2.020 Å
X-ray
2012-09-18
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 |
---|---|
F | 100 % |
B-Factor: | 29.762 |
---|---|
Number of residues: | 43 |
Including | |
Standard Amino Acids: | 33 |
Non Standard Amino Acids: | 3 |
Water Molecules: | 7 |
Cofactors: | |
Metals: | MG MG MG |
Ligandability | Volume (Å3) |
---|---|
0.278 | 381.375 |
% Hydrophobic | % Polar |
---|---|
44.25 | 55.75 |
According to VolSite |
HET Code: | YS4 |
---|---|
Formula: | C15H16N2O7P2 |
Molecular weight: | 398.244 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 70.79 % |
Polar Surface area: | 180.15 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 9 |
H-Bond Donors: | 1 |
Rings: | 2 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
16.2407 | 30.1813 | -7.16477 |
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 |
C3 | CZ | PHE- 98 | 3.79 | 0 | Hydrophobic |
C2 | CD1 | PHE- 99 | 4.19 | 0 | Hydrophobic |
C4 | CD1 | PHE- 99 | 3.49 | 0 | Hydrophobic |
C8 | CB | PHE- 99 | 3.38 | 0 | Hydrophobic |
C11 | CD2 | LEU- 100 | 4.38 | 0 | Hydrophobic |
C1 | CB | ALA- 102 | 3.76 | 0 | Hydrophobic |
N1 | OD1 | ASP- 103 | 3.12 | 120.35 | H-Bond (Ligand Donor) |
C11 | CB | ASP- 103 | 3.76 | 0 | Hydrophobic |
C8 | CB | ASP- 103 | 3.47 | 0 | Hydrophobic |
C1 | SD | MET- 106 | 3.93 | 0 | Hydrophobic |
O5 | CZ | ARG- 112 | 3.78 | 0 | Ionic (Protein Cationic) |
O6 | CZ | ARG- 112 | 3.14 | 0 | Ionic (Protein Cationic) |
O5 | NH2 | ARG- 112 | 2.82 | 140.85 | H-Bond (Protein Donor) |
O6 | NH1 | ARG- 112 | 2.52 | 155.41 | H-Bond (Protein Donor) |
O6 | NH2 | ARG- 112 | 2.91 | 132.74 | H-Bond (Protein Donor) |
C15 | CG2 | THR- 167 | 4.35 | 0 | Hydrophobic |
C6 | CG2 | THR- 167 | 3.37 | 0 | Hydrophobic |
C3 | CG | GLU- 168 | 3.8 | 0 | Hydrophobic |
C4 | CG | GLN- 171 | 4.01 | 0 | Hydrophobic |
C5 | CB | GLN- 171 | 3.42 | 0 | Hydrophobic |
O2 | NZ | LYS- 200 | 2.6 | 150.28 | H-Bond (Protein Donor) |
O2 | NZ | LYS- 200 | 2.6 | 0 | Ionic (Protein Cationic) |
O4 | NZ | LYS- 200 | 3.79 | 0 | Ionic (Protein Cationic) |
C15 | CB | LYS- 200 | 4.32 | 0 | Hydrophobic |
O6 | NZ | LYS- 257 | 3.12 | 121.17 | H-Bond (Protein Donor) |
O7 | NZ | LYS- 257 | 2.86 | 160.24 | H-Bond (Protein Donor) |
O6 | NZ | LYS- 257 | 3.12 | 0 | Ionic (Protein Cationic) |
O7 | NZ | LYS- 257 | 2.86 | 0 | Ionic (Protein Cationic) |
O3 | MG | MG- 403 | 2.11 | 0 | Metal Acceptor |
O5 | MG | MG- 404 | 2.33 | 0 | Metal Acceptor |
O3 | MG | MG- 404 | 2.05 | 0 | Metal Acceptor |
O7 | MG | MG- 405 | 1.95 | 0 | Metal Acceptor |
O4 | MG | MG- 405 | 2.02 | 0 | Metal Acceptor |