sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.500 Å
X-ray
2016-01-11
| 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 |
|---|---|
| B | 100 % |
| B-Factor: | 31.312 |
|---|---|
| Number of residues: | 35 |
| Including | |
| Standard Amino Acids: | 35 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.017 | 567.000 |
| % Hydrophobic | % Polar |
|---|---|
| 50.60 | 49.40 |
| According to VolSite | |
| HET Code: | B1E |
|---|---|
| Formula: | C27H25N5O2 |
| Molecular weight: | 451.520 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 66.2 % |
| Polar Surface area: | 97.59 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 5 |
| H-Bond Donors: | 2 |
| Rings: | 4 |
| Aromatic rings: | 3 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 5 |
| X | Y | Z |
|---|---|---|
| -0.564235 | 12.4858 | -15.2136 |
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 |
| C33 | CG2 | ILE- 463 | 4.29 | 0 | Hydrophobic |
| C19 | CG1 | VAL- 471 | 3.95 | 0 | Hydrophobic |
| C6 | CG1 | VAL- 471 | 3.86 | 0 | Hydrophobic |
| C1 | CB | ALA- 481 | 4.31 | 0 | Hydrophobic |
| C19 | CB | ALA- 481 | 3.81 | 0 | Hydrophobic |
| C3 | CB | ALA- 481 | 3.35 | 0 | Hydrophobic |
| C16 | CD | LYS- 483 | 4.23 | 0 | Hydrophobic |
| C13 | CD | LYS- 483 | 4.27 | 0 | Hydrophobic |
| C19 | CB | LYS- 483 | 3.6 | 0 | Hydrophobic |
| N20 | OE2 | GLU- 501 | 2.76 | 152.55 | H-Bond (Ligand Donor) |
| C28 | CG | GLU- 501 | 3.61 | 0 | Hydrophobic |
| C26 | CG1 | VAL- 504 | 4.4 | 0 | Hydrophobic |
| C32 | CG1 | VAL- 504 | 3.88 | 0 | Hydrophobic |
| C16 | CD1 | LEU- 505 | 3.99 | 0 | Hydrophobic |
| C32 | CD2 | LEU- 505 | 4.06 | 0 | Hydrophobic |
| C24 | CD2 | LEU- 505 | 3.76 | 0 | Hydrophobic |
| C3 | CD1 | LEU- 514 | 3.87 | 0 | Hydrophobic |
| C4 | CD2 | LEU- 514 | 3.86 | 0 | Hydrophobic |
| C18 | CD2 | LEU- 514 | 3.72 | 0 | Hydrophobic |
| C16 | CG2 | ILE- 527 | 3.74 | 0 | Hydrophobic |
| C14 | CG2 | THR- 529 | 3.9 | 0 | Hydrophobic |
| C15 | CG2 | THR- 529 | 3.39 | 0 | Hydrophobic |
| C33 | CH2 | TRP- 531 | 3.91 | 0 | Hydrophobic |
| N10 | N | CYS- 532 | 3.1 | 160.35 | H-Bond (Protein Donor) |
| C32 | CD2 | LEU- 567 | 4.4 | 0 | Hydrophobic |
| C31 | CG2 | ILE- 572 | 4.09 | 0 | Hydrophobic |
| C33 | CE2 | PHE- 583 | 3.84 | 0 | Hydrophobic |
| O23 | N | ASP- 594 | 2.97 | 166.58 | H-Bond (Protein Donor) |
| C22 | CB | ASP- 594 | 3.75 | 0 | Hydrophobic |
