sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.980 Å
X-ray
2013-06-19
| Name: | Abscisic acid receptor PYL2 |
|---|---|
| ID: | PYL2_ARATH |
| AC: | O80992 |
| Organism: | Arabidopsis thaliana |
| Reign: | Eukaryota |
| TaxID: | 3702 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 91 % |
| B | 9 % |
| B-Factor: | 25.496 |
|---|---|
| Number of residues: | 35 |
| Including | |
| Standard Amino Acids: | 32 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 3 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.175 | 486.000 |
| % Hydrophobic | % Polar |
|---|---|
| 61.81 | 38.19 |
| According to VolSite | |
| HET Code: | A1O |
|---|---|
| Formula: | C20H24N2O3S |
| Molecular weight: | 372.481 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 74.23 % |
| Polar Surface area: | 74.86 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 3 |
| H-Bond Donors: | 1 |
| Rings: | 3 |
| Aromatic rings: | 2 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| 19.4334 | -13.4118 | -13.5503 |
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 |
| C15 | CD | LYS- 64 | 3.93 | 0 | Hydrophobic |
| C18 | CD | LYS- 64 | 4.23 | 0 | Hydrophobic |
| C3 | CB | PHE- 66 | 4.21 | 0 | Hydrophobic |
| C6 | CD2 | PHE- 66 | 4.35 | 0 | Hydrophobic |
| C14 | CE2 | PHE- 66 | 3.95 | 0 | Hydrophobic |
| C5 | CG1 | VAL- 85 | 4.22 | 0 | Hydrophobic |
| C3 | CG1 | VAL- 87 | 4.02 | 0 | Hydrophobic |
| C14 | CD1 | LEU- 91 | 4.09 | 0 | Hydrophobic |
| C12 | CB | ALA- 93 | 4.45 | 0 | Hydrophobic |
| C9 | CB | SER- 96 | 4.13 | 0 | Hydrophobic |
| C7 | CB | SER- 96 | 3.55 | 0 | Hydrophobic |
| C15 | CZ | PHE- 112 | 3.88 | 0 | Hydrophobic |
| C17 | CG2 | VAL- 114 | 4.27 | 0 | Hydrophobic |
| C12 | CB | HIS- 119 | 4.03 | 0 | Hydrophobic |
| C12 | CD1 | LEU- 121 | 3.48 | 0 | Hydrophobic |
| C19 | CD1 | LEU- 121 | 4.43 | 0 | Hydrophobic |
| C20 | CD1 | LEU- 121 | 3.59 | 0 | Hydrophobic |
| C20 | CZ | TYR- 124 | 3.7 | 0 | Hydrophobic |
| C6 | CZ | PHE- 165 | 3.63 | 0 | Hydrophobic |
| C14 | CE1 | PHE- 165 | 4.08 | 0 | Hydrophobic |
| C20 | CG1 | VAL- 166 | 4.38 | 0 | Hydrophobic |
| C10 | CG1 | VAL- 169 | 4.11 | 0 | Hydrophobic |
| C20 | CG1 | VAL- 169 | 4.27 | 0 | Hydrophobic |
| C6 | CG2 | VAL- 169 | 3.87 | 0 | Hydrophobic |
| O2 | O | HOH- 303 | 3.17 | 155.91 | H-Bond (Protein Donor) |
| O3 | O | HOH- 317 | 2.87 | 153.35 | H-Bond (Protein Donor) |
| C14 | CG1 | VAL- 393 | 4.36 | 0 | Hydrophobic |
