sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.810 Å
X-ray
2014-05-05
| Name: | Prostaglandin G/H synthase 2 |
|---|---|
| ID: | PGH2_MOUSE |
| AC: | Q05769 |
| Organism: | Mus musculus |
| Reign: | Eukaryota |
| TaxID: | 10090 |
| EC Number: | 1.14.99.1 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 25.816 |
|---|---|
| Number of residues: | 27 |
| Including | |
| Standard Amino Acids: | 25 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.398 | 783.000 |
| % Hydrophobic | % Polar |
|---|---|
| 64.22 | 35.78 |
| According to VolSite | |
| HET Code: | IBP |
|---|---|
| Formula: | C13H17O2 |
| Molecular weight: | 205.273 g/mol |
| DrugBank ID: | DB09213 |
| Buried Surface Area: | 70 % |
| Polar Surface area: | 40.12 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| H-Bond Donors: | 0 |
| Rings: | 1 |
| Aromatic rings: | 1 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 4 |
| X | Y | Z |
|---|---|---|
| 13.0081 | 23.4872 | 25.2556 |
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 |
| C7 | CG1 | VAL- 117 | 4.16 | 0 | Hydrophobic |
| O1 | CZ | ARG- 121 | 3.8 | 0 | Ionic (Protein Cationic) |
| O2 | CZ | ARG- 121 | 3.78 | 0 | Ionic (Protein Cationic) |
| O1 | NE | ARG- 121 | 2.97 | 152.79 | H-Bond (Protein Donor) |
| O2 | NH2 | ARG- 121 | 3.01 | 162.78 | H-Bond (Protein Donor) |
| C7 | CG1 | VAL- 350 | 3.75 | 0 | Hydrophobic |
| C13 | CG1 | VAL- 350 | 3.36 | 0 | Hydrophobic |
| C2 | CD1 | LEU- 353 | 4.01 | 0 | Hydrophobic |
| C10 | CB | LEU- 353 | 4.49 | 0 | Hydrophobic |
| C6 | CB | SER- 354 | 4.4 | 0 | Hydrophobic |
| C9 | CB | SER- 354 | 4.06 | 0 | Hydrophobic |
| C6 | CE2 | TYR- 356 | 3.53 | 0 | Hydrophobic |
| C7 | CD1 | LEU- 360 | 3.92 | 0 | Hydrophobic |
| C5 | CE2 | TYR- 386 | 4.01 | 0 | Hydrophobic |
| C5 | CZ2 | TRP- 388 | 3.89 | 0 | Hydrophobic |
| C4 | CE2 | PHE- 519 | 4.45 | 0 | Hydrophobic |
| C9 | CG1 | VAL- 524 | 4.43 | 0 | Hydrophobic |
| C13 | CB | ALA- 528 | 3.62 | 0 | Hydrophobic |
| C12 | CB | ALA- 528 | 3.85 | 0 | Hydrophobic |
| C12 | CB | SER- 531 | 4.2 | 0 | Hydrophobic |
| C7 | CD1 | LEU- 532 | 4.32 | 0 | Hydrophobic |
| C13 | CD2 | LEU- 532 | 4.26 | 0 | Hydrophobic |
