sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.860 Å
X-ray
2014-07-10
| Name: | Enoyl-[acyl-carrier-protein] reductase [NADH] |
|---|---|
| ID: | INHA_MYCTU |
| AC: | P9WGR1 |
| Organism: | Mycobacterium tuberculosis |
| Reign: | Bacteria |
| TaxID: | 83332 |
| EC Number: | 1.3.1.9 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 23.812 |
|---|---|
| Number of residues: | 29 |
| Including | |
| Standard Amino Acids: | 27 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 1 |
| Cofactors: | NAD |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.658 | 583.875 |
| % Hydrophobic | % Polar |
|---|---|
| 64.74 | 35.26 |
| According to VolSite | |
| HET Code: | 468 |
|---|---|
| Formula: | C18H23ClN2O2 |
| Molecular weight: | 334.840 g/mol |
| DrugBank ID: | DB07090 |
| Buried Surface Area: | 67.92 % |
| 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 |
|---|---|---|
| 39.2189 | 51.9218 | 60.9397 |
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 |
| C20 | CE | MET- 103 | 3.66 | 0 | Hydrophobic |
| C8 | CG | PHE- 149 | 4.45 | 0 | Hydrophobic |
| C23 | CE1 | PHE- 149 | 3.36 | 0 | Hydrophobic |
| C23 | SD | MET- 155 | 4.43 | 0 | Hydrophobic |
| CL1 | SD | MET- 155 | 3.85 | 0 | Hydrophobic |
| C18 | CB | ALA- 157 | 3.53 | 0 | Hydrophobic |
| O15 | OH | TYR- 158 | 2.7 | 176.69 | H-Bond (Protein Donor) |
| C23 | CD1 | TYR- 158 | 4.26 | 0 | Hydrophobic |
| CL1 | CB | TYR- 158 | 4.24 | 0 | Hydrophobic |
| C8 | CE1 | TYR- 158 | 3.71 | 0 | Hydrophobic |
| C17 | CB | TYR- 158 | 3.98 | 0 | Hydrophobic |
| C4 | CG | MET- 161 | 4.46 | 0 | Hydrophobic |
| C5 | SD | MET- 161 | 4.43 | 0 | Hydrophobic |
| C9 | SD | MET- 199 | 3.48 | 0 | Hydrophobic |
| C20 | CE | MET- 199 | 3.77 | 0 | Hydrophobic |
| C16 | CE | MET- 199 | 4.45 | 0 | Hydrophobic |
| C20 | CD1 | ILE- 202 | 4.37 | 0 | Hydrophobic |
| CL1 | CG1 | ILE- 215 | 4 | 0 | Hydrophobic |
| C19 | CD1 | ILE- 215 | 3.31 | 0 | Hydrophobic |
| C18 | CG1 | ILE- 215 | 3.25 | 0 | Hydrophobic |
| C23 | CD2 | LEU- 218 | 4.19 | 0 | Hydrophobic |
| CL1 | CD1 | LEU- 218 | 3.93 | 0 | Hydrophobic |
| C1 | C5B | NAD- 500 | 3.98 | 0 | Hydrophobic |
| C2 | C2D | NAD- 500 | 4.02 | 0 | Hydrophobic |
| C8 | C3N | NAD- 500 | 3.49 | 0 | Hydrophobic |
| O15 | O2D | NAD- 500 | 2.7 | 149.45 | H-Bond (Protein Donor) |
