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. FGGdpmsVtLfGeSAG |
| Chain | Residue | Details |
| A | PHE190-GLY205 | |
| site_id | PS00941 |
| Number of Residues | 11 |
| Details | CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWtP |
| Chain | Residue | Details |
| A | GLU94-PRO104 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-ester intermediate"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qe3 |
| Chain | Residue | Details |
| A | GLU334 | |
| A | HIS447 | |
| A | SER203 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1qe3 |
| Chain | Residue | Details |
| B | GLU334 | |
| B | HIS447 | |
| B | SER203 | |