sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.700 Å
X-ray
2003-01-06
| Name: | Protein farnesyltransferase subunit beta |
|---|---|
| ID: | FNTB_RAT |
| AC: | Q02293 |
| Organism: | Rattus norvegicus |
| Reign: | Eukaryota |
| TaxID: | 10116 |
| EC Number: | 2.5.1.58 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 21 % |
| B | 79 % |
| B-Factor: | 30.000 |
|---|---|
| Number of residues: | 30 |
| Including | |
| Standard Amino Acids: | 28 |
| Non Standard Amino Acids: | 2 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | ZN |
| Ligandability | Volume (Å3) |
|---|---|
| 0.654 | 1063.125 |
| % Hydrophobic | % Polar |
|---|---|
| 38.10 | 61.90 |
| According to VolSite | |
| HET Code: | HFP |
|---|---|
| Formula: | C15H31O4P |
| Molecular weight: | 306.378 g/mol |
| DrugBank ID: | DB07895 |
| Buried Surface Area: | 54.29 % |
| Polar Surface area: | 93.23 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 4 |
| H-Bond Donors: | 1 |
| Rings: | 0 |
| Aromatic rings: | 0 |
| Anionic atoms: | 2 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 11 |
| X | Y | Z |
|---|---|---|
| 55.3617 | 44.7957 | 0.95785 |
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 |
| C14 | CZ2 | TRP- 102 | 3.63 | 0 | Hydrophobic |
| C15 | CH2 | TRP- 102 | 4.46 | 0 | Hydrophobic |
| C15 | CE2 | TYR- 154 | 4.03 | 0 | Hydrophobic |
| O1P | NZ | LYS- 164 | 3.33 | 171.81 | H-Bond (Protein Donor) |
| O1P | NZ | LYS- 164 | 3.33 | 0 | Ionic (Protein Cationic) |
| C4 | CZ | TYR- 166 | 4.19 | 0 | Hydrophobic |
| C5 | CZ | TYR- 166 | 4.14 | 0 | Hydrophobic |
| C4 | CD2 | TYR- 200 | 4 | 0 | Hydrophobic |
| C11 | CD | ARG- 202 | 4.35 | 0 | Hydrophobic |
| C15 | CD2 | TYR- 205 | 3.23 | 0 | Hydrophobic |
| C15 | SG | CYS- 206 | 3.98 | 0 | Hydrophobic |
| O2P | NE2 | HIS- 248 | 2.78 | 144.64 | H-Bond (Protein Donor) |
| C4 | CE1 | TYR- 251 | 3.66 | 0 | Hydrophobic |
| C5 | CZ | TYR- 251 | 4.3 | 0 | Hydrophobic |
| C15 | SG | CYS- 254 | 4.03 | 0 | Hydrophobic |
| O2P | OH | TYR- 300 | 3.1 | 120.57 | H-Bond (Protein Donor) |
| O3P | OH | TYR- 300 | 3.3 | 139.68 | H-Bond (Protein Donor) |
| C9 | CE2 | TRP- 303 | 3.46 | 0 | Hydrophobic |
| C10 | CZ2 | TRP- 303 | 3.65 | 0 | Hydrophobic |
