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 | 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 | 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 | 0000773 | molecular_function | phosphatidyl-N-methylethanolamine N-methyltransferase activity |
| 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 | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
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 | 14 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JAN-2013","submissionDatabase":"PDB data bank","title":"Crystal structure of N-methyl transferase (PMT-2) from Caenorhabditis elegant complexed with S-adenosyl homocysteine and phosphoethanolamine.","authors":["Lukk T.","Nair S.K."]}},{"source":"PDB","id":"4INE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2013","submissionDatabase":"PDB data bank","title":"Crystal structure of N-methyl transferase (PMT-2) from Caenorhabditis elegant complexed with S-adenosyl homocysteine and phosphoethanolamine.","authors":["Lukk T.","Nair S.K."]}},{"source":"PDB","id":"4INE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
