sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.400 Å
X-ray
2011-01-04
| 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: | 24.257 |
|---|---|
| Number of residues: | 30 |
| Including | |
| Standard Amino Acids: | 27 |
| Non Standard Amino Acids: | 2 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | CL |
| Ligandability | Volume (Å3) |
|---|---|
| 1.504 | 948.375 |
| % Hydrophobic | % Polar |
|---|---|
| 64.77 | 35.23 |
| According to VolSite | |
| HET Code: | NPX |
|---|---|
| Formula: | C14H13O3 |
| Molecular weight: | 229.251 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 75.46 % |
| Polar Surface area: | 49.36 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 3 |
| 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 |
|---|---|---|
| -40.4294 | 51.0458 | 22.2139 |
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 |
| O | CZ | ARG- 120 | 3.73 | 0 | Ionic (Protein Cationic) |
| OXT | CZ | ARG- 120 | 3.89 | 0 | Ionic (Protein Cationic) |
| O | NH2 | ARG- 120 | 2.87 | 149.19 | H-Bond (Protein Donor) |
| OXT | NE | ARG- 120 | 3.19 | 160.11 | H-Bond (Protein Donor) |
| C13 | CG2 | VAL- 349 | 4.05 | 0 | Hydrophobic |
| C10 | CG1 | VAL- 349 | 3.85 | 0 | Hydrophobic |
| C11 | CG1 | VAL- 349 | 3.51 | 0 | Hydrophobic |
| C4 | CD1 | LEU- 352 | 3.58 | 0 | Hydrophobic |
| C10 | CB | SER- 353 | 3.33 | 0 | Hydrophobic |
| O | OH | TYR- 355 | 2.85 | 134.87 | H-Bond (Protein Donor) |
| C10 | CE2 | TYR- 355 | 3.49 | 0 | Hydrophobic |
| C10 | CD1 | LEU- 359 | 4.41 | 0 | Hydrophobic |
| C12 | CE1 | PHE- 381 | 3.87 | 0 | Hydrophobic |
| C12 | CD1 | LEU- 384 | 4.27 | 0 | Hydrophobic |
| C12 | CZ | TYR- 385 | 3.43 | 0 | Hydrophobic |
| C12 | CZ2 | TRP- 387 | 3.88 | 0 | Hydrophobic |
| C7 | CG1 | VAL- 523 | 4.01 | 0 | Hydrophobic |
| C8 | CB | ALA- 527 | 3.67 | 0 | Hydrophobic |
| C12 | CB | SER- 530 | 4.4 | 0 | Hydrophobic |
| C13 | CB | SER- 530 | 3.65 | 0 | Hydrophobic |
| C11 | CD2 | LEU- 531 | 4.07 | 0 | Hydrophobic |
