sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.840 Å
X-ray
2010-07-14
| Min | Mean | Median | Standard Deviation | Max | Count | |
|---|---|---|---|---|---|---|
| pChEMBL: | 9.000 | 9.390 | 9.250 | 0.330 | 9.890 | 6 |
| Name: | Beta-2 adrenergic receptor |
|---|---|
| ID: | ADRB2_HUMAN |
| AC: | P07550 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 0.000 |
|---|---|
| Number of residues: | 28 |
| Including | |
| Standard Amino Acids: | 28 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.168 | 1188.000 |
| % Hydrophobic | % Polar |
|---|---|
| 55.68 | 44.32 |
| According to VolSite | |
| HET Code: | JRZ |
|---|---|
| Formula: | C17H28NO2 |
| Molecular weight: | 278.410 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 63 % |
| Polar Surface area: | 46.07 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| H-Bond Donors: | 2 |
| Rings: | 2 |
| Aromatic rings: | 1 |
| Anionic atoms: | 0 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| 2.2488 | 4.68495 | 51.3982 |
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 |
| C17 | CZ3 | TRP- 109 | 4.26 | 0 | Hydrophobic |
| N1 | OD2 | ASP- 113 | 3.83 | 0 | Ionic (Ligand Cationic) |
| O2 | OD1 | ASP- 113 | 2.65 | 167.94 | H-Bond (Ligand Donor) |
| C14 | CB | ASP- 113 | 3.87 | 0 | Hydrophobic |
| C14 | CG2 | VAL- 114 | 4.49 | 0 | Hydrophobic |
| C8 | CG1 | VAL- 114 | 3.44 | 0 | Hydrophobic |
| C11 | CG2 | VAL- 117 | 4.41 | 0 | Hydrophobic |
| C9 | CB | VAL- 117 | 3.85 | 0 | Hydrophobic |
| C17 | CB | PHE- 193 | 3.68 | 0 | Hydrophobic |
| C2 | CE2 | PHE- 193 | 3.91 | 0 | Hydrophobic |
| C1 | CB | SER- 203 | 4.24 | 0 | Hydrophobic |
| C7 | CB | SER- 203 | 4.28 | 0 | Hydrophobic |
| C7 | CB | SER- 207 | 3.2 | 0 | Hydrophobic |
| C11 | CZ3 | TRP- 286 | 3.98 | 0 | Hydrophobic |
| C3 | CE1 | PHE- 289 | 4.2 | 0 | Hydrophobic |
| C11 | CE1 | PHE- 289 | 4.29 | 0 | Hydrophobic |
| C12 | CZ | PHE- 289 | 3.91 | 0 | Hydrophobic |
| C1 | CE1 | PHE- 290 | 4.3 | 0 | Hydrophobic |
| C3 | CE1 | PHE- 290 | 4.45 | 0 | Hydrophobic |
| C16 | CE2 | TYR- 308 | 4.15 | 0 | Hydrophobic |
| N1 | OD1 | ASN- 312 | 2.78 | 161.5 | H-Bond (Ligand Donor) |
| O2 | ND2 | ASN- 312 | 3.08 | 155.11 | H-Bond (Protein Donor) |
