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
2010-05-28
| Min | Mean | Median | Standard Deviation | Max | Count | |
|---|---|---|---|---|---|---|
| pChEMBL: | 6.000 | 6.000 | 6.000 | 0.000 | 6.000 | 1 |
| 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: | 58.179 |
|---|---|
| Number of residues: | 27 |
| Including | |
| Standard Amino Acids: | 26 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.383 | 793.125 |
| % Hydrophobic | % Polar |
|---|---|
| 73.19 | 26.81 |
| According to VolSite | |
| HET Code: | FLP |
|---|---|
| Formula: | C15H12FO2 |
| Molecular weight: | 243.253 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 76.62 % |
| Polar Surface area: | 40.12 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| 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 |
|---|---|---|
| -21.0132 | 50.2354 | 10.1062 |
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 | 3.89 | 0 | Hydrophobic |
| O | NE | ARG- 120 | 2.74 | 144.93 | H-Bond (Protein Donor) |
| O1 | NE | ARG- 120 | 3.06 | 141.82 | H-Bond (Protein Donor) |
| O1 | NH2 | ARG- 120 | 2.79 | 154.2 | H-Bond (Protein Donor) |
| O | CZ | ARG- 120 | 3.67 | 0 | Ionic (Protein Cationic) |
| O1 | CZ | ARG- 120 | 3.36 | 0 | Ionic (Protein Cationic) |
| C3 | CG2 | VAL- 349 | 4.22 | 0 | Hydrophobic |
| C13 | CG1 | VAL- 349 | 3.94 | 0 | Hydrophobic |
| C8 | CG1 | VAL- 349 | 3.37 | 0 | Hydrophobic |
| F | CD2 | LEU- 352 | 3.6 | 0 | Hydrophobic |
| C3 | CD2 | LEU- 352 | 3.4 | 0 | Hydrophobic |
| C10 | CB | SER- 353 | 4.06 | 0 | Hydrophobic |
| O1 | OH | TYR- 355 | 3.35 | 148.58 | H-Bond (Protein Donor) |
| C12 | CE1 | TYR- 355 | 3.55 | 0 | Hydrophobic |
| C13 | CD1 | LEU- 359 | 3.9 | 0 | Hydrophobic |
| C | CD2 | LEU- 384 | 4.1 | 0 | Hydrophobic |
| C5 | CH2 | TRP- 387 | 3.45 | 0 | Hydrophobic |
| F | CZ | PHE- 518 | 4.3 | 0 | Hydrophobic |
| C10 | CG2 | ILE- 523 | 4.18 | 0 | Hydrophobic |
| F | CG1 | ILE- 523 | 4.21 | 0 | Hydrophobic |
| C8 | CB | ALA- 527 | 3.54 | 0 | Hydrophobic |
| C7 | CB | SER- 530 | 3.96 | 0 | Hydrophobic |
| C3 | CB | SER- 530 | 3.57 | 0 | Hydrophobic |
| C7 | CG | LEU- 531 | 4.2 | 0 | Hydrophobic |
| C8 | CD2 | LEU- 531 | 3.72 | 0 | Hydrophobic |
| C13 | CD2 | LEU- 531 | 4.41 | 0 | Hydrophobic |
