sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.310 Å
X-ray
2011-06-13
| Name: | HTH-type transcriptional regulator EthR |
|---|---|
| ID: | ETHR_MYCTU |
| AC: | P9WMC1 |
| Organism: | Mycobacterium tuberculosis |
| Reign: | Bacteria |
| TaxID: | 83332 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 22.949 |
|---|---|
| Number of residues: | 35 |
| Including | |
| Standard Amino Acids: | 35 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.417 | 577.125 |
| % Hydrophobic | % Polar |
|---|---|
| 61.40 | 38.60 |
| According to VolSite | |
| HET Code: | 3SF |
|---|---|
| Formula: | C15H17F3N4O2S |
| Molecular weight: | 374.381 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 76.53 % |
| Polar Surface area: | 100.36 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 4 |
| H-Bond Donors: | 0 |
| Rings: | 3 |
| Aromatic rings: | 2 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| 28.0528 | -10.12 | -5.39028 |
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 | CD2 | LEU- 87 | 4.3 | 0 | Hydrophobic |
| S | CG | MET- 102 | 4.49 | 0 | Hydrophobic |
| C7 | CZ3 | TRP- 103 | 4.33 | 0 | Hydrophobic |
| C8 | CG1 | ILE- 107 | 4.06 | 0 | Hydrophobic |
| F | CB | PHE- 110 | 3.49 | 0 | Hydrophobic |
| C2 | CG | PHE- 110 | 3.67 | 0 | Hydrophobic |
| C3 | CD2 | PHE- 110 | 3.68 | 0 | Hydrophobic |
| C6 | CE2 | PHE- 110 | 4.29 | 0 | Hydrophobic |
| C1 | CD1 | PHE- 110 | 3.63 | 0 | Hydrophobic |
| F | CE2 | PHE- 114 | 3.29 | 0 | Hydrophobic |
| F1 | CZ2 | TRP- 138 | 3.22 | 0 | Hydrophobic |
| C1 | SD | MET- 142 | 4.15 | 0 | Hydrophobic |
| F1 | SD | MET- 142 | 3.94 | 0 | Hydrophobic |
| C1 | CE3 | TRP- 145 | 3.68 | 0 | Hydrophobic |
| F1 | CZ3 | TRP- 145 | 4.17 | 0 | Hydrophobic |
| C3 | CE3 | TRP- 145 | 4.2 | 0 | Hydrophobic |
| C7 | CB | THR- 149 | 4.49 | 0 | Hydrophobic |
| O | ND2 | ASN- 179 | 2.89 | 160.98 | H-Bond (Protein Donor) |
| C2 | CB | ASN- 179 | 4.1 | 0 | Hydrophobic |
| F2 | CB | ASN- 179 | 3.71 | 0 | Hydrophobic |
| F1 | CG | GLU- 180 | 4.18 | 0 | Hydrophobic |
| F2 | CB | GLU- 180 | 3.68 | 0 | Hydrophobic |
| F | CD1 | LEU- 183 | 3.74 | 0 | Hydrophobic |
| F1 | CZ | PHE- 184 | 3.61 | 0 | Hydrophobic |
| C7 | CH2 | TRP- 207 | 3.79 | 0 | Hydrophobic |
