8VCD
Crystal Structure of plant Carboxylesterase 15 bound to SL intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| A | 0106435 | molecular_function | carboxylesterase activity |
| A | 1901600 | biological_process | strigolactone metabolic process |
| A | 2000032 | biological_process | regulation of secondary shoot formation |
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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"39090154","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"39090154","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q5NUF3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"39090154","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"8VCD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
