2.130 Å
X-ray
2007-01-23
Name: | Geranylgeranyl pyrophosphate synthase |
---|---|
ID: | GGPPS_YEAST |
AC: | Q12051 |
Organism: | Saccharomyces cerevisiae |
Reign: | Eukaryota |
TaxID: | 559292 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 41.084 |
---|---|
Number of residues: | 17 |
Including | |
Standard Amino Acids: | 16 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.035 | 455.625 |
% Hydrophobic | % Polar |
---|---|
42.96 | 57.04 |
According to VolSite |
HET Code: | IPE |
---|---|
Formula: | C5H9O7P2 |
Molecular weight: | 243.068 g/mol |
DrugBank ID: | DB04714 |
Buried Surface Area: | 46.69 % |
Polar Surface area: | 141.4 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 0 |
Rings: | 0 |
Aromatic rings: | 0 |
Anionic atoms: | 3 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 6 |
X | Y | Z |
---|---|---|
20.4751 | 27.5955 | 34.1516 |
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 |
O1B | NZ | LYS- 38 | 3.15 | 153.14 | H-Bond (Protein Donor) |
O1B | NZ | LYS- 38 | 3.15 | 0 | Ionic (Protein Cationic) |
O3B | NZ | LYS- 38 | 3.51 | 0 | Ionic (Protein Cationic) |
O1B | NE2 | HIS- 73 | 3.09 | 154.47 | H-Bond (Protein Donor) |
C4 | CD2 | LEU- 77 | 3.78 | 0 | Hydrophobic |
O1A | CZ | ARG- 90 | 3.14 | 0 | Ionic (Protein Cationic) |
O1B | CZ | ARG- 90 | 3.34 | 0 | Ionic (Protein Cationic) |
O2B | CZ | ARG- 90 | 3.26 | 0 | Ionic (Protein Cationic) |
O2A | OH | TYR- 210 | 3.12 | 150.63 | H-Bond (Protein Donor) |
C2 | CE2 | TYR- 210 | 3.51 | 0 | Hydrophobic |