sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.050 Å
X-ray
2013-02-28
| Name: | Peptidyl-prolyl cis-trans isomerase FKBP5 |
|---|---|
| ID: | FKBP5_HUMAN |
| AC: | Q13451 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 5.2.1.8 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 13.816 |
|---|---|
| Number of residues: | 23 |
| Including | |
| Standard Amino Acids: | 22 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.587 | 249.750 |
| % Hydrophobic | % Polar |
|---|---|
| 48.65 | 51.35 |
| According to VolSite | |
| HET Code: | 1KT |
|---|---|
| Formula: | C28H32N2O8 |
| Molecular weight: | 524.562 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 52.03 % |
| Polar Surface area: | 103.84 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 8 |
| H-Bond Donors: | 0 |
| Rings: | 5 |
| Aromatic rings: | 2 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 7 |
| X | Y | Z |
|---|---|---|
| 29.2611 | 11.9917 | -20.1196 |
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 | CZ | TYR- 57 | 3.58 | 0 | Hydrophobic |
| O5 | OH | TYR- 57 | 3.14 | 133.67 | H-Bond (Protein Donor) |
| C25 | CB | ASP- 68 | 3.87 | 0 | Hydrophobic |
| C30 | CB | ASP- 68 | 3.77 | 0 | Hydrophobic |
| C26 | CE1 | PHE- 77 | 4.19 | 0 | Hydrophobic |
| C15 | CZ | PHE- 77 | 3.82 | 0 | Hydrophobic |
| C14 | CE2 | PHE- 77 | 3.67 | 0 | Hydrophobic |
| C14 | CG1 | VAL- 86 | 3.97 | 0 | Hydrophobic |
| C13 | CB | VAL- 86 | 4.42 | 0 | Hydrophobic |
| O3 | N | ILE- 87 | 2.85 | 151.03 | H-Bond (Protein Donor) |
| C13 | CG1 | ILE- 87 | 4.4 | 0 | Hydrophobic |
| C15 | CH2 | TRP- 90 | 4.22 | 0 | Hydrophobic |
| C14 | CE3 | TRP- 90 | 3.65 | 0 | Hydrophobic |
| C13 | CE2 | TRP- 90 | 3.35 | 0 | Hydrophobic |
| O4 | OH | TYR- 113 | 2.72 | 160.79 | H-Bond (Protein Donor) |
| C28 | CE1 | TYR- 113 | 3.52 | 0 | Hydrophobic |
| C28 | CB | SER- 118 | 3.75 | 0 | Hydrophobic |
| C24 | CD | LYS- 121 | 3.92 | 0 | Hydrophobic |
| C30 | CD | LYS- 121 | 3.76 | 0 | Hydrophobic |
| C23 | CG | LYS- 121 | 4.26 | 0 | Hydrophobic |
| C13 | CZ | PHE- 130 | 4.43 | 0 | Hydrophobic |
