5Z7R
Crystal structure of crotonase from Clostridium acetobutylicum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0018812 | molecular_function | 3-hydroxyacyl-CoA dehydratase activity |
| A | 0019605 | biological_process | butyrate metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0018812 | molecular_function | 3-hydroxyacyl-CoA dehydratase activity |
| B | 0019605 | biological_process | butyrate metabolic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0016836 | molecular_function | hydro-lyase activity |
| C | 0018812 | molecular_function | 3-hydroxyacyl-CoA dehydratase activity |
| C | 0019605 | biological_process | butyrate metabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaVNGfalGGGceiaMsCDI |
| Chain | Residue | Details |
| A | ILE101-ILE121 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q5LLW6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q5LLW6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
