sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.650 Å
X-ray
2015-03-12
| Name: | Stimulator of interferon genes protein |
|---|---|
| ID: | STING_MOUSE |
| AC: | Q3TBT3 |
| Organism: | Mus musculus |
| Reign: | Eukaryota |
| TaxID: | 10090 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 50 % |
| B | 50 % |
| B-Factor: | 28.812 |
|---|---|
| Number of residues: | 42 |
| Including | |
| Standard Amino Acids: | 40 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 2 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.188 | 486.000 |
| % Hydrophobic | % Polar |
|---|---|
| 41.67 | 58.33 |
| According to VolSite | |
| HET Code: | 2BA |
|---|---|
| Formula: | C20H22N10O12P2 |
| Molecular weight: | 656.396 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 73.62 % |
| Polar Surface area: | 334.95 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 20 |
| H-Bond Donors: | 4 |
| Rings: | 7 |
| Aromatic rings: | 4 |
| Anionic atoms: | 2 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 2 |
| Rotatable Bonds: | 2 |
| X | Y | Z |
|---|---|---|
| -17.043 | 6.37914 | -24.5637 |
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 |
| C1' | CD1 | TYR- 162 | 4.23 | 0 | Hydrophobic |
| C1'1 | CD1 | TYR- 162 | 4.2 | 0 | Hydrophobic |
| C4' | CB | TYR- 166 | 4.48 | 0 | Hydrophobic |
| C1' | CB | TYR- 166 | 3.52 | 0 | Hydrophobic |
| C1'1 | CG | TYR- 166 | 3.86 | 0 | Hydrophobic |
| DuAr | DuAr | TYR- 166 | 3.8 | 0 | Aromatic Face/Face |
| O2P | NH2 | ARG- 237 | 2.79 | 131.19 | H-Bond (Protein Donor) |
| O2P | NH1 | ARG- 237 | 3.28 | 120.03 | H-Bond (Protein Donor) |
| N7 | NH2 | ARG- 237 | 3.14 | 136.45 | H-Bond (Protein Donor) |
| O2P1 | NH2 | ARG- 237 | 2.72 | 141.09 | H-Bond (Protein Donor) |
| N71 | NH2 | ARG- 237 | 3.28 | 132.34 | H-Bond (Protein Donor) |
| DuAr | CZ | ARG- 237 | 3.92 | 172.81 | Pi/Cation |
| DuAr | CZ | ARG- 237 | 3.46 | 175.06 | Pi/Cation |
| N6 | O | VAL- 238 | 3.23 | 134.02 | H-Bond (Ligand Donor) |
| N61 | O | VAL- 238 | 3.18 | 137.77 | H-Bond (Ligand Donor) |
| C2' | CB | THR- 262 | 4.1 | 0 | Hydrophobic |
| C2'1 | CB | THR- 262 | 3.97 | 0 | Hydrophobic |
| N11 | O | HOH- 412 | 2.89 | 179.96 | H-Bond (Protein Donor) |
| N1 | O | HOH- 520 | 2.71 | 179.96 | H-Bond (Protein Donor) |
