5L2P
Structure of arylesterase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004063 | molecular_function | aryldialkylphosphatase activity |
| A | 0004064 | molecular_function | arylesterase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0004063 | molecular_function | aryldialkylphosphatase activity |
| B | 0004064 | molecular_function | arylesterase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0004063 | molecular_function | aryldialkylphosphatase activity |
| C | 0004064 | molecular_function | arylesterase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0004063 | molecular_function | aryldialkylphosphatase activity |
| D | 0004064 | molecular_function | arylesterase activity |
| D | 0016787 | molecular_function | hydrolase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"18931117","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
