sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.900 Å
X-ray
1996-12-18
| 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: | 8.564 |
|---|---|
| Number of residues: | 34 |
| Including | |
| Standard Amino Acids: | 34 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.452 | 1177.875 |
| % Hydrophobic | % Polar |
|---|---|
| 58.17 | 41.83 |
| According to VolSite | |
| HET Code: | IMN |
|---|---|
| Formula: | C19H15ClNO4 |
| Molecular weight: | 356.780 g/mol |
| DrugBank ID: | DB00328 |
| Buried Surface Area: | 68.31 % |
| Polar Surface area: | 71.36 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 4 |
| H-Bond Donors: | 0 |
| Rings: | 3 |
| Aromatic rings: | 3 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 4 |
| X | Y | Z |
|---|---|---|
| 24.8487 | 22.2946 | 15.1256 |
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 |
| O2 | CZ | ARG- 120 | 3.41 | 0 | Ionic (Protein Cationic) |
| C16 | CG1 | VAL- 349 | 3.6 | 0 | Hydrophobic |
| C17 | CG1 | VAL- 349 | 4.16 | 0 | Hydrophobic |
| C1 | CG1 | VAL- 349 | 4.28 | 0 | Hydrophobic |
| C5 | CB | LEU- 352 | 4.14 | 0 | Hydrophobic |
| C6 | CB | SER- 353 | 4.35 | 0 | Hydrophobic |
| C3 | CB | SER- 353 | 3.41 | 0 | Hydrophobic |
| C6 | CE1 | TYR- 355 | 4.36 | 0 | Hydrophobic |
| C17 | CE2 | TYR- 355 | 4.41 | 0 | Hydrophobic |
| O2 | OH | TYR- 355 | 3.08 | 146.07 | H-Bond (Protein Donor) |
| CL | CE1 | PHE- 381 | 4 | 0 | Hydrophobic |
| CL | CB | LEU- 384 | 3.61 | 0 | Hydrophobic |
| CL | CD2 | TYR- 385 | 4.29 | 0 | Hydrophobic |
| CL | CZ2 | TRP- 387 | 4.11 | 0 | Hydrophobic |
| CL | SD | MET- 522 | 3.93 | 0 | Hydrophobic |
| C6 | CG2 | VAL- 523 | 3.78 | 0 | Hydrophobic |
| C2 | CG1 | VAL- 523 | 3.9 | 0 | Hydrophobic |
| C4 | CG2 | VAL- 523 | 3.35 | 0 | Hydrophobic |
| C15 | CB | ALA- 527 | 4.12 | 0 | Hydrophobic |
| C16 | CB | ALA- 527 | 3.78 | 0 | Hydrophobic |
| C17 | CB | ALA- 527 | 4.29 | 0 | Hydrophobic |
| C1 | CB | ALA- 527 | 4.39 | 0 | Hydrophobic |
| C16 | CB | SER- 530 | 4.29 | 0 | Hydrophobic |
| C10 | CB | SER- 530 | 4.09 | 0 | Hydrophobic |
| C16 | CG | LEU- 531 | 3.49 | 0 | Hydrophobic |
| C17 | CD1 | LEU- 531 | 4.42 | 0 | Hydrophobic |
