sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
3.000 Å
X-ray
2010-10-16
| Name: | Lanosterol 14-alpha-demethylase |
|---|---|
| ID: | Q385E8_TRYB2 |
| AC: | Q385E8 |
| Organism: | Trypanosoma brucei brucei |
| Reign: | Eukaryota |
| TaxID: | 185431 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| D | 100 % |
| B-Factor: | 64.668 |
|---|---|
| Number of residues: | 37 |
| Including | |
| Standard Amino Acids: | 35 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.370 | 2173.500 |
| % Hydrophobic | % Polar |
|---|---|
| 65.37 | 34.63 |
| According to VolSite | |
| HET Code: | LNP |
|---|---|
| Formula: | C33H54O |
| Molecular weight: | 466.781 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 65.66 % |
| Polar Surface area: | 20.23 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 1 |
| H-Bond Donors: | 1 |
| Rings: | 5 |
| Aromatic rings: | 0 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| 29.6464 | -12.6077 | -39.1248 |
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 |
| CAA | CE1 | TYR- 103 | 3.52 | 0 | Hydrophobic |
| CAB | CD1 | TYR- 103 | 4.08 | 0 | Hydrophobic |
| CAF | CD1 | TYR- 103 | 4.49 | 0 | Hydrophobic |
| CAL | CZ | TYR- 103 | 3.71 | 0 | Hydrophobic |
| CAT | CG | TYR- 103 | 3.29 | 0 | Hydrophobic |
| CAK | CE1 | TYR- 103 | 3.81 | 0 | Hydrophobic |
| CAX | CZ | PHE- 105 | 3.81 | 0 | Hydrophobic |
| CAS | CE | MET- 106 | 4.29 | 0 | Hydrophobic |
| CAE | CZ | PHE- 110 | 4.31 | 0 | Hydrophobic |
| CAP | CZ | PHE- 110 | 4.48 | 0 | Hydrophobic |
| CAS | CE1 | PHE- 110 | 3.59 | 0 | Hydrophobic |
| CAV | CZ | PHE- 110 | 4.09 | 0 | Hydrophobic |
| CBE | CG1 | VAL- 114 | 4.48 | 0 | Hydrophobic |
| CBD | CB | ALA- 115 | 4.37 | 0 | Hydrophobic |
| CAY | CE1 | TYR- 116 | 4.22 | 0 | Hydrophobic |
| CBD | CB | GLN- 126 | 4.01 | 0 | Hydrophobic |
| CBA | CD2 | LEU- 127 | 3.73 | 0 | Hydrophobic |
| CBD | CD2 | LEU- 127 | 3.71 | 0 | Hydrophobic |
| CBC | CD2 | LEU- 130 | 4.1 | 0 | Hydrophobic |
| CBC | CG | MET- 284 | 3.92 | 0 | Hydrophobic |
| CBE | SD | MET- 284 | 3.59 | 0 | Hydrophobic |
| CAP | CB | ALA- 287 | 4.27 | 0 | Hydrophobic |
| CAZ | CB | ALA- 287 | 3.3 | 0 | Hydrophobic |
| CBC | CB | ALA- 287 | 4.03 | 0 | Hydrophobic |
| CAD | CB | ALA- 291 | 3.96 | 0 | Hydrophobic |
| CAQ | CB | ALA- 291 | 4.08 | 0 | Hydrophobic |
| CBH | CB | ALA- 291 | 3.65 | 0 | Hydrophobic |
| CBH | CG2 | THR- 295 | 4.21 | 0 | Hydrophobic |
| CAI | CD2 | LEU- 356 | 4.03 | 0 | Hydrophobic |
| CAK | CD1 | LEU- 356 | 4.05 | 0 | Hydrophobic |
| CAM | CD2 | LEU- 356 | 3.99 | 0 | Hydrophobic |
| CAW | CD2 | LEU- 356 | 3.53 | 0 | Hydrophobic |
| CBG | CD1 | LEU- 356 | 3.41 | 0 | Hydrophobic |
| OBH | O | MET- 358 | 3.14 | 145.72 | H-Bond (Ligand Donor) |
| CAL | CD2 | LEU- 359 | 4.42 | 0 | Hydrophobic |
