Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 601 |
| Chain | Residue |
| A | HIS168 |
| A | GLU342 |
| A | ACT610 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 602 |
| Chain | Residue |
| A | ASP79 |
| A | HIS487 |
| A | GLU489 |
| A | ACT609 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 603 |
| Chain | Residue |
| A | ASP476 |
| A | ASP77 |
| A | GLU78 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 604 |
| Chain | Residue |
| A | MET281 |
| A | ASP328 |
| A | PHE351 |
| A | GLU388 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 605 |
| Chain | Residue |
| A | HIS48 |
| A | ACT611 |
| A | HOH716 |
| A | HOH730 |
| A | HOH798 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue ZN A 606 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 607 |
| Chain | Residue |
| A | HIS322 |
| A | ASP434 |
| A | ACT612 |
| A | HOH805 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 608 |
| Chain | Residue |
| A | GLY107 |
| A | ALA108 |
| A | PHE109 |
| A | LEU110 |
| A | SER194 |
| A | ALA195 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue ACT A 609 |
| Chain | Residue |
| A | ASP77 |
| A | ASP79 |
| A | HIS487 |
| A | GLU489 |
| A | PRO490 |
| A | ZN602 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue ACT A 610 |
| Chain | Residue |
| A | HIS168 |
| A | TYR208 |
| A | GLU341 |
| A | GLU342 |
| A | ZN601 |
| A | HOH703 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 611 |
| Chain | Residue |
| A | HIS48 |
| A | TYR82 |
| A | ZN605 |
| A | HOH716 |
| A | HOH730 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 612 |
| Chain | Residue |
| A | HIS322 |
| A | ILE323 |
| A | ASP434 |
| A | ZN607 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 613 |
| Chain | Residue |
| A | GLY315 |
| A | THR316 |
| A | LEU394 |
| A | THR397 |
| A | GLU398 |
| A | LEU401 |
| A | TYR416 |
| A | TYR498 |
| A | LEU514 |
Functional Information from PROSITE/UniProt
| site_id | PS00122 |
| Number of Residues | 16 |
| Details | CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpdnItLfGeSAG |
| Chain | Residue | Details |
| A | PHE181-GLY196 | |
| site_id | PS00941 |
| Number of Residues | 11 |
| Details | CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIWvP |
| Chain | Residue | Details |
| A | GLU78-PRO88 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | SER194 | |
| Chain | Residue | Details |
| A | ASP320 | |
| A | HIS435 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine |
| Chain | Residue | Details |
| A | ASN187 | |
