Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE VXA A 400 |
| Chain | Residue |
| A | SER14 |
| A | GLY66 |
| A | ASN106 |
| A | HIS283 |
| site_id | S1 |
| Number of Residues | 2 |
| Details | |
| Chain | Residue |
| A | SER14 |
| A | HIS283 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1esc |
| Chain | Residue | Details |
| A | TRP280 | |
| A | SER14 | |
| A | HIS283 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 556 |
| Chain | Residue | Details |
| A | SER14 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY66 | electrostatic stabiliser |
| A | ASN106 | electrostatic stabiliser, modifies pKa |
| A | HIS283 | electrostatic stabiliser, proton acceptor, proton donor |
