sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.750 Å
X-ray
2000-12-28
| Name: | Prostaglandin G/H synthase 1 |
|---|---|
| ID: | PGH1_SHEEP |
| AC: | P05979 |
| Organism: | Ovis aries |
| Reign: | Eukaryota |
| TaxID: | 9940 |
| EC Number: | 1.14.99.1 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 35.088 |
|---|---|
| Number of residues: | 27 |
| Including | |
| Standard Amino Acids: | 26 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.761 | 597.375 |
| % Hydrophobic | % Polar |
|---|---|
| 65.54 | 34.46 |
| According to VolSite | |
| HET Code: | FL2 |
|---|---|
| Formula: | C16H15FO2 |
| Molecular weight: | 258.288 g/mol |
| DrugBank ID: | DB03753 |
| Buried Surface Area: | 72.43 % |
| Polar Surface area: | 26.3 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| H-Bond Donors: | 0 |
| Rings: | 2 |
| Aromatic rings: | 2 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 4 |
| X | Y | Z |
|---|---|---|
| 26.5544 | 33.5872 | 201.282 |
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 |
| C13 | CG1 | VAL- 116 | 4.35 | 0 | Hydrophobic |
| C16 | CG1 | VAL- 116 | 3.2 | 0 | Hydrophobic |
| O | NH2 | ARG- 120 | 3.12 | 159.99 | H-Bond (Protein Donor) |
| O1 | NH2 | ARG- 120 | 3.05 | 134.75 | H-Bond (Protein Donor) |
| O1 | NE | ARG- 120 | 2.7 | 159.77 | H-Bond (Protein Donor) |
| C16 | CG | ARG- 120 | 3.29 | 0 | Hydrophobic |
| C3 | CG2 | VAL- 349 | 4.45 | 0 | Hydrophobic |
| C13 | CG1 | VAL- 349 | 4.02 | 0 | Hydrophobic |
| C8 | CG1 | VAL- 349 | 3.54 | 0 | Hydrophobic |
| F | CD1 | LEU- 352 | 4.28 | 0 | Hydrophobic |
| C4 | CD1 | LEU- 352 | 3.72 | 0 | Hydrophobic |
| C10 | CB | SER- 353 | 4.19 | 0 | Hydrophobic |
| C12 | CB | SER- 353 | 4.38 | 0 | Hydrophobic |
| C12 | CE1 | TYR- 355 | 3.48 | 0 | Hydrophobic |
| C13 | CD2 | LEU- 359 | 3.71 | 0 | Hydrophobic |
| C | CD2 | LEU- 384 | 4.22 | 0 | Hydrophobic |
| C5 | CZ2 | TRP- 387 | 3.39 | 0 | Hydrophobic |
| F | CZ | PHE- 518 | 4.14 | 0 | Hydrophobic |
| F | CG1 | ILE- 523 | 3.9 | 0 | Hydrophobic |
| C10 | CG2 | ILE- 523 | 4.07 | 0 | Hydrophobic |
| C16 | CB | ALA- 527 | 3.71 | 0 | Hydrophobic |
| C8 | CB | ALA- 527 | 3.7 | 0 | Hydrophobic |
| C7 | CB | SER- 530 | 4.13 | 0 | Hydrophobic |
| C3 | CB | SER- 530 | 3.77 | 0 | Hydrophobic |
| C8 | CG | LEU- 531 | 4.24 | 0 | Hydrophobic |
| C16 | CD1 | LEU- 531 | 3.27 | 0 | Hydrophobic |
