2.750 Å
X-ray
2013-02-21
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 | 60 % |
B | 40 % |
B-Factor: | 45.471 |
---|---|
Number of residues: | 31 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.892 | 536.625 |
% Hydrophobic | % Polar |
---|---|
47.80 | 52.20 |
According to VolSite |
HET Code: | 1K5 |
---|---|
Formula: | C15H10NO3 |
Molecular weight: | 252.245 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 69.73 % |
Polar Surface area: | 60.44 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 4 |
H-Bond Donors: | 0 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 1 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
-38.6239 | -0.705474 | 16.8932 |
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 |
C13 | CB | SER- 161 | 4.08 | 0 | Hydrophobic |
C12 | CB | SER- 161 | 3.58 | 0 | Hydrophobic |
C13 | CB | TYR- 162 | 4.08 | 0 | Hydrophobic |
C03 | CG2 | ILE- 164 | 3.84 | 0 | Hydrophobic |
C01 | CD1 | ILE- 234 | 3.25 | 0 | Hydrophobic |
O18 | NH1 | ARG- 237 | 2.58 | 146.75 | H-Bond (Protein Donor) |
O18 | CZ | ARG- 237 | 3.52 | 0 | Ionic (Protein Cationic) |
C06 | CB | THR- 262 | 3.62 | 0 | Hydrophobic |
C12 | CG | PRO- 263 | 3.66 | 0 | Hydrophobic |
C03 | CB | GLN- 265 | 3.88 | 0 | Hydrophobic |
C04 | CB | THR- 266 | 4.37 | 0 | Hydrophobic |
O15 | OG1 | THR- 266 | 2.64 | 168.24 | H-Bond (Protein Donor) |