Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003847 | molecular_function | 1-alkyl-2-acetylglycerophosphocholine esterase activity |
B | 0003847 | molecular_function | 1-alkyl-2-acetylglycerophosphocholine esterase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue BWL B 501 |
Chain | Residue |
B | PHE110 |
B | PHE357 |
B | LEU371 |
B | LEU121 |
B | LEU153 |
B | SER273 |
B | PHE274 |
B | TRP298 |
B | PHE322 |
B | HIS351 |
B | GLN352 |
Functional Information from PROSITE/UniProt
site_id | PS00120 |
Number of Residues | 10 |
Details | LIPASE_SER Lipases, serine active site. IAVIGHSFGG |
Chain | Residue | Details |
A | ILE267-GLY276 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18784071","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10037","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18784071","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |