sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
3.000 Å
X-ray
1996-12-17
| 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 |
|---|---|
| B | 100 % |
| B-Factor: | 6.806 |
|---|---|
| Number of residues: | 37 |
| Including | |
| Standard Amino Acids: | 37 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.740 | 513.000 |
| % Hydrophobic | % Polar |
|---|---|
| 73.68 | 26.32 |
| According to VolSite | |
| HET Code: | S58 |
|---|---|
| Formula: | C16H11BrF3N3O2S |
| Molecular weight: | 446.242 g/mol |
| DrugBank ID: | DB03477 |
| Buried Surface Area: | 75.98 % |
| Polar Surface area: | 86.36 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 3 |
| H-Bond Donors: | 1 |
| Rings: | 3 |
| Aromatic rings: | 3 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 4 |
| X | Y | Z |
|---|---|---|
| 71.4454 | 14.9737 | 9.36419 |
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 |
| N3 | NE2 | HIS- 90 | 2.76 | 166.47 | H-Bond (Ligand Donor) |
| F3 | CB | VAL- 116 | 4.45 | 0 | Hydrophobic |
| F2 | CG | ARG- 120 | 4.07 | 0 | Hydrophobic |
| C4 | CD | ARG- 120 | 4.11 | 0 | Hydrophobic |
| C12 | CG1 | VAL- 349 | 4.32 | 0 | Hydrophobic |
| F1 | CG1 | VAL- 349 | 3.59 | 0 | Hydrophobic |
| C10 | CD2 | LEU- 352 | 3.25 | 0 | Hydrophobic |
| C13 | CD2 | LEU- 352 | 3.74 | 0 | Hydrophobic |
| C6 | CB | SER- 353 | 3.88 | 0 | Hydrophobic |
| F3 | CE2 | TYR- 355 | 3.22 | 0 | Hydrophobic |
| F1 | CD1 | LEU- 359 | 3.63 | 0 | Hydrophobic |
| BR1 | CE1 | PHE- 381 | 4.31 | 0 | Hydrophobic |
| BR1 | CD1 | LEU- 384 | 4.46 | 0 | Hydrophobic |
| BR1 | CZ | TYR- 385 | 3.72 | 0 | Hydrophobic |
| BR1 | CZ2 | TRP- 387 | 3.66 | 0 | Hydrophobic |
| C9 | CE1 | PHE- 518 | 3.48 | 0 | Hydrophobic |
| C16 | CG1 | VAL- 523 | 4.23 | 0 | Hydrophobic |
| C9 | CG2 | VAL- 523 | 3.47 | 0 | Hydrophobic |
| C6 | CG1 | VAL- 523 | 3.65 | 0 | Hydrophobic |
| F2 | CB | ALA- 527 | 4.31 | 0 | Hydrophobic |
| C16 | CB | ALA- 527 | 3.53 | 0 | Hydrophobic |
| C13 | CB | SER- 530 | 4.2 | 0 | Hydrophobic |
| F2 | CD1 | LEU- 531 | 3.67 | 0 | Hydrophobic |
