sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.840 Å
X-ray
2011-04-28
| 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 |
|---|---|
| C | 100 % |
| B-Factor: | 40.392 |
|---|---|
| Number of residues: | 27 |
| Including | |
| Standard Amino Acids: | 26 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.576 | 1161.000 |
| % Hydrophobic | % Polar |
|---|---|
| 63.37 | 36.63 |
| According to VolSite | |
| HET Code: | FLR |
|---|---|
| Formula: | C15H12FO2 |
| Molecular weight: | 243.253 g/mol |
| DrugBank ID: | DB05289 |
| Buried Surface Area: | 72.96 % |
| Polar Surface area: | 40.12 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| H-Bond Donors: | 0 |
| Rings: | 2 |
| Aromatic rings: | 2 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 3 |
| X | Y | Z |
|---|---|---|
| 74.4172 | -52.5691 | 8.44839 |
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 |
| O1 | NH2 | ARG- 120 | 3.34 | 149.88 | H-Bond (Protein Donor) |
| O | NE | ARG- 120 | 2.94 | 163.44 | H-Bond (Protein Donor) |
| O | CZ | ARG- 120 | 3.69 | 0 | Ionic (Protein Cationic) |
| C13 | CG1 | VAL- 349 | 3.6 | 0 | Hydrophobic |
| C8 | CG1 | VAL- 349 | 3.58 | 0 | Hydrophobic |
| C1 | CD2 | LEU- 352 | 4.38 | 0 | Hydrophobic |
| C11 | CD1 | LEU- 352 | 3.71 | 0 | Hydrophobic |
| C13 | CB | SER- 353 | 4.42 | 0 | Hydrophobic |
| C13 | CE2 | TYR- 355 | 3.9 | 0 | Hydrophobic |
| O1 | OH | TYR- 355 | 2.77 | 127.29 | H-Bond (Protein Donor) |
| C13 | CD1 | LEU- 359 | 3.51 | 0 | Hydrophobic |
| C5 | CD1 | LEU- 384 | 4.31 | 0 | Hydrophobic |
| C11 | CG1 | VAL- 523 | 4.47 | 0 | Hydrophobic |
| F | CG2 | VAL- 523 | 3.47 | 0 | Hydrophobic |
| C12 | CB | ALA- 527 | 4.16 | 0 | Hydrophobic |
| C8 | CB | ALA- 527 | 3.38 | 0 | Hydrophobic |
| C7 | CB | SER- 530 | 3.82 | 0 | Hydrophobic |
| C1 | CB | SER- 530 | 3.53 | 0 | Hydrophobic |
| C8 | CD1 | LEU- 531 | 3.92 | 0 | Hydrophobic |
| C12 | CD1 | LEU- 531 | 4.13 | 0 | Hydrophobic |
