Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016829 | molecular_function | lyase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016829 | molecular_function | lyase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0016829 | molecular_function | lyase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 301 |
| Chain | Residue |
| A | PHE152 |
| A | SER153 |
| A | HOH402 |
| C | LYS148 |
| C | LYS149 |
| C | PRO176 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | LEU8 |
| A | GLU10 |
| A | HOH499 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 301 |
| Chain | Residue |
| B | LYS148 |
| B | LYS149 |
| C | PHE152 |
| C | SER153 |
| C | HOH407 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| A | ASP117 |
| A | ILE118 |
| A | VAL119 |
| A | PRO176 |
| A | HOH416 |
| B | SER153 |
| B | LEU154 |
| B | GLN156 |
| B | GLU157 |
| B | ARG173 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 303 |
| Chain | Residue |
| B | LEU8 |
| B | GLU10 |
| B | HOH478 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 304 |
| Chain | Residue |
| B | TYR188 |
| B | GLU191 |
| B | GLU195 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 305 |
| Chain | Residue |
| B | ILE74 |
| B | PHE131 |
| B | PHE136 |
| B | GLY139 |
| B | MET140 |
| B | HIS230 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 306 |
| Chain | Residue |
| B | VAL6 |
| B | LEU8 |
| B | GLN39 |
| B | ALA40 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 301 |
| Chain | Residue |
| B | LYS178 |
| B | TYR188 |
| C | ARG173 |
Functional Information from PROSITE/UniProt
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaMQGhgiGGGfvmgLfADI |
| Chain | Residue | Details |
| A | ILE98-ILE118 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"32948786","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Q1K","evidenceCode":"ECO:0007744"}]} |
