Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0016829 | molecular_function | lyase activity |
| E | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0016829 | molecular_function | lyase activity |
| F | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ACO B 1251 |
| Chain | Residue |
| B | GLU28 |
| B | PHE118 |
| B | GLY119 |
| B | GLY120 |
| B | SER142 |
| B | TRP146 |
| B | HOH2060 |
| E | LYS29 |
| B | LYS29 |
| B | ARG30 |
| B | ALA32 |
| B | ALA68 |
| B | GLY69 |
| B | MET70 |
| B | ASP71 |
| B | TRP116 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ACO D 1249 |
| Chain | Residue |
| D | GLU28 |
| D | LYS29 |
| D | ARG30 |
| D | ALA32 |
| D | ALA68 |
| D | MET70 |
| D | ASP71 |
| D | LEU72 |
| D | PHE76 |
| D | PHE118 |
| D | GLY120 |
| D | SER142 |
| D | TRP146 |
| D | V551250 |
| D | HOH2004 |
| D | HOH2060 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ACO E 1250 |
| Chain | Residue |
| B | LYS29 |
| B | LYS73 |
| E | GLU28 |
| E | LYS29 |
| E | ARG30 |
| E | ALA32 |
| E | ALA68 |
| E | GLY69 |
| E | MET70 |
| E | ASP71 |
| E | LEU72 |
| E | PHE118 |
| E | GLY119 |
| E | GLY120 |
| E | SER142 |
| E | GLU143 |
| E | HOH2061 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ACO F 1249 |
| Chain | Residue |
| F | GLU28 |
| F | ARG29 |
| F | ARG30 |
| F | ALA32 |
| F | GLU64 |
| F | ALA68 |
| F | MET70 |
| F | ASP71 |
| F | LEU72 |
| F | PHE76 |
| F | TRP116 |
| F | PHE118 |
| F | GLY120 |
| F | SER142 |
| F | GLU143 |
| F | TRP146 |
| F | HOH2009 |
| F | HOH2060 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE V55 D 1250 |
| Chain | Residue |
| D | MET70 |
| D | TYR75 |
| D | PHE76 |
| D | ALA94 |
| D | GLN98 |
| D | GLU143 |
| D | GLY151 |
| D | ASN152 |
| D | ACO1249 |
| E | TYR239 |
Functional Information from PROSITE/UniProt
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAmVNGwcfGGGfsplVaCDL |
| Chain | Residue | Details |
| E | ILE110-LEU130 | |
| F | ILE110-LEU130 | |
| A | ILE110-LEU130 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| F | ARG29 | |
| B | LYS29 | |
| B | ALA68 | |
| B | MET70 | |
| B | LEU72 | |
| B | TYR75 | |
| B | GLY120 | |
| B | SER142 | |
| B | GLY151 | |
| B | TYR239 | |
| C | LYS29 | |
| F | ALA68 | |
| C | ALA68 | |
| C | MET70 | |
| C | LEU72 | |
| C | TYR75 | |
| C | GLY120 | |
| C | SER142 | |
| C | GLY151 | |
| C | TYR239 | |
| D | LYS29 | |
| D | ALA68 | |
| F | MET70 | |
| D | MET70 | |
| D | LEU72 | |
| D | TYR75 | |
| D | GLY120 | |
| D | SER142 | |
| D | GLY151 | |
| D | TYR239 | |
| F | LEU72 | |
| F | TYR75 | |
| F | GLY120 | |
| F | SER142 | |
| F | GLY151 | |
| F | TYR239 | |
| Chain | Residue | Details |
| F | TRP146 | |
| B | TRP146 | |
| C | TRP146 | |
| D | TRP146 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| E | GLY120 | |
| E | GLU143 | |
| E | SER123 | |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| D | GLU143 | |
| D | GLY151 | |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| E | GLU143 | |
| E | GLY151 | |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| F | GLU143 | |
| F | GLY151 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| A | GLY120 | |
| A | GLU143 | |
| A | SER123 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| B | GLY120 | |
| B | GLU143 | |
| B | SER123 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| C | GLY120 | |
| C | GLU143 | |
| C | SER123 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| D | GLY120 | |
| D | GLU143 | |
| D | SER123 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| F | GLY120 | |
| F | GLU143 | |
| F | SER123 | |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| A | GLU143 | |
| A | GLY151 | |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| B | GLU143 | |
| B | GLY151 | |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| C | GLU143 | |
| C | GLY151 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 347 |
| Chain | Residue | Details |
| F | MET70 | electrostatic stabiliser, hydrogen bond donor |
| F | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
| F | GLY120 | electrostatic stabiliser, hydrogen bond donor |
| F | GLU143 | activator, proton acceptor, proton donor |
| F | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 347 |
| Chain | Residue | Details |
| B | MET70 | electrostatic stabiliser, hydrogen bond donor |
| B | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | GLY120 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU143 | activator, proton acceptor, proton donor |
| B | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 347 |
| Chain | Residue | Details |
| C | MET70 | electrostatic stabiliser, hydrogen bond donor |
| C | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
| C | GLY120 | electrostatic stabiliser, hydrogen bond donor |
| C | GLU143 | activator, proton acceptor, proton donor |
| C | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 347 |
| Chain | Residue | Details |
| D | MET70 | electrostatic stabiliser, hydrogen bond donor |
| D | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
| D | GLY120 | electrostatic stabiliser, hydrogen bond donor |
| D | GLU143 | activator, proton acceptor, proton donor |
| D | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |
