sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.930 Å
X-ray
2013-05-17
| 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: | 78.087 |
|---|---|
| Number of residues: | 34 |
| Including | |
| Standard Amino Acids: | 34 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.403 | 820.125 |
| % Hydrophobic | % Polar |
|---|---|
| 55.56 | 44.44 |
| According to VolSite | |
| HET Code: | 1SU |
|---|---|
| Formula: | C27H18F4N4O3S |
| Molecular weight: | 554.515 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 63.45 % |
| Polar Surface area: | 132.35 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 5 |
| H-Bond Donors: | 2 |
| Rings: | 5 |
| Aromatic rings: | 4 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 2 |
| Rotatable Bonds: | 8 |
| X | Y | Z |
|---|---|---|
| 29.3875 | -15.5766 | 2.19059 |
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 |
| C11 | CG1 | VAL- 470 | 4.09 | 0 | Hydrophobic |
| C7 | CB | ALA- 480 | 4.14 | 0 | Hydrophobic |
| C5 | CB | ALA- 480 | 3.27 | 0 | Hydrophobic |
| F35 | CD | LYS- 482 | 4.08 | 0 | Hydrophobic |
| C8 | CB | LYS- 482 | 3.46 | 0 | Hydrophobic |
| C26 | CG | GLU- 500 | 3.94 | 0 | Hydrophobic |
| N30 | OE2 | GLU- 500 | 2.92 | 158.1 | H-Bond (Ligand Donor) |
| F38 | CG1 | VAL- 503 | 4.01 | 0 | Hydrophobic |
| F35 | CD1 | LEU- 504 | 3.67 | 0 | Hydrophobic |
| C26 | CD2 | LEU- 504 | 4.28 | 0 | Hydrophobic |
| F37 | CD2 | LEU- 504 | 3.38 | 0 | Hydrophobic |
| F37 | CG2 | ILE- 512 | 3.88 | 0 | Hydrophobic |
| C5 | CD1 | LEU- 513 | 4 | 0 | Hydrophobic |
| C6 | CD2 | LEU- 513 | 3.82 | 0 | Hydrophobic |
| C10 | CD2 | LEU- 513 | 4.02 | 0 | Hydrophobic |
| C8 | CB | ILE- 526 | 4.49 | 0 | Hydrophobic |
| F35 | CG2 | ILE- 526 | 3.32 | 0 | Hydrophobic |
| C8 | CG2 | THR- 528 | 3.57 | 0 | Hydrophobic |
| S39 | CZ3 | TRP- 530 | 4.11 | 0 | Hydrophobic |
| C23 | CZ2 | TRP- 530 | 3.62 | 0 | Hydrophobic |
| C5 | SG | CYS- 531 | 4.23 | 0 | Hydrophobic |
| N29 | N | CYS- 531 | 3.13 | 166.68 | H-Bond (Protein Donor) |
| N31 | O | CYS- 531 | 3.16 | 162.21 | H-Bond (Ligand Donor) |
| F36 | CD1 | LEU- 566 | 4.06 | 0 | Hydrophobic |
| F38 | CD2 | LEU- 566 | 3.67 | 0 | Hydrophobic |
| F38 | CG2 | ILE- 571 | 4.2 | 0 | Hydrophobic |
| S39 | CE1 | PHE- 582 | 4.3 | 0 | Hydrophobic |
| C25 | CZ | PHE- 582 | 3.8 | 0 | Hydrophobic |
| F36 | CG2 | ILE- 591 | 3.82 | 0 | Hydrophobic |
| O33 | N | ASP- 593 | 2.82 | 162.67 | H-Bond (Protein Donor) |
| C12 | CB | ASP- 593 | 3.95 | 0 | Hydrophobic |
| C3 | CB | ASP- 593 | 3.59 | 0 | Hydrophobic |
