5XZD
Structure of acryloyl-CoA hydratase AcuH from Roseovarius nubinhibens ISM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016836 | molecular_function | hydro-lyase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016836 | molecular_function | hydro-lyase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0016836 | molecular_function | hydro-lyase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| D | 0006635 | biological_process | fatty acid beta-oxidation |
| D | 0016836 | molecular_function | hydro-lyase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| E | 0006635 | biological_process | fatty acid beta-oxidation |
| E | 0016836 | molecular_function | hydro-lyase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| F | 0006635 | biological_process | fatty acid beta-oxidation |
| F | 0016836 | molecular_function | hydro-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue ACY A 301 |
| Chain | Residue |
| A | PHE84 |
| A | GLY109 |
| A | GLU112 |
| A | GLU132 |
| A | ALA139 |
| A | GLY140 |
| A | MET141 |
| A | HOH437 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue ACY B 301 |
| Chain | Residue |
| B | GLY109 |
| B | GLU112 |
| B | GLU132 |
| B | ALA139 |
| B | GLY140 |
| B | MET141 |
| B | HOH415 |
| B | PHE84 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue ACY C 301 |
| Chain | Residue |
| A | PHE231 |
| C | PHE84 |
| C | GLY109 |
| C | GLU112 |
| C | GLU132 |
| C | ALA139 |
| C | GLY140 |
| C | MET141 |
| C | HOH466 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue ACY D 301 |
| Chain | Residue |
| D | PHE84 |
| D | GLY109 |
| D | GLU112 |
| D | GLU132 |
| D | GLY140 |
| D | MET141 |
| D | HOH416 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue ACY E 301 |
| Chain | Residue |
| E | PHE84 |
| E | GLY109 |
| E | GLU112 |
| E | GLU132 |
| E | ALA139 |
| E | GLY140 |
| E | MET141 |
| E | HOH417 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ACY F 301 |
| Chain | Residue |
| F | PHE84 |
| F | GLU112 |
| F | GLU132 |
| F | GLY140 |
| F | MET141 |
| F | HOH456 |
Functional Information from PROSITE/UniProt
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaVSGyalGGGcelaMmCDF |
| Chain | Residue | Details |
| A | ILE99-PHE119 |
