sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.950 Å
X-ray
2010-08-10
| Min | Mean | Median | Standard Deviation | Max | Count | |
|---|---|---|---|---|---|---|
| pChEMBL: | 8.850 | 8.850 | 8.850 | 0.000 | 8.850 | 2 |
| Name: | Tyrosine-protein kinase BTK |
|---|---|
| ID: | BTK_HUMAN |
| AC: | Q06187 |
| 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: | 27.006 |
|---|---|
| Number of residues: | 36 |
| Including | |
| Standard Amino Acids: | 36 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.379 | 641.250 |
| % Hydrophobic | % Polar |
|---|---|
| 53.68 | 46.32 |
| According to VolSite | |
| HET Code: | 1N1 |
|---|---|
| Formula: | C22H27ClN7O2S |
| Molecular weight: | 489.013 g/mol |
| DrugBank ID: | DB01254 |
| Buried Surface Area: | 63.39 % |
| Polar Surface area: | 135.94 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 7 |
| H-Bond Donors: | 4 |
| Rings: | 4 |
| Aromatic rings: | 3 |
| Anionic atoms: | 0 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 7 |
| X | Y | Z |
|---|---|---|
| 12.1031 | 2.07682 | 23.1745 |
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 |
| C12 | CD2 | LEU- 408 | 4.32 | 0 | Hydrophobic |
| C15 | CB | LEU- 408 | 4.05 | 0 | Hydrophobic |
| S | CD1 | LEU- 408 | 4.44 | 0 | Hydrophobic |
| C15 | CD2 | PHE- 413 | 4.13 | 0 | Hydrophobic |
| C10 | CG2 | VAL- 416 | 4.32 | 0 | Hydrophobic |
| C15 | CG1 | VAL- 416 | 4.45 | 0 | Hydrophobic |
| S | CG2 | VAL- 416 | 4.11 | 0 | Hydrophobic |
| C10 | CB | ALA- 428 | 3.97 | 0 | Hydrophobic |
| S | CB | ALA- 428 | 4.25 | 0 | Hydrophobic |
| C8 | CD | LYS- 430 | 3.45 | 0 | Hydrophobic |
| C10 | CB | LYS- 430 | 3.47 | 0 | Hydrophobic |
| C7 | CE | MET- 449 | 3.69 | 0 | Hydrophobic |
| CL | CB | VAL- 458 | 3.88 | 0 | Hydrophobic |
| C8 | CG2 | ILE- 472 | 3.78 | 0 | Hydrophobic |
| N2 | OG1 | THR- 474 | 2.91 | 151.34 | H-Bond (Ligand Donor) |
| C5 | CG2 | THR- 474 | 4.14 | 0 | Hydrophobic |
| C9 | CG2 | THR- 474 | 3.62 | 0 | Hydrophobic |
| N | O | MET- 477 | 2.81 | 135.72 | H-Bond (Ligand Donor) |
| N1 | N | MET- 477 | 2.81 | 165.1 | H-Bond (Protein Donor) |
| O1 | OD1 | ASN- 479 | 3.26 | 159.95 | H-Bond (Ligand Donor) |
| S | CD1 | LEU- 528 | 3.86 | 0 | Hydrophobic |
| CL | CD1 | LEU- 528 | 3.85 | 0 | Hydrophobic |
| CL | CB | SER- 538 | 3.68 | 0 | Hydrophobic |
| C6 | CB | PHE- 540 | 3.73 | 0 | Hydrophobic |
