sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.100 Å
X-ray
2006-10-17
| Name: | Estrogen receptor beta |
|---|---|
| ID: | ESR2_RAT |
| AC: | Q62986 |
| Organism: | Rattus norvegicus |
| Reign: | Eukaryota |
| TaxID: | 10116 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 43.190 |
|---|---|
| Number of residues: | 30 |
| Including | |
| Standard Amino Acids: | 29 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.388 | 290.250 |
| % Hydrophobic | % Polar |
|---|---|
| 72.09 | 27.91 |
| According to VolSite | |
| HET Code: | EST |
|---|---|
| Formula: | C18H24O2 |
| Molecular weight: | 272.382 g/mol |
| DrugBank ID: | DB00783 |
| Buried Surface Area: | 78.31 % |
| Polar Surface area: | 40.46 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| H-Bond Donors: | 2 |
| Rings: | 4 |
| Aromatic rings: | 1 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 0 |
| X | Y | Z |
|---|---|---|
| 49.2447 | 30.9454 | 76.6209 |
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 |
| C12 | CE | MET- 250 | 4.41 | 0 | Hydrophobic |
| C17 | CE | MET- 250 | 4.08 | 0 | Hydrophobic |
| C11 | CB | LEU- 253 | 4 | 0 | Hydrophobic |
| C2 | CD2 | LEU- 256 | 3.9 | 0 | Hydrophobic |
| C11 | CB | ALA- 257 | 4.49 | 0 | Hydrophobic |
| C1 | CB | ALA- 257 | 4.11 | 0 | Hydrophobic |
| O3 | OE1 | GLU- 260 | 2.54 | 145.8 | H-Bond (Ligand Donor) |
| O3 | OE2 | GLU- 260 | 3.22 | 124.15 | H-Bond (Ligand Donor) |
| C8 | SD | MET- 291 | 4.4 | 0 | Hydrophobic |
| C18 | CE | MET- 291 | 3.4 | 0 | Hydrophobic |
| C4 | CB | LEU- 294 | 3.81 | 0 | Hydrophobic |
| C6 | CG | MET- 295 | 3.8 | 0 | Hydrophobic |
| C7 | CE | MET- 295 | 4.13 | 0 | Hydrophobic |
| C6 | CD2 | LEU- 298 | 3.99 | 0 | Hydrophobic |
| O3 | NH2 | ARG- 301 | 3.15 | 143.44 | H-Bond (Protein Donor) |
| C9 | CE1 | PHE- 311 | 4.06 | 0 | Hydrophobic |
| C7 | CE1 | PHE- 311 | 4.02 | 0 | Hydrophobic |
| C16 | CG1 | ILE- 328 | 4.2 | 0 | Hydrophobic |
| C17 | CD1 | ILE- 328 | 4.27 | 0 | Hydrophobic |
| C15 | CG2 | ILE- 331 | 4.02 | 0 | Hydrophobic |
| C16 | CD1 | ILE- 331 | 3.91 | 0 | Hydrophobic |
| C7 | CD1 | LEU- 335 | 4.1 | 0 | Hydrophobic |
| C16 | CB | HIS- 430 | 3.99 | 0 | Hydrophobic |
| O17 | ND1 | HIS- 430 | 3.08 | 152.68 | H-Bond (Ligand Donor) |
| C18 | CB | LEU- 431 | 3.99 | 0 | Hydrophobic |
| O3 | O | HOH- 2015 | 3.05 | 124.56 | H-Bond (Protein Donor) |
