sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.650 Å
X-ray
2012-06-12
| Name: | Serine/threonine-protein kinase B-raf |
|---|---|
| ID: | BRAF_HUMAN |
| AC: | P15056 |
| 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: | 32.932 |
|---|---|
| Number of residues: | 33 |
| Including | |
| Standard Amino Acids: | 33 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.051 | 715.500 |
| % Hydrophobic | % Polar |
|---|---|
| 56.60 | 43.40 |
| According to VolSite | |
| HET Code: | 325 |
|---|---|
| Formula: | C21H16F2N4O3S |
| Molecular weight: | 442.439 g/mol |
| DrugBank ID: | DB07000 |
| Buried Surface Area: | 62.79 % |
| Polar Surface area: | 113.19 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 5 |
| H-Bond Donors: | 2 |
| Rings: | 4 |
| Aromatic rings: | 4 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| -1.98535 | 50.2041 | 20.1495 |
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 |
| C6 | CG2 | ILE- 463 | 4.12 | 0 | Hydrophobic |
| F29 | CG1 | VAL- 471 | 3.43 | 0 | Hydrophobic |
| C11 | CG1 | VAL- 471 | 4.43 | 0 | Hydrophobic |
| C11 | CB | ALA- 481 | 4.42 | 0 | Hydrophobic |
| F29 | CB | ALA- 481 | 3.55 | 0 | Hydrophobic |
| C19 | CB | LYS- 483 | 3.41 | 0 | Hydrophobic |
| C26 | CD1 | LEU- 505 | 3.78 | 0 | Hydrophobic |
| C31 | CD2 | LEU- 505 | 3.76 | 0 | Hydrophobic |
| C31 | CD2 | LEU- 514 | 4.26 | 0 | Hydrophobic |
| C22 | CD2 | LEU- 514 | 3.49 | 0 | Hydrophobic |
| C26 | CG2 | ILE- 527 | 4.36 | 0 | Hydrophobic |
| C20 | CG2 | ILE- 527 | 3.9 | 0 | Hydrophobic |
| C26 | CG2 | THR- 529 | 3.97 | 0 | Hydrophobic |
| C20 | CG2 | THR- 529 | 3.78 | 0 | Hydrophobic |
| N15 | O | GLN- 530 | 3.18 | 157.1 | H-Bond (Ligand Donor) |
| N9 | N | CYS- 532 | 3.1 | 146.66 | H-Bond (Protein Donor) |
| F28 | CE1 | PHE- 583 | 3.54 | 0 | Hydrophobic |
| C31 | CE2 | PHE- 595 | 3.78 | 0 | Hydrophobic |
| O27 | N | PHE- 595 | 2.99 | 155.28 | H-Bond (Protein Donor) |
| O27 | N | GLY- 596 | 3.26 | 124.69 | H-Bond (Protein Donor) |
