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
2006-10-17
| Name: | Serine/threonine-protein kinase 10 |
|---|---|
| ID: | STK10_HUMAN |
| AC: | O94804 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 2.7.11.1 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 40.092 |
|---|---|
| Number of residues: | 39 |
| Including | |
| Standard Amino Acids: | 37 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | CA |
| Ligandability | Volume (Å3) |
|---|---|
| 0.977 | 934.875 |
| % Hydrophobic | % Polar |
|---|---|
| 55.96 | 44.04 |
| According to VolSite | |
| HET Code: | 274 |
|---|---|
| Formula: | C28H31ClN5O4S |
| Molecular weight: | 569.095 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 57.93 % |
| Polar Surface area: | 115.39 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 4 |
| H-Bond Donors: | 3 |
| Rings: | 5 |
| Aromatic rings: | 3 |
| Anionic atoms: | 0 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 5 |
| X | Y | Z |
|---|---|---|
| -5.8271 | 36.717 | 19.4606 |
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 |
| C23 | CD2 | LEU- 42 | 4.19 | 0 | Hydrophobic |
| C7 | CG2 | VAL- 50 | 4.02 | 0 | Hydrophobic |
| C6 | CG1 | VAL- 50 | 4.24 | 0 | Hydrophobic |
| C12 | CB | ALA- 63 | 3.74 | 0 | Hydrophobic |
| C11 | CB | ALA- 63 | 3.83 | 0 | Hydrophobic |
| C6 | CB | ALA- 63 | 4.22 | 0 | Hydrophobic |
| CL1 | CD | LYS- 65 | 4.41 | 0 | Hydrophobic |
| C4 | CB | LYS- 65 | 3.91 | 0 | Hydrophobic |
| C5 | CG | LYS- 65 | 4.14 | 0 | Hydrophobic |
| C2 | CD | LYS- 65 | 4.03 | 0 | Hydrophobic |
| CL1 | CD2 | TYR- 78 | 4.17 | 0 | Hydrophobic |
| CL1 | CG | GLU- 81 | 4.5 | 0 | Hydrophobic |
| C11 | CG1 | VAL- 94 | 3.93 | 0 | Hydrophobic |
| CL1 | CD1 | ILE- 108 | 3.78 | 0 | Hydrophobic |
| C4 | CG2 | ILE- 108 | 3.92 | 0 | Hydrophobic |
| C11 | CG2 | ILE- 110 | 3.67 | 0 | Hydrophobic |
| C2 | CD1 | ILE- 110 | 3.5 | 0 | Hydrophobic |
| C4 | CD1 | ILE- 110 | 3.4 | 0 | Hydrophobic |
| N2 | O | GLU- 111 | 2.92 | 154.06 | H-Bond (Ligand Donor) |
| C23 | CE1 | PHE- 112 | 4.06 | 0 | Hydrophobic |
| O3 | N | CYS- 113 | 2.89 | 167.97 | H-Bond (Protein Donor) |
| O4 | N | ALA- 117 | 2.97 | 170.27 | H-Bond (Protein Donor) |
| C21 | CB | ALA- 117 | 4.39 | 0 | Hydrophobic |
| C21 | CD2 | LEU- 164 | 4.38 | 0 | Hydrophobic |
| C12 | CD1 | LEU- 164 | 3.32 | 0 | Hydrophobic |
| C8 | CB | ALA- 174 | 4.05 | 0 | Hydrophobic |
| O2 | N | ASP- 175 | 2.78 | 140.69 | H-Bond (Protein Donor) |
| O2 | O | HOH- 2007 | 2.82 | 153.26 | H-Bond (Protein Donor) |
