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
2013-07-29
| Name: | Lanosterol 14-alpha demethylase |
|---|---|
| ID: | CP51_YEAST |
| AC: | P10614 |
| Organism: | Saccharomyces cerevisiae |
| Reign: | Eukaryota |
| TaxID: | 559292 |
| EC Number: | 1.14.13.70 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 47.144 |
|---|---|
| Number of residues: | 33 |
| Including | |
| Standard Amino Acids: | 31 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.148 | 1596.375 |
| % Hydrophobic | % Polar |
|---|---|
| 59.62 | 40.38 |
| According to VolSite | |
| HET Code: | LAN |
|---|---|
| Formula: | C30H50O |
| Molecular weight: | 426.717 g/mol |
| DrugBank ID: | DB03696 |
| Buried Surface Area: | 66.77 % |
| Polar Surface area: | 20.23 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 1 |
| H-Bond Donors: | 1 |
| Rings: | 4 |
| Aromatic rings: | 0 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 4 |
| X | Y | Z |
|---|---|---|
| 18.545 | 11.0271 | 17.0009 |
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 |
| C5 | CE2 | TYR- 126 | 3.42 | 0 | Hydrophobic |
| C4 | CD2 | TYR- 126 | 3.83 | 0 | Hydrophobic |
| C21 | CE1 | TYR- 126 | 4.25 | 0 | Hydrophobic |
| C9 | CE1 | TYR- 126 | 3.46 | 0 | Hydrophobic |
| C11 | CD1 | LEU- 129 | 3.69 | 0 | Hydrophobic |
| C26 | CG2 | THR- 130 | 4.02 | 0 | Hydrophobic |
| C2 | CG2 | THR- 130 | 3.36 | 0 | Hydrophobic |
| C26 | CE2 | PHE- 134 | 3.77 | 0 | Hydrophobic |
| C30 | CZ | PHE- 134 | 3.79 | 0 | Hydrophobic |
| C26 | CG2 | ILE- 139 | 3.93 | 0 | Hydrophobic |
| C4 | CE2 | TYR- 140 | 3.68 | 0 | Hydrophobic |
| C27 | CZ | TYR- 140 | 4.46 | 0 | Hydrophobic |
| C26 | CE2 | TYR- 140 | 3.28 | 0 | Hydrophobic |
| C2 | CE1 | PHE- 236 | 3.49 | 0 | Hydrophobic |
| C23 | CZ | PHE- 236 | 3.75 | 0 | Hydrophobic |
| C31 | CZ | PHE- 236 | 3.21 | 0 | Hydrophobic |
| C19 | CB | PRO- 238 | 4.2 | 0 | Hydrophobic |
| C18 | CG | PRO- 238 | 4.26 | 0 | Hydrophobic |
| C11 | CE2 | PHE- 241 | 3.46 | 0 | Hydrophobic |
| C21 | CE2 | PHE- 241 | 4.2 | 0 | Hydrophobic |
| C14 | CE2 | PHE- 241 | 3.55 | 0 | Hydrophobic |
| O29 | O | GLY- 310 | 3.38 | 135.07 | H-Bond (Ligand Donor) |
| C8 | CD1 | LEU- 380 | 3.33 | 0 | Hydrophobic |
| C22 | CD2 | LEU- 380 | 3.46 | 0 | Hydrophobic |
| C8 | CD2 | LEU- 383 | 3.38 | 0 | Hydrophobic |
| C9 | CD2 | LEU- 383 | 4.42 | 0 | Hydrophobic |
| C9 | CD2 | PHE- 384 | 4.14 | 0 | Hydrophobic |
| C21 | CE2 | PHE- 384 | 3.44 | 0 | Hydrophobic |
| C14 | CE2 | PHE- 384 | 3.41 | 0 | Hydrophobic |
| C13 | CE | MET- 509 | 3.91 | 0 | Hydrophobic |
| C11 | SD | MET- 509 | 3.49 | 0 | Hydrophobic |
