Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| A | 0106435 | molecular_function | carboxylesterase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 4PA A 369 |
| Chain | Residue |
| A | GLY92 |
| A | GLY93 |
| A | SER169 |
| A | ALA170 |
| A | TRP231 |
| A | HIS306 |
| A | HOH505 |
Functional Information from PROSITE/UniProt
| site_id | PS01173 |
| Number of Residues | 17 |
| Details | LIPASE_GDXG_HIS Lipolytic enzymes "G-D-X-G" family, putative histidine active site. VVyFHGGGFilfSaaST |
| Chain | Residue | Details |
| A | VAL86-THR102 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Motif: {"description":"Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole","evidences":[{"source":"UniProtKB","id":"Q5NUF3","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17256879","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2O7V","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"17256879","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2O7V","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1jkm |
| Chain | Residue | Details |
| A | HIS306 | |
| A | ASP276 | |
| A | SER169 | |
