sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.400 Å
X-ray
2009-08-18
| Name: | Oxysterols receptor LXR-alpha |
|---|---|
| ID: | NR1H3_HUMAN |
| AC: | Q13133 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 34.536 |
|---|---|
| Number of residues: | 38 |
| Including | |
| Standard Amino Acids: | 38 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.052 | 722.250 |
| % Hydrophobic | % Polar |
|---|---|
| 63.08 | 36.92 |
| According to VolSite | |
| HET Code: | O40 |
|---|---|
| Formula: | C23H23F3N3O5 |
| Molecular weight: | 478.441 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 69.5 % |
| Polar Surface area: | 107.73 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 5 |
| H-Bond Donors: | 1 |
| Rings: | 3 |
| Aromatic rings: | 3 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 10 |
| X | Y | Z |
|---|---|---|
| 20.4181 | -16.1248 | 18.9551 |
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 |
| DuAr | CZ | ARG- 232 | 3.58 | 14.81 | Pi/Cation |
| C16 | CD | ARG- 232 | 3.72 | 0 | Hydrophobic |
| F40 | CE1 | PHE- 254 | 4.06 | 0 | Hydrophobic |
| C1 | CB | PHE- 257 | 4.31 | 0 | Hydrophobic |
| C15 | CD2 | PHE- 257 | 4.03 | 0 | Hydrophobic |
| F39 | CG2 | THR- 258 | 3.78 | 0 | Hydrophobic |
| F40 | CG2 | THR- 258 | 4.33 | 0 | Hydrophobic |
| C15 | CB | LEU- 260 | 3.86 | 0 | Hydrophobic |
| C15 | CB | ALA- 261 | 4.32 | 0 | Hydrophobic |
| C1 | CB | ALA- 261 | 3.61 | 0 | Hydrophobic |
| C22 | CB | SER- 264 | 4.49 | 0 | Hydrophobic |
| C29 | CB | SER- 264 | 4.18 | 0 | Hydrophobic |
| C12 | CD1 | ILE- 295 | 3.87 | 0 | Hydrophobic |
| C22 | CG | MET- 298 | 4.38 | 0 | Hydrophobic |
| C12 | SD | MET- 298 | 3.98 | 0 | Hydrophobic |
| C17 | CD2 | LEU- 299 | 4.21 | 0 | Hydrophobic |
| C22 | CB | GLU- 301 | 4 | 0 | Hydrophobic |
| C19 | CD | ARG- 305 | 4.27 | 0 | Hydrophobic |
| C22 | CE1 | PHE- 315 | 3.97 | 0 | Hydrophobic |
| C29 | CE1 | PHE- 315 | 4.29 | 0 | Hydrophobic |
| C10 | CB | PHE- 315 | 3.72 | 0 | Hydrophobic |
| C26 | CZ | PHE- 315 | 3.52 | 0 | Hydrophobic |
| C13 | CD2 | LEU- 316 | 4.04 | 0 | Hydrophobic |
| C20 | CE2 | PHE- 326 | 3.8 | 0 | Hydrophobic |
| F40 | CD1 | LEU- 331 | 3.7 | 0 | Hydrophobic |
| C17 | CD1 | ILE- 339 | 4.32 | 0 | Hydrophobic |
| N8 | NE2 | HIS- 421 | 3.34 | 121.69 | H-Bond (Protein Donor) |
| F38 | CG | GLN- 424 | 4.07 | 0 | Hydrophobic |
| F38 | CD2 | LEU- 428 | 3.25 | 0 | Hydrophobic |
| F38 | CD2 | LEU- 435 | 3.95 | 0 | Hydrophobic |
| F39 | CD1 | LEU- 439 | 3.95 | 0 | Hydrophobic |
| F39 | CZ3 | TRP- 443 | 3.79 | 0 | Hydrophobic |
