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 | 13 |
Details | BINDING SITE FOR RESIDUE ACO A 1250 |
Chain | Residue |
A | GLU28 |
A | GLY119 |
A | GLY120 |
A | SER142 |
A | GLU143 |
A | LYS29 |
A | ALA32 |
A | ALA68 |
A | GLY69 |
A | MET70 |
A | ASP71 |
A | LEU72 |
A | PHE118 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ACO B 1251 |
Chain | Residue |
B | GLU28 |
B | LYS29 |
B | ARG30 |
B | ALA32 |
B | ALA68 |
B | MET70 |
B | ASP71 |
B | LEU72 |
B | GLY119 |
B | GLY120 |
B | SER142 |
B | GLU143 |
B | TRP146 |
E | LYS29 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ACO D 1250 |
Chain | Residue |
D | GLU28 |
D | LYS29 |
D | ARG30 |
D | ALA32 |
D | ALA68 |
D | GLY69 |
D | MET70 |
D | ASP71 |
D | LEU72 |
D | PHE76 |
D | PHE118 |
D | GLY120 |
D | SER142 |
D | TRP146 |
D | V551251 |
D | HOH2011 |
site_id | AC4 |
Number of Residues | 16 |
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 | GLY119 |
E | GLY120 |
E | SER142 |
E | TYR146 |
E | HOH2084 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ACO F 1249 |
Chain | Residue |
F | GLU28 |
F | ARG29 |
F | ARG30 |
F | ALA32 |
F | ALA68 |
F | GLY69 |
F | MET70 |
F | ASP71 |
F | LEU72 |
F | PHE118 |
F | GLY120 |
F | SER142 |
F | GLU143 |
F | TRP146 |
F | HOH2003 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE V55 D 1251 |
Chain | Residue |
D | MET70 |
D | TYR75 |
D | PHE76 |
D | ALA94 |
D | GLN98 |
D | GLU143 |
D | GLY151 |
D | ASN152 |
D | ACO1250 |
D | HOH2043 |
E | TYR239 |
Functional Information from PROSITE/UniProt
site_id | PS00166 |
Number of Residues | 21 |
Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAmVNGwcfGGGfaplVaCDL |
Chain | Residue | Details |
F | ILE110-LEU130 | |
E | ILE110-LEU130 | |
A | ILE110-LEU130 | |
C | 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 | |
D | LYS29 | |
F | ALA68 | |
D | ALA68 | |
D | MET70 | |
D | LEU72 | |
D | TYR75 | |
D | GLY120 | |
D | SER142 | |
D | GLY151 | |
D | TYR239 | |
F | MET70 | |
F | LEU72 | |
F | TYR75 | |
F | GLY120 | |
F | SER142 | |
F | GLY151 | |
F | TYR239 | |
Chain | Residue | Details |
F | TRP146 | |
B | 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 | ALA123 | |
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 | ALA123 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
B | GLY120 | |
B | GLU143 | |
B | ALA123 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
D | GLY120 | |
D | GLU143 | |
D | ALA123 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
C | GLY120 | |
C | GLU143 | |
C | ALA123 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
F | GLY120 | |
F | GLU143 | |
F | ALA123 | |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
C | GLU143 | |
C | GLY151 | |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
A | GLU143 | |
A | GLY151 | |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
B | GLU143 | |
B | 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 |
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 |