sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.100 Å
X-ray
2003-01-14
| 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 | 18 % |
| B | 82 % |
| B-Factor: | 24.125 |
|---|---|
| Number of residues: | 44 |
| Including | |
| Standard Amino Acids: | 39 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 4 |
| Cofactors: | |
| Metals: | ZN |
| Ligandability | Volume (Å3) |
|---|---|
| 0.893 | 594.000 |
| % Hydrophobic | % Polar |
|---|---|
| 47.16 | 52.84 |
| According to VolSite | |
| HET Code: | 2NH |
|---|---|
| Formula: | C36H61N4O6S2 |
| Molecular weight: | 710.023 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 53.36 % |
| Polar Surface area: | 207.13 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 8 |
| H-Bond Donors: | 4 |
| Rings: | 0 |
| Aromatic rings: | 0 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 24 |
| X | Y | Z |
|---|---|---|
| 187.447 | 126.039 | 31.4845 |
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 |
| SD | CB | SER- 99 | 4.43 | 0 | Hydrophobic |
| CD1 | CH2 | TRP- 102 | 3.86 | 0 | Hydrophobic |
| C13 | CZ2 | TRP- 102 | 3.6 | 0 | Hydrophobic |
| C14 | CH2 | TRP- 102 | 4 | 0 | Hydrophobic |
| CD1 | CZ2 | TRP- 106 | 3.78 | 0 | Hydrophobic |
| CE | CE2 | TYR- 131 | 3.52 | 0 | Hydrophobic |
| SD | CB | ALA- 151 | 3.73 | 0 | Hydrophobic |
| CB5 | CB | ALA- 151 | 4 | 0 | Hydrophobic |
| CE | CG | PRO- 152 | 4.15 | 0 | Hydrophobic |
| C14 | CE2 | TYR- 154 | 4.1 | 0 | Hydrophobic |
| CG2 | CE1 | TYR- 166 | 4.29 | 0 | Hydrophobic |
| OT1 | NE2 | GLN- 167 | 2.82 | 175.1 | H-Bond (Protein Donor) |
| C8 | CD | ARG- 202 | 3.91 | 0 | Hydrophobic |
| C9 | CG | ARG- 202 | 4.16 | 0 | Hydrophobic |
| C10 | CD | ARG- 202 | 3.97 | 0 | Hydrophobic |
| C13 | CD | ARG- 202 | 3.75 | 0 | Hydrophobic |
| O23 | NH2 | ARG- 202 | 2.61 | 129.51 | H-Bond (Protein Donor) |
| C14 | CD2 | TYR- 205 | 3.59 | 0 | Hydrophobic |
| C13 | SG | CYS- 206 | 4.44 | 0 | Hydrophobic |
| C14 | SG | CYS- 206 | 3.92 | 0 | Hydrophobic |
| C8 | CZ | TYR- 251 | 4.05 | 0 | Hydrophobic |
| C9 | SG | CYS- 254 | 4.14 | 0 | Hydrophobic |
| C14 | SG | CYS- 254 | 4.1 | 0 | Hydrophobic |
| C3 | SG | CYS- 299 | 4.32 | 0 | Hydrophobic |
| SG | SG | CYS- 299 | 4.09 | 0 | Hydrophobic |
| C3 | CZ | TYR- 300 | 3.99 | 0 | Hydrophobic |
| C10 | CZ2 | TRP- 303 | 3.97 | 0 | Hydrophobic |
| CG3 | CE1 | TYR- 361 | 3.69 | 0 | Hydrophobic |
| C3 | CZ | TYR- 361 | 4.25 | 0 | Hydrophobic |
| CD1 | CE1 | TYR- 361 | 3.92 | 0 | Hydrophobic |
| CB2 | CE2 | TYR- 361 | 3.47 | 0 | Hydrophobic |
| OT1 | O | HOH- 3036 | 3.03 | 179.95 | H-Bond (Protein Donor) |
