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 |