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 |
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 |