sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
3.000 Å
X-ray
2003-10-15
| Name: | Thyroid hormone receptor beta |
|---|---|
| ID: | THB_HUMAN |
| AC: | P10828 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 73.941 |
|---|---|
| Number of residues: | 46 |
| Including | |
| Standard Amino Acids: | 46 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.835 | 492.750 |
| % Hydrophobic | % Polar |
|---|---|
| 73.29 | 26.71 |
| According to VolSite | |
| HET Code: | 442 |
|---|---|
| Formula: | C23H24Br2NO5 |
| Molecular weight: | 554.248 g/mol |
| DrugBank ID: | DB02106 |
| Buried Surface Area: | 79.71 % |
| Polar Surface area: | 106.76 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 5 |
| H-Bond Donors: | 5 |
| Rings: | 3 |
| Aromatic rings: | 3 |
| Anionic atoms: | 0 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 9 |
| X | Y | Z |
|---|---|---|
| 51.0268 | 6.22432 | 13.1165 |
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 |
| C30 | CE1 | PHE- 269 | 4.16 | 0 | Hydrophobic |
| C12 | CB | PHE- 272 | 4.25 | 0 | Hydrophobic |
| BR1 | CG1 | ILE- 275 | 3.96 | 0 | Hydrophobic |
| BR1 | CG1 | ILE- 276 | 3.9 | 0 | Hydrophobic |
| C15 | CD1 | ILE- 276 | 3.47 | 0 | Hydrophobic |
| C6 | CB | ALA- 279 | 3.44 | 0 | Hydrophobic |
| O3 | NH1 | ARG- 282 | 3.2 | 142.57 | H-Bond (Protein Donor) |
| O3 | NH2 | ARG- 282 | 2.98 | 156.62 | H-Bond (Protein Donor) |
| O3 | CZ | ARG- 282 | 3.55 | 0 | Ionic (Protein Cationic) |
| BR2 | CE | MET- 310 | 4.26 | 0 | Hydrophobic |
| C15 | CE | MET- 310 | 4.03 | 0 | Hydrophobic |
| C7 | CG | MET- 313 | 3.63 | 0 | Hydrophobic |
| C6 | SD | MET- 313 | 4.19 | 0 | Hydrophobic |
| C4 | CB | MET- 313 | 3.62 | 0 | Hydrophobic |
| C16 | CE | MET- 313 | 4.31 | 0 | Hydrophobic |
| BR2 | CB | ALA- 317 | 4.16 | 0 | Hydrophobic |
| C4 | CB | ALA- 317 | 4.14 | 0 | Hydrophobic |
| O3 | NH2 | ARG- 320 | 3.17 | 122.42 | H-Bond (Protein Donor) |
| O2 | NH2 | ARG- 320 | 3.11 | 121.94 | H-Bond (Protein Donor) |
| BR1 | CD1 | LEU- 330 | 4.45 | 0 | Hydrophobic |
| C3 | CD2 | LEU- 330 | 3.86 | 0 | Hydrophobic |
| C2 | CD2 | LEU- 330 | 3.75 | 0 | Hydrophobic |
| O2 | N | ASN- 331 | 3.2 | 168.25 | H-Bond (Protein Donor) |
| C12 | CD1 | LEU- 341 | 4.07 | 0 | Hydrophobic |
| C12 | CD1 | LEU- 346 | 3.61 | 0 | Hydrophobic |
| C14 | CD2 | LEU- 346 | 3.82 | 0 | Hydrophobic |
| BR2 | CD1 | ILE- 353 | 3.73 | 0 | Hydrophobic |
| O | NE2 | HIS- 435 | 3.43 | 148.09 | H-Bond (Ligand Donor) |
| C35 | CG | ARG- 438 | 3.63 | 0 | Hydrophobic |
| C34 | CB | ARG- 438 | 3.94 | 0 | Hydrophobic |
| C34 | CB | PHE- 439 | 3.72 | 0 | Hydrophobic |
| C36 | CG | MET- 442 | 3.43 | 0 | Hydrophobic |
| C30 | CE2 | PHE- 451 | 4.3 | 0 | Hydrophobic |
