2J5I
Crystal Structure of Hydroxycinnamoyl-CoA Hydratase-Lyase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0008300 | biological_process | isoprenoid catabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0008300 | biological_process | isoprenoid catabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
C | 0003824 | molecular_function | catalytic activity |
C | 0008300 | biological_process | isoprenoid catabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
D | 0003824 | molecular_function | catalytic activity |
D | 0008300 | biological_process | isoprenoid catabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
E | 0003824 | molecular_function | catalytic activity |
E | 0008300 | biological_process | isoprenoid catabolic process |
E | 0016829 | molecular_function | lyase activity |
E | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
F | 0003824 | molecular_function | catalytic activity |
F | 0008300 | biological_process | isoprenoid catabolic process |
F | 0016829 | molecular_function | lyase activity |
F | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
G | 0003824 | molecular_function | catalytic activity |
G | 0008300 | biological_process | isoprenoid catabolic process |
G | 0016829 | molecular_function | lyase activity |
G | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
H | 0003824 | molecular_function | catalytic activity |
H | 0008300 | biological_process | isoprenoid catabolic process |
H | 0016829 | molecular_function | lyase activity |
H | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
I | 0003824 | molecular_function | catalytic activity |
I | 0008300 | biological_process | isoprenoid catabolic process |
I | 0016829 | molecular_function | lyase activity |
I | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
J | 0003824 | molecular_function | catalytic activity |
J | 0008300 | biological_process | isoprenoid catabolic process |
J | 0016829 | molecular_function | lyase activity |
J | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
K | 0003824 | molecular_function | catalytic activity |
K | 0008300 | biological_process | isoprenoid catabolic process |
K | 0016829 | molecular_function | lyase activity |
K | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
L | 0003824 | molecular_function | catalytic activity |
L | 0008300 | biological_process | isoprenoid catabolic process |
L | 0016829 | molecular_function | lyase activity |
L | 0050547 | molecular_function | feruloyl-CoA hydratase/lyase activity |
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 |
I | ILE110-LEU130 | |
B | ILE110-LEU130 | |
A | ILE110-LEU130 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18479250, ECO:0007744|PDB:2VSS, ECO:0007744|PDB:2VSU |
Chain | Residue | Details |
I | LYS29 | |
C | LYS29 | |
C | ALA68 | |
C | MET70 | |
C | LEU72 | |
C | TYR75 | |
C | GLY120 | |
C | SER142 | |
C | GLY151 | |
C | TYR239 | |
D | LYS29 | |
I | ALA68 | |
D | ALA68 | |
D | MET70 | |
D | LEU72 | |
D | TYR75 | |
D | GLY120 | |
D | SER142 | |
D | GLY151 | |
D | TYR239 | |
E | LYS29 | |
E | ALA68 | |
I | MET70 | |
E | MET70 | |
E | LEU72 | |
E | TYR75 | |
E | GLY120 | |
E | SER142 | |
E | GLY151 | |
E | TYR239 | |
F | LYS29 | |
F | ALA68 | |
F | MET70 | |
I | LEU72 | |
F | LEU72 | |
F | TYR75 | |
F | GLY120 | |
F | SER142 | |
F | GLY151 | |
F | TYR239 | |
G | LYS29 | |
G | ALA68 | |
G | MET70 | |
G | LEU72 | |
I | TYR75 | |
G | TYR75 | |
G | GLY120 | |
G | SER142 | |
G | GLY151 | |
G | TYR239 | |
H | LYS29 | |
H | ALA68 | |
H | MET70 | |
H | LEU72 | |
H | TYR75 | |
I | GLY120 | |
H | GLY120 | |
H | SER142 | |
H | GLY151 | |
H | TYR239 | |
J | LYS29 | |
J | ALA68 | |
J | MET70 | |
J | LEU72 | |
J | TYR75 | |
J | GLY120 | |
I | SER142 | |
J | SER142 | |
J | GLY151 | |
J | TYR239 | |
K | LYS29 | |
K | ALA68 | |
K | MET70 | |
K | LEU72 | |
K | TYR75 | |
K | GLY120 | |
K | SER142 | |
I | GLY151 | |
K | GLY151 | |
K | TYR239 | |
L | LYS29 | |
L | ALA68 | |
L | MET70 | |
L | LEU72 | |
L | TYR75 | |
L | GLY120 | |
L | SER142 | |
L | GLY151 | |
I | TYR239 | |
L | TYR239 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18479250, ECO:0007744|PDB:2VSS |
Chain | Residue | Details |
I | TRP146 | |
L | TRP146 | |
C | TRP146 | |
D | TRP146 | |
E | TRP146 | |
F | TRP146 | |
G | TRP146 | |
H | TRP146 | |
J | TRP146 | |
K | TRP146 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
B | GLY120 | |
B | GLU143 | |
B | SER123 |
site_id | CSA10 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
L | GLY120 | |
L | GLU143 | |
L | SER123 |
site_id | CSA11 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
I | GLY120 | |
I | GLU143 | |
I | SER123 |
site_id | CSA12 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
A | GLY120 | |
A | GLU143 | |
A | SER123 |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
A | GLU143 | |
A | GLY151 |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
B | GLU143 | |
B | GLY151 |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
C | GLU143 | |
C | GLY151 |
site_id | CSA16 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
D | GLU143 | |
D | GLY151 |
site_id | CSA17 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
E | GLU143 | |
E | GLY151 |
site_id | CSA18 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
F | GLU143 | |
F | GLY151 |
site_id | CSA19 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
G | GLU143 | |
G | GLY151 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
C | GLY120 | |
C | GLU143 | |
C | SER123 |
site_id | CSA20 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
H | GLU143 | |
H | GLY151 |
site_id | CSA21 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
J | GLU143 | |
J | GLY151 |
site_id | CSA22 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
K | GLU143 | |
K | GLY151 |
site_id | CSA23 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
L | GLU143 | |
L | GLY151 |
site_id | CSA24 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
I | GLU143 | |
I | GLY151 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
D | GLY120 | |
D | GLU143 | |
D | SER123 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
E | GLY120 | |
E | GLU143 | |
E | SER123 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
F | GLY120 | |
F | GLU143 | |
F | SER123 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
G | GLY120 | |
G | GLU143 | |
G | SER123 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
H | GLY120 | |
H | GLU143 | |
H | SER123 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
J | GLY120 | |
J | GLU143 | |
J | SER123 |
site_id | CSA9 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dci |
Chain | Residue | Details |
K | GLY120 | |
K | GLU143 | |
K | SER123 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 347 |
Chain | Residue | Details |
I | MET70 | electrostatic stabiliser, hydrogen bond donor |
I | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
I | GLY120 | electrostatic stabiliser, hydrogen bond donor |
I | GLU143 | activator, proton acceptor, proton donor |
I | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA10 |
Number of Residues | 5 |
Details | M-CSA 347 |
Chain | Residue | Details |
L | MET70 | electrostatic stabiliser, hydrogen bond donor |
L | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
L | GLY120 | electrostatic stabiliser, hydrogen bond donor |
L | GLU143 | activator, proton acceptor, proton donor |
L | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA2 |
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 | 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 |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 347 |
Chain | Residue | Details |
E | MET70 | electrostatic stabiliser, hydrogen bond donor |
E | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
E | GLY120 | electrostatic stabiliser, hydrogen bond donor |
E | GLU143 | activator, proton acceptor, proton donor |
E | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA5 |
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 | MCSA6 |
Number of Residues | 5 |
Details | M-CSA 347 |
Chain | Residue | Details |
G | MET70 | electrostatic stabiliser, hydrogen bond donor |
G | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
G | GLY120 | electrostatic stabiliser, hydrogen bond donor |
G | GLU143 | activator, proton acceptor, proton donor |
G | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA7 |
Number of Residues | 5 |
Details | M-CSA 347 |
Chain | Residue | Details |
H | MET70 | electrostatic stabiliser, hydrogen bond donor |
H | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
H | GLY120 | electrostatic stabiliser, hydrogen bond donor |
H | GLU143 | activator, proton acceptor, proton donor |
H | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA8 |
Number of Residues | 5 |
Details | M-CSA 347 |
Chain | Residue | Details |
J | MET70 | electrostatic stabiliser, hydrogen bond donor |
J | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
J | GLY120 | electrostatic stabiliser, hydrogen bond donor |
J | GLU143 | activator, proton acceptor, proton donor |
J | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA9 |
Number of Residues | 5 |
Details | M-CSA 347 |
Chain | Residue | Details |
K | MET70 | electrostatic stabiliser, hydrogen bond donor |
K | TYR75 | electrostatic stabiliser, hydrogen bond donor, steric role |
K | GLY120 | electrostatic stabiliser, hydrogen bond donor |
K | GLU143 | activator, proton acceptor, proton donor |
K | TYR239 | electrostatic stabiliser, hydrogen bond donor, steric role |