sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.800 Å
X-ray
2003-05-06
| Name: | Oxysterols receptor LXR-beta |
|---|---|
| ID: | NR1H2_HUMAN |
| AC: | P55055 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| B | 100 % |
| B-Factor: | 22.146 |
|---|---|
| Number of residues: | 34 |
| Including | |
| Standard Amino Acids: | 34 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.686 | 688.500 |
| % Hydrophobic | % Polar |
|---|---|
| 68.63 | 31.37 |
| According to VolSite | |
| HET Code: | CO1 |
|---|---|
| Formula: | C27H44O2 |
| Molecular weight: | 400.637 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 64.67 % |
| Polar Surface area: | 32.76 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| H-Bond Donors: | 1 |
| Rings: | 5 |
| Aromatic rings: | 0 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 4 |
| X | Y | Z |
|---|---|---|
| 35.1958 | -26.6134 | 92.0449 |
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 |
| C22 | CE1 | PHE- 243 | 4.03 | 0 | Hydrophobic |
| C18 | CZ | PHE- 243 | 3.43 | 0 | Hydrophobic |
| C13 | CD2 | PHE- 271 | 3.42 | 0 | Hydrophobic |
| C6 | CG | PHE- 271 | 3.88 | 0 | Hydrophobic |
| C28 | CG2 | THR- 272 | 3.92 | 0 | Hydrophobic |
| C4 | CB | LEU- 274 | 3.56 | 0 | Hydrophobic |
| C18 | CB | SER- 278 | 4.37 | 0 | Hydrophobic |
| C4 | CB | SER- 278 | 4.46 | 0 | Hydrophobic |
| C3 | CB | SER- 278 | 4.46 | 0 | Hydrophobic |
| C15 | CB | SER- 278 | 4.32 | 0 | Hydrophobic |
| O24 | OE2 | GLU- 281 | 3.06 | 142.7 | H-Bond (Ligand Donor) |
| C11 | CB | MET- 312 | 3.8 | 0 | Hydrophobic |
| C19 | CB | GLU- 315 | 3.35 | 0 | Hydrophobic |
| C4 | CD2 | PHE- 329 | 3.95 | 0 | Hydrophobic |
| C1 | CE2 | PHE- 329 | 4.14 | 0 | Hydrophobic |
| C12 | CZ | PHE- 329 | 3.47 | 0 | Hydrophobic |
| C6 | CE2 | PHE- 329 | 4.15 | 0 | Hydrophobic |
| C16 | CD1 | PHE- 329 | 3.55 | 0 | Hydrophobic |
| C12 | CZ | PHE- 340 | 3.93 | 0 | Hydrophobic |
| C20 | CD1 | LEU- 345 | 4.27 | 0 | Hydrophobic |
| C29 | CD2 | LEU- 345 | 4.07 | 0 | Hydrophobic |
| C21 | CZ | PHE- 349 | 4.25 | 0 | Hydrophobic |
| C20 | CE2 | PHE- 349 | 3.9 | 0 | Hydrophobic |
| O27 | NE2 | HIS- 435 | 3.5 | 143.57 | H-Bond (Protein Donor) |
| C29 | CG | GLN- 438 | 4.07 | 0 | Hydrophobic |
| C29 | CG | LEU- 442 | 4.31 | 0 | Hydrophobic |
| C25 | CZ3 | TRP- 457 | 4.33 | 0 | Hydrophobic |
