2.700 Å
X-ray
2007-01-29
| Name: | Farnesyl pyrophosphate synthase |
|---|---|
| ID: | FPPS_HUMAN |
| AC: | P14324 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 2.5.1.10 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 44.040 |
|---|---|
| Number of residues: | 25 |
| Including | |
| Standard Amino Acids: | 21 |
| Non Standard Amino Acids: | 3 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | MG MG MG |
| Ligandability | Volume (Å3) |
|---|---|
| 0.830 | 1144.125 |
| % Hydrophobic | % Polar |
|---|---|
| 40.12 | 59.88 |
| According to VolSite | |

| HET Code: | SUF |
|---|---|
| Formula: | C4H10O7P2S |
| Molecular weight: | 264.131 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 59.2 % |
| Polar Surface area: | 170.43 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 7 |
| H-Bond Donors: | 2 |
| Rings: | 0 |
| Aromatic rings: | 0 |
| Anionic atoms: | 4 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 4 |
| X | Y | Z |
|---|---|---|
| 15.2783 | 78.2668 | 25.6876 |
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 |
| O7 | NZ | LYS- 214 | 3.44 | 124.55 | H-Bond (Protein Donor) |
| O7 | NZ | LYS- 214 | 3.44 | 0 | Ionic (Protein Cationic) |
| C3 | CD | LYS- 214 | 3.21 | 0 | Hydrophobic |
| O2 | OE1 | GLN- 254 | 3.22 | 132.38 | H-Bond (Ligand Donor) |
| O1 | MG | MG- 907 | 2.76 | 0 | Metal Acceptor |
| O1 | MG | MG- 909 | 2.03 | 0 | Metal Acceptor |
| O3 | MG | MG- 909 | 2.56 | 0 | Metal Acceptor |