A | ARG179 |
A | TYR181 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE SAH A 302 |
Chain | Residue |
A | TYR19 |
A | ILE36 |
A | SER37 |
A | GLY63 |
A | GLY65 |
A | ASP85 |
A | ILE86 |
A | CYS87 |
A | ILE90 |
A | ASN109 |
A | ASP110 |
A | ILE111 |
A | ARG127 |
A | ALA128 |
A | ALA129 |
A | HIS132 |
A | PC301 |
A | HOH408 |
A | HOH443 |
A | HOH469 |
A | HOH471 |
A | HOH577 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PC B 301 |
Chain | Residue |
B | GLN18 |
B | TYR19 |
B | TYR27 |
B | ILE36 |
B | ALA128 |
B | TYR160 |
B | TYR175 |
B | ARG179 |
B | TYR181 |
B | LYS247 |
B | SAH302 |
B | HOH409 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SAH B 302 |
Chain | Residue |
B | TYR19 |
B | ILE36 |
B | SER37 |
B | GLY63 |
B | GLY65 |
B | ASP85 |
B | ILE86 |
B | CYS87 |
B | ASN109 |
B | ASP110 |
B | ILE111 |
B | ARG127 |
B | ALA128 |
B | ALA129 |
B | PC301 |
B | HOH420 |
B | HOH448 |
B | HOH464 |
B | HOH485 |
B | HOH629 |
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 |