4INE
Crystal structure of N-methyl transferase (PMT-2) from Caenorhabditis elegant complexed with S-adenosyl homocysteine and phosphoethanolamine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000234 | molecular_function | phosphoethanolamine N-methyltransferase activity |
A | 0000773 | molecular_function | phosphatidyl-N-methylethanolamine N-methyltransferase activity |
A | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008654 | biological_process | phospholipid biosynthetic process |
A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
A | 0032259 | biological_process | methylation |
A | 0052667 | molecular_function | phosphomethylethanolamine N-methyltransferase activity |
A | 0080101 | molecular_function | phosphatidyl-N-dimethylethanolamine N-methyltransferase activity |
B | 0000234 | molecular_function | phosphoethanolamine N-methyltransferase activity |
B | 0000773 | molecular_function | phosphatidyl-N-methylethanolamine N-methyltransferase activity |
B | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008654 | biological_process | phospholipid biosynthetic process |
B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
B | 0032259 | biological_process | methylation |
B | 0052667 | molecular_function | phosphomethylethanolamine N-methyltransferase activity |
B | 0080101 | molecular_function | phosphatidyl-N-dimethylethanolamine N-methyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE SAH A 501 |
Chain | Residue |
A | LEU182 |
A | MET259 |
A | THR280 |
A | ASP281 |
A | ALA282 |
A | ARG298 |
A | ASP299 |
A | CYS300 |
A | HIS303 |
A | HOH630 |
A | HOH634 |
A | TYR187 |
A | HOH635 |
A | HOH636 |
A | ILE204 |
A | SER205 |
A | GLY232 |
A | GLY234 |
A | ASP254 |
A | LEU255 |
A | SER256 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE OPE A 502 |
Chain | Residue |
A | GLN186 |
A | TYR187 |
A | TYR195 |
A | TYR329 |
A | TYR343 |
A | ARG347 |
A | TYR349 |
A | LYS415 |
A | HOH616 |
A | HOH640 |
A | HOH655 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME A 503 |
Chain | Residue |
A | CYS110 |
A | HOH719 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SAH B 501 |
Chain | Residue |
B | LEU182 |
B | TYR187 |
B | ILE204 |
B | SER205 |
B | GLY232 |
B | ASP254 |
B | LEU255 |
B | SER256 |
B | MET259 |
B | THR280 |
B | ASP281 |
B | ALA282 |
B | ARG298 |
B | ASP299 |
B | CYS300 |
B | HIS303 |
B | HOH611 |
B | HOH612 |
B | HOH617 |
B | HOH633 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE OPE B 502 |
Chain | Residue |
B | GLN186 |
B | TYR187 |
B | TYR195 |
B | TYR329 |
B | TYR343 |
B | ARG347 |
B | TYR349 |
B | LYS415 |
B | HOH607 |
B | HOH624 |
B | HOH636 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME B 503 |
Chain | Residue |
B | CYS110 |
B | HOH746 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000305|Ref.3, ECO:0007744|PDB:4INE |
Chain | Residue | Details |
A | ASN189 | |
B | GLN346 | |
B | PHE350 | |
B | TYR418 | |
A | MET198 | |
A | GLY332 | |
A | GLN346 | |
A | PHE350 | |
A | TYR418 | |
B | ASN189 | |
B | MET198 | |
B | GLY332 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|Ref.3, ECO:0007744|PDB:4INE |
Chain | Residue | Details |
A | GLY207 | |
B | ILE301 | |
A | ILE235 | |
A | SER257 | |
A | VAL284 | |
A | ILE301 | |
B | GLY207 | |
B | ILE235 | |
B | SER257 | |
B | VAL284 |