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 GOL A 301 |
Chain | Residue |
A | HIS210 |
A | LEU211 |
A | PRO214 |
A | HOH438 |
A | HOH496 |
C | THR143 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 302 |
Chain | Residue |
B | HIS210 |
B | PRO214 |
B | HOH461 |
A | THR143 |
A | HOH536 |
A | HOH572 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 303 |
Chain | Residue |
A | TYR188 |
A | GLU191 |
A | LEU192 |
A | GLU195 |
B | HIS235 |
C | EPE301 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 304 |
Chain | Residue |
A | GLU171 |
A | LYS178 |
A | VAL179 |
A | HOH484 |
C | LYS172 |
C | EPE301 |
C | HOH437 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 305 |
Chain | Residue |
A | LEU71 |
A | ILE74 |
A | PHE81 |
A | PHE131 |
A | GLY139 |
A | HIS230 |
A | HOH404 |
A | HOH528 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 306 |
Chain | Residue |
A | GLU231 |
A | LYS232 |
A | THR233 |
A | PHE234 |
A | HIS235 |
A | HIS236 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 307 |
Chain | Residue |
A | ASN60 |
A | HIS104 |
A | GLU124 |
A | ARG182 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL B 301 |
Chain | Residue |
B | TYR61 |
B | ILE106 |
site_id | AC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE EPE C 301 |
Chain | Residue |
A | LYS178 |
A | TYR188 |
A | GLU195 |
A | GOL303 |
A | GOL304 |
C | GLU157 |
C | ASN161 |
C | GLY163 |
C | SER164 |
C | TYR165 |
C | ASP169 |
C | ARG173 |
C | HOH437 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL C 302 |
Chain | Residue |
A | LYS148 |
A | LYS149 |
A | GLY151 |
A | PRO176 |
C | PHE152 |
C | SER153 |
C | HOH402 |
C | HOH505 |
C | HOH509 |
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 | |