sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.600 Å
X-ray
1995-10-18
| Name: | Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic |
|---|---|
| ID: | FABI_BRANA |
| AC: | P80030 |
| Organism: | Brassica napus |
| Reign: | Eukaryota |
| TaxID: | 3708 |
| EC Number: | 1.3.1.9 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 24.072 |
|---|---|
| Number of residues: | 49 |
| Including | |
| Standard Amino Acids: | 44 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 5 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.833 | 469.125 |
| % Hydrophobic | % Polar |
|---|---|
| 49.64 | 50.36 |
| According to VolSite | |
| HET Code: | NAD |
|---|---|
| Formula: | C21H26N7O14P2 |
| Molecular weight: | 662.417 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 60.8 % |
| Polar Surface area: | 343.54 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 18 |
| H-Bond Donors: | 6 |
| Rings: | 5 |
| Aromatic rings: | 3 |
| Anionic atoms: | 2 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 3 |
| Rotatable Bonds: | 11 |
| X | Y | Z |
|---|---|---|
| 3.84245 | 16.5991 | 39.6402 |
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 |
| C3B | CB | ALA- 27 | 4.48 | 0 | Hydrophobic |
| O2N | N | TYR- 32 | 2.94 | 164.01 | H-Bond (Protein Donor) |
| C3N | CE2 | TYR- 32 | 3.17 | 0 | Hydrophobic |
| C2B | CE3 | TRP- 52 | 4.13 | 0 | Hydrophobic |
| C1B | CB | TRP- 52 | 4.28 | 0 | Hydrophobic |
| N6A | OD1 | ASP- 89 | 2.76 | 145.64 | H-Bond (Ligand Donor) |
| N1A | N | ALA- 90 | 2.88 | 167.7 | H-Bond (Protein Donor) |
| C5D | CB | SER- 136 | 4.45 | 0 | Hydrophobic |
| C1B | CG | LEU- 137 | 4.37 | 0 | Hydrophobic |
| O3D | O | LEU- 137 | 3.29 | 154.06 | H-Bond (Ligand Donor) |
| C3D | CB | ALA- 138 | 3.68 | 0 | Hydrophobic |
| C4D | CB | LEU- 186 | 3.76 | 0 | Hydrophobic |
| C5N | CB | TYR- 188 | 3.73 | 0 | Hydrophobic |
| C5N | CB | ALA- 233 | 4.04 | 0 | Hydrophobic |
| O7N | N | LEU- 236 | 2.92 | 170.87 | H-Bond (Protein Donor) |
| O2A | O | HOH- 506 | 2.6 | 164.86 | H-Bond (Protein Donor) |
| O3D | O | HOH- 518 | 3.34 | 137.9 | H-Bond (Ligand Donor) |
