sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.900 Å
X-ray
2011-04-04
| Name: | (Iso)eugenol O-methyltransferase |
|---|---|
| ID: | IEMT_CLABR |
| AC: | O04385 |
| Organism: | Clarkia breweri |
| Reign: | Eukaryota |
| TaxID: | 36903 |
| EC Number: | 2.1.1.146 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| C | 100 % |
| B-Factor: | 29.522 |
|---|---|
| Number of residues: | 21 |
| Including | |
| Standard Amino Acids: | 19 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.633 | 766.125 |
| % Hydrophobic | % Polar |
|---|---|
| 65.20 | 34.80 |
| According to VolSite | |
| HET Code: | EUG |
|---|---|
| Formula: | C10H12O2 |
| Molecular weight: | 164.201 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 69.1 % |
| Polar Surface area: | 29.46 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| H-Bond Donors: | 1 |
| Rings: | 1 |
| Aromatic rings: | 1 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 2 |
| X | Y | Z |
|---|---|---|
| -19.5952 | -10.7071 | -1.54873 |
Image generated by PoseView
Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand
| Ligand | Protein | Interaction | |||
|---|---|---|---|---|---|
| Atom | Atom | Residue | Distance (Å) | Angle (°) | Type |
| C7 | CZ | PHE- 130 | 4.28 | 0 | Hydrophobic |
| C10 | CD1 | LEU- 133 | 4.13 | 0 | Hydrophobic |
| C10 | CB | ALA- 134 | 3.89 | 0 | Hydrophobic |
| C10 | CD1 | LEU- 139 | 3.47 | 0 | Hydrophobic |
| C5 | CD1 | ILE- 165 | 4 | 0 | Hydrophobic |
| C2 | CE | MET- 183 | 3.73 | 0 | Hydrophobic |
| C9 | CB | ASP- 273 | 4.16 | 0 | Hydrophobic |
| C8 | CD1 | LEU- 322 | 3.82 | 0 | Hydrophobic |
| C4 | CE | MET- 323 | 4.32 | 0 | Hydrophobic |
| C5 | CB | TYR- 326 | 4.35 | 0 | Hydrophobic |
| C8 | CE2 | TYR- 326 | 3.63 | 0 | Hydrophobic |
| O4 | ND2 | ASN- 327 | 3.16 | 136.47 | H-Bond (Protein Donor) |
