sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.400 Å
X-ray
1997-04-28
| Name: | Enoyl-CoA hydratase, mitochondrial |
|---|---|
| ID: | ECHM_RAT |
| AC: | P14604 |
| Organism: | Rattus norvegicus |
| Reign: | Eukaryota |
| TaxID: | 10116 |
| EC Number: | 4.2.1.17 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| B | 86 % |
| C | 14 % |
| B-Factor: | 34.850 |
|---|---|
| Number of residues: | 43 |
| Including | |
| Standard Amino Acids: | 43 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.451 | 1039.500 |
| % Hydrophobic | % Polar |
|---|---|
| 59.74 | 40.26 |
| According to VolSite | |
| HET Code: | CO8 |
|---|---|
| Formula: | C29H46N7O17P3S |
| Molecular weight: | 889.699 g/mol |
| DrugBank ID: | DB02910 |
| Buried Surface Area: | 51.45 % |
| Polar Surface area: | 429.68 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 22 |
| H-Bond Donors: | 5 |
| Rings: | 3 |
| Aromatic rings: | 2 |
| Anionic atoms: | 4 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 2 |
| Rotatable Bonds: | 26 |
| X | Y | Z |
|---|---|---|
| 94.013 | 122.505 | 148.252 |
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 |
| C1B | CB | ALA- 57 | 4.15 | 0 | Hydrophobic |
| C5B | CG | LEU- 58 | 4.05 | 0 | Hydrophobic |
| CCP | CD1 | LEU- 58 | 3.54 | 0 | Hydrophobic |
| O4A | NZ | LYS- 92 | 3.16 | 156.38 | H-Bond (Protein Donor) |
| O4A | NZ | LYS- 92 | 3.16 | 0 | Ionic (Protein Cationic) |
| CEP | CB | ALA- 96 | 3.66 | 0 | Hydrophobic |
| N4P | O | ALA- 96 | 3.27 | 150.24 | H-Bond (Ligand Donor) |
| O1' | N | ALA- 98 | 3.49 | 154 | H-Bond (Protein Donor) |
| S1P | CB | ALA- 98 | 4.11 | 0 | Hydrophobic |
| N1A | N | ILE- 100 | 2.95 | 155.64 | H-Bond (Protein Donor) |
| S1P | CD1 | ILE- 100 | 3.75 | 0 | Hydrophobic |
| O2B | NZ | LYS- 101 | 2.88 | 150.04 | H-Bond (Protein Donor) |
| O7A | NZ | LYS- 101 | 3.87 | 0 | Ionic (Protein Cationic) |
| S1P | CE | MET- 103 | 3.82 | 0 | Hydrophobic |
| C8' | CB | TRP- 120 | 4.18 | 0 | Hydrophobic |
| CCP | CE2 | TYR- 137 | 3.98 | 0 | Hydrophobic |
| CDP | CZ | TYR- 137 | 4.38 | 0 | Hydrophobic |
| CEP | CD2 | TYR- 137 | 3.91 | 0 | Hydrophobic |
| CDP | CD1 | LEU- 139 | 4.41 | 0 | Hydrophobic |
| CEP | CD1 | LEU- 139 | 3.49 | 0 | Hydrophobic |
| O1' | N | GLY- 141 | 2.61 | 124.02 | H-Bond (Protein Donor) |
| C6P | CG | PRO- 163 | 4.23 | 0 | Hydrophobic |
| S1P | CG | GLU- 164 | 3.8 | 0 | Hydrophobic |
| C2' | CG | GLU- 164 | 3.38 | 0 | Hydrophobic |
| S1P | CD1 | LEU- 167 | 4.09 | 0 | Hydrophobic |
| C6' | CB | ALA- 173 | 4.45 | 0 | Hydrophobic |
| C4' | CB | ALA- 173 | 3.81 | 0 | Hydrophobic |
| C8' | CD | LYS- 260 | 4.25 | 0 | Hydrophobic |
| C2' | CE1 | PHE- 263 | 4.46 | 0 | Hydrophobic |
| C5' | CZ | PHE- 263 | 3.89 | 0 | Hydrophobic |
| C7' | CE2 | PHE- 263 | 4.21 | 0 | Hydrophobic |
| O2B | NZ | LYS- 282 | 3.48 | 165.57 | H-Bond (Protein Donor) |
