sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.800 Å
X-ray
2010-04-28
| 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 |
|---|---|
| D | 100 % |
| B-Factor: | 48.520 |
|---|---|
| Number of residues: | 31 |
| Including | |
| Standard Amino Acids: | 31 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.441 | 1269.000 |
| % Hydrophobic | % Polar |
|---|---|
| 58.78 | 41.22 |
| According to VolSite | |
| HET Code: | 416 |
|---|---|
| Formula: | C15H13ClF3O3 |
| Molecular weight: | 333.710 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 61.15 % |
| Polar Surface area: | 49.36 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 3 |
| H-Bond Donors: | 0 |
| Rings: | 2 |
| Aromatic rings: | 1 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 3 |
| X | Y | Z |
|---|---|---|
| 33.2511 | -46.7242 | 15.6487 |
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 |
| C1 | CG1 | VAL- 335 | 3.61 | 0 | Hydrophobic |
| C6 | CG1 | VAL- 335 | 3.95 | 0 | Hydrophobic |
| C14 | CD2 | LEU- 338 | 3.52 | 0 | Hydrophobic |
| C10 | CB | SER- 339 | 4.35 | 0 | Hydrophobic |
| C11 | CB | SER- 339 | 4.36 | 0 | Hydrophobic |
| C10 | CZ | TYR- 341 | 4.09 | 0 | Hydrophobic |
| C11 | CE2 | TYR- 341 | 4.11 | 0 | Hydrophobic |
| C11 | CD1 | LEU- 345 | 4.5 | 0 | Hydrophobic |
| F2 | CE1 | TYR- 371 | 4.29 | 0 | Hydrophobic |
| O3 | OH | TYR- 371 | 3.5 | 173.52 | H-Bond (Protein Donor) |
| F2 | CZ2 | TRP- 373 | 3.94 | 0 | Hydrophobic |
| F3 | CE2 | PHE- 504 | 3.83 | 0 | Hydrophobic |
| F3 | CG | MET- 508 | 4.47 | 0 | Hydrophobic |
| F1 | CG1 | VAL- 509 | 4.29 | 0 | Hydrophobic |
| F3 | CG2 | VAL- 509 | 3.79 | 0 | Hydrophobic |
| C2 | CG1 | VAL- 509 | 3.75 | 0 | Hydrophobic |
| C10 | CG1 | VAL- 509 | 3.55 | 0 | Hydrophobic |
| F1 | CB | ALA- 513 | 4.28 | 0 | Hydrophobic |
| CL1 | CB | ALA- 513 | 3.82 | 0 | Hydrophobic |
| C9 | CB | ALA- 513 | 3.86 | 0 | Hydrophobic |
| C5 | CB | ALA- 513 | 3.96 | 0 | Hydrophobic |
| C4 | CB | ALA- 513 | 3.58 | 0 | Hydrophobic |
| O3 | OG | SER- 516 | 2.83 | 148.77 | H-Bond (Protein Donor) |
| CL1 | CD2 | LEU- 517 | 4.16 | 0 | Hydrophobic |
