sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.250 Å
X-ray
2002-01-25
| Name: | Enoyl-[acyl-carrier-protein] reductase 1, mitochondrial |
|---|---|
| ID: | ETR1_CANTR |
| AC: | Q8WZM3 |
| Organism: | Candida tropicalis |
| Reign: | Eukaryota |
| TaxID: | 5482 |
| EC Number: | 1.3.1.10 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 98 % |
| B | 2 % |
| B-Factor: | 18.035 |
|---|---|
| Number of residues: | 44 |
| Including | |
| Standard Amino Acids: | 42 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 2 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.253 | 1390.500 |
| % Hydrophobic | % Polar |
|---|---|
| 50.24 | 49.76 |
| According to VolSite | |
| HET Code: | NDP |
|---|---|
| Formula: | C21H26N7O17P3 |
| Molecular weight: | 741.389 g/mol |
| DrugBank ID: | DB02338 |
| Buried Surface Area: | 56.9 % |
| Polar Surface area: | 404.9 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 22 |
| H-Bond Donors: | 5 |
| Rings: | 5 |
| Aromatic rings: | 2 |
| Anionic atoms: | 4 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 2 |
| Rotatable Bonds: | 13 |
| X | Y | Z |
|---|---|---|
| 67.0136 | -21.1213 | 54.6444 |
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 |
| C3D | CG | PRO- 69 | 3.24 | 0 | Hydrophobic |
| C5N | CG1 | VAL- 171 | 3.7 | 0 | Hydrophobic |
| C4N | CG2 | THR- 175 | 3.99 | 0 | Hydrophobic |
| O3B | OG1 | THR- 199 | 2.63 | 145.12 | H-Bond (Ligand Donor) |
| C3B | CB | SER- 200 | 4.24 | 0 | Hydrophobic |
| C4B | CB | SER- 200 | 3.69 | 0 | Hydrophobic |
| O1A | N | ALA- 201 | 3.16 | 163.6 | H-Bond (Protein Donor) |
| O1N | N | VAL- 202 | 2.86 | 167.66 | H-Bond (Protein Donor) |
| C5N | CG2 | VAL- 202 | 3.85 | 0 | Hydrophobic |
| O2B | NH2 | ARG- 222 | 3.3 | 140.36 | H-Bond (Protein Donor) |
| O1X | NE | ARG- 222 | 3.22 | 151.96 | H-Bond (Protein Donor) |
| O1X | NH2 | ARG- 222 | 3.35 | 143.61 | H-Bond (Protein Donor) |
| O3X | NH2 | ARG- 222 | 3.35 | 150.51 | H-Bond (Protein Donor) |
| O1X | CZ | ARG- 222 | 3.72 | 0 | Ionic (Protein Cationic) |
| DuAr | CZ | ARG- 222 | 3.57 | 163.74 | Pi/Cation |
| O1X | CZ | ARG- 224 | 3.75 | 0 | Ionic (Protein Cationic) |
| O1X | NH1 | ARG- 224 | 3.25 | 138.75 | H-Bond (Protein Donor) |
| O1X | NH2 | ARG- 224 | 3.42 | 133.51 | H-Bond (Protein Donor) |
| O2X | NH2 | ARG- 224 | 3.24 | 167.08 | H-Bond (Protein Donor) |
| N7N | O | TYR- 296 | 3.07 | 153.95 | H-Bond (Ligand Donor) |
| C1B | CG | MET- 299 | 4.29 | 0 | Hydrophobic |
| C5B | CE | MET- 299 | 3.66 | 0 | Hydrophobic |
| C3D | SD | MET- 299 | 3.42 | 0 | Hydrophobic |
| N7N | O | PHE- 321 | 2.92 | 134.07 | H-Bond (Ligand Donor) |
| O7N | N | VAL- 323 | 2.86 | 174.55 | H-Bond (Protein Donor) |
| C4N | CG1 | VAL- 323 | 4.47 | 0 | Hydrophobic |
| O2N | NZ | LYS- 381 | 3.04 | 169.29 | H-Bond (Protein Donor) |
| O2N | NZ | LYS- 381 | 3.04 | 0 | Ionic (Protein Cationic) |
