sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.730 Å
X-ray
2014-06-17
| Name: | Enoyl-[acyl-carrier-protein] reductase [NADH] |
|---|---|
| ID: | INHA_MYCTO |
| AC: | P9WGR0 |
| Organism: | Mycobacterium tuberculosis |
| Reign: | Bacteria |
| TaxID: | 83331 |
| EC Number: | 1.3.1.9 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 23.260 |
|---|---|
| Number of residues: | 31 |
| Including | |
| Standard Amino Acids: | 28 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 2 |
| Cofactors: | NAD |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.377 | 874.125 |
| % Hydrophobic | % Polar |
|---|---|
| 57.92 | 42.08 |
| According to VolSite | |
| HET Code: | 665 |
|---|---|
| Formula: | C17H21BrN2O2 |
| Molecular weight: | 365.265 g/mol |
| DrugBank ID: | DB07192 |
| Buried Surface Area: | 72.11 % |
| Polar Surface area: | 49.41 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 2 |
| H-Bond Donors: | 1 |
| Rings: | 3 |
| Aromatic rings: | 1 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 3 |
| X | Y | Z |
|---|---|---|
| 9.43423 | 32.4579 | 60.6191 |
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 |
| C1 | SD | MET- 103 | 4.47 | 0 | Hydrophobic |
| C2 | CE | MET- 103 | 4.16 | 0 | Hydrophobic |
| C17 | CE | MET- 103 | 3.73 | 0 | Hydrophobic |
| BR1 | CE | MET- 103 | 3.88 | 0 | Hydrophobic |
| C8 | CG | PHE- 149 | 4.43 | 0 | Hydrophobic |
| C20 | SD | MET- 155 | 4.22 | 0 | Hydrophobic |
| C19 | CB | ALA- 157 | 3.86 | 0 | Hydrophobic |
| BR1 | CB | ALA- 157 | 3.6 | 0 | Hydrophobic |
| O15 | OH | TYR- 158 | 2.64 | 174.59 | H-Bond (Protein Donor) |
| C8 | CE1 | TYR- 158 | 3.74 | 0 | Hydrophobic |
| C20 | CB | TYR- 158 | 3.79 | 0 | Hydrophobic |
| C1 | SD | MET- 161 | 4.43 | 0 | Hydrophobic |
| C2 | CE | MET- 161 | 4.48 | 0 | Hydrophobic |
| C9 | SD | MET- 199 | 3.44 | 0 | Hydrophobic |
| C17 | CE | MET- 199 | 4.19 | 0 | Hydrophobic |
| BR1 | CG2 | ILE- 202 | 4.34 | 0 | Hydrophobic |
| BR1 | CD1 | LEU- 207 | 4.28 | 0 | Hydrophobic |
| C17 | CD1 | ILE- 215 | 3.62 | 0 | Hydrophobic |
| C18 | CD1 | ILE- 215 | 3.55 | 0 | Hydrophobic |
| C19 | CG1 | ILE- 215 | 3.74 | 0 | Hydrophobic |
| C21 | CD2 | LEU- 218 | 3.85 | 0 | Hydrophobic |
| C4 | C2D | NAD- 500 | 4.07 | 0 | Hydrophobic |
| C5 | C5B | NAD- 500 | 3.98 | 0 | Hydrophobic |
| C8 | C3N | NAD- 500 | 3.44 | 0 | Hydrophobic |
| O15 | O2D | NAD- 500 | 2.7 | 146.52 | H-Bond (Protein Donor) |
