3LKE
Crystal structure of enoyl-CoA hydratase from Bacillus halodurans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005782 | cellular_component | peroxisomal matrix |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005782 | cellular_component | peroxisomal matrix |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| C | 0005777 | cellular_component | peroxisome |
| C | 0005782 | cellular_component | peroxisomal matrix |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 264 |
| Chain | Residue |
| A | TYR159 |
| A | GLU160 |
| A | HOH266 |
| A | HOH339 |
| B | PHE98 |
| B | ARG155 |
| B | ILE156 |
| B | HOH299 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 264 |
| Chain | Residue |
| B | HOH278 |
| B | HOH279 |
| C | PHE98 |
| C | ILE156 |
| B | GLU160 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 264 |
| Chain | Residue |
| A | PHE98 |
| A | ARG155 |
| A | ILE156 |
| C | GLU160 |
| C | HOH275 |
| C | HOH293 |
| C | HOH308 |
