sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.000 Å
X-ray
2012-09-10
| Name: | Protein-tyrosine kinase 2-beta |
|---|---|
| ID: | FAK2_HUMAN |
| AC: | Q14289 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 2.7.10.2 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 21.175 |
|---|---|
| Number of residues: | 38 |
| Including | |
| Standard Amino Acids: | 37 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.484 | 907.875 |
| % Hydrophobic | % Polar |
|---|---|
| 63.94 | 36.06 |
| According to VolSite | |
| HET Code: | 0YH |
|---|---|
| Formula: | C26H30N6O2 |
| Molecular weight: | 458.555 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 69.06 % |
| Polar Surface area: | 96.86 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 4 |
| H-Bond Donors: | 3 |
| Rings: | 4 |
| Aromatic rings: | 4 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| -4.81679 | -2.91426 | 11.2079 |
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 | CD1 | LEU- 431 | 4.03 | 0 | Hydrophobic |
| C12 | CB | ALA- 455 | 4.39 | 0 | Hydrophobic |
| N27 | NZ | LYS- 457 | 3.07 | 143.87 | H-Bond (Protein Donor) |
| N31 | OE2 | GLU- 474 | 2.81 | 140.74 | H-Bond (Ligand Donor) |
| C16 | CB | GLU- 474 | 3.85 | 0 | Hydrophobic |
| C7 | CG | GLU- 474 | 3.69 | 0 | Hydrophobic |
| C8 | CD1 | ILE- 477 | 3.99 | 0 | Hydrophobic |
| C10 | CG2 | ILE- 477 | 4.2 | 0 | Hydrophobic |
| C3 | SD | MET- 478 | 4.2 | 0 | Hydrophobic |
| C10 | SD | MET- 478 | 3.94 | 0 | Hydrophobic |
| C3 | CD1 | LEU- 481 | 3.98 | 0 | Hydrophobic |
| C3 | CG2 | ILE- 486 | 3.79 | 0 | Hydrophobic |
| C4 | CG2 | ILE- 486 | 4.18 | 0 | Hydrophobic |
| C12 | CB | MET- 502 | 4.14 | 0 | Hydrophobic |
| C6 | CD1 | LEU- 504 | 3.84 | 0 | Hydrophobic |
| C19 | CD1 | LEU- 504 | 4.26 | 0 | Hydrophobic |
| O34 | N | TYR- 505 | 3.12 | 176.17 | H-Bond (Protein Donor) |
| C3 | CD2 | LEU- 540 | 4.16 | 0 | Hydrophobic |
| C5 | CD1 | LEU- 540 | 3.81 | 0 | Hydrophobic |
| C6 | CD2 | LEU- 556 | 3.89 | 0 | Hydrophobic |
| C11 | CD1 | LEU- 556 | 3.49 | 0 | Hydrophobic |
| C4 | CG | LEU- 565 | 3.95 | 0 | Hydrophobic |
| O33 | N | ASP- 567 | 2.89 | 168.38 | H-Bond (Protein Donor) |
| C5 | CB | ASP- 567 | 4.16 | 0 | Hydrophobic |
| C2 | CD2 | PHE- 568 | 3.7 | 0 | Hydrophobic |
| DuAr | CZ | ARG- 572 | 3.78 | 155.11 | Pi/Cation |
| C9 | CD | ARG- 572 | 3.72 | 0 | Hydrophobic |
| C8 | CB | ASP- 576 | 3.98 | 0 | Hydrophobic |
| N29 | O | HOH- 803 | 2.91 | 165.68 | H-Bond (Protein Donor) |
