Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004104 | molecular_function | cholinesterase activity |
| B | 0004104 | molecular_function | cholinesterase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00122 |
| Number of Residues | 16 |
| Details | CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpsrVtLfGeSAG |
| Chain | Residue | Details |
| A | PHE347-GLY362 | |
| site_id | PS00941 |
| Number of Residues | 11 |
| Details | CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYINVVaP |
| Chain | Residue | Details |
| A | GLU253-PRO263 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10039","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |