sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.740 Å
X-ray
2015-08-06
| Name: | 14-3-3 protein zeta/delta |
|---|---|
| ID: | 1433Z_HUMAN |
| AC: | P63104 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| B | 91 % |
| C | 9 % |
| B-Factor: | 55.541 |
|---|---|
| Number of residues: | 33 |
| Including | |
| Standard Amino Acids: | 33 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.817 | 675.000 |
| % Hydrophobic | % Polar |
|---|---|
| 52.50 | 47.50 |
| According to VolSite | |
| HET Code: | FSC |
|---|---|
| Formula: | C36H56O12 |
| Molecular weight: | 680.823 g/mol |
| DrugBank ID: | DB01780 |
| Buried Surface Area: | 47.42 % |
| Polar Surface area: | 170.43 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 12 |
| H-Bond Donors: | 4 |
| Rings: | 4 |
| Aromatic rings: | 0 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 2 |
| Rotatable Bonds: | 14 |
| X | Y | Z |
|---|---|---|
| 6.32123 | -14.411 | 21.6166 |
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 |
| C7 | CB | ASN- 42 | 3.66 | 0 | Hydrophobic |
| C47 | CB | ASN- 42 | 4.42 | 0 | Hydrophobic |
| C47 | CD2 | LEU- 43 | 4.27 | 0 | Hydrophobic |
| C27 | CB | SER- 45 | 4.47 | 0 | Hydrophobic |
| C38 | CB | SER- 45 | 4.1 | 0 | Hydrophobic |
| C6 | CG2 | VAL- 46 | 4.15 | 0 | Hydrophobic |
| C7 | CG2 | VAL- 46 | 4.08 | 0 | Hydrophobic |
| C47 | CG2 | VAL- 46 | 3.73 | 0 | Hydrophobic |
| C27 | CE2 | PHE- 119 | 3.72 | 0 | Hydrophobic |
| C38 | CZ | PHE- 119 | 3.41 | 0 | Hydrophobic |
| C23 | CE2 | PHE- 119 | 3.63 | 0 | Hydrophobic |
| O32 | NZ | LYS- 122 | 3.35 | 131.67 | H-Bond (Protein Donor) |
| C38 | CD | LYS- 122 | 4.29 | 0 | Hydrophobic |
| C26 | CD | LYS- 122 | 3.82 | 0 | Hydrophobic |
| C38 | CG | MET- 123 | 3.43 | 0 | Hydrophobic |
| C9 | CB | PRO- 167 | 4.12 | 0 | Hydrophobic |
| C23 | CG1 | ILE- 168 | 3.78 | 0 | Hydrophobic |
| C36 | CB | LYS- 214 | 4.36 | 0 | Hydrophobic |
| C36 | CB | ASP- 215 | 4.07 | 0 | Hydrophobic |
| C28 | CB | ASP- 215 | 4.39 | 0 | Hydrophobic |
| C11 | CB | ASP- 215 | 3.93 | 0 | Hydrophobic |
| O16 | OD2 | ASP- 215 | 3.29 | 164.09 | H-Bond (Ligand Donor) |
| C18 | CD2 | LEU- 218 | 3.78 | 0 | Hydrophobic |
| C17 | CD2 | LEU- 218 | 4.27 | 0 | Hydrophobic |
| C36 | CD2 | LEU- 218 | 4.31 | 0 | Hydrophobic |
| C18 | CG1 | ILE- 219 | 4.17 | 0 | Hydrophobic |
| C25 | CD1 | ILE- 219 | 3.81 | 0 | Hydrophobic |
| C18 | CG1 | VAL- 779 | 4.27 | 0 | Hydrophobic |
| C10 | CG1 | VAL- 779 | 4.07 | 0 | Hydrophobic |
| C25 | CG1 | VAL- 779 | 4.44 | 0 | Hydrophobic |
