sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.100 Å
X-ray
2002-08-26
| 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 |
|---|---|
| A | 83 % |
| B | 17 % |
| B-Factor: | 27.333 |
|---|---|
| Number of residues: | 45 |
| Including | |
| Standard Amino Acids: | 42 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 3 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.306 | 614.250 |
| % Hydrophobic | % Polar |
|---|---|
| 67.58 | 32.42 |
| According to VolSite | |
| HET Code: | HXC |
|---|---|
| Formula: | C27H42N7O17P3S |
| Molecular weight: | 861.645 g/mol |
| DrugBank ID: | DB02563 |
| Buried Surface Area: | 56.42 % |
| 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: | 24 |
| X | Y | Z |
|---|---|---|
| 58.5464 | 111.444 | 183.988 |
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 |
| C5' | CG | LEU- 58 | 3.97 | 0 | Hydrophobic |
| CPB | CD1 | LEU- 58 | 3.71 | 0 | Hydrophobic |
| O22 | NZ | LYS- 92 | 3.83 | 0 | Ionic (Protein Cationic) |
| CP8 | CB | ALA- 96 | 4.34 | 0 | Hydrophobic |
| NP1 | O | ALA- 96 | 3.05 | 130.72 | H-Bond (Ligand Donor) |
| N6 | O | ALA- 98 | 3.1 | 155.2 | H-Bond (Ligand Donor) |
| OM2 | N | ALA- 98 | 2.8 | 152.62 | H-Bond (Protein Donor) |
| N1 | N | ILE- 100 | 3.02 | 164.37 | H-Bond (Protein Donor) |
| O31 | NZ | LYS- 101 | 3.83 | 0 | Ionic (Protein Cationic) |
| O33 | NZ | LYS- 101 | 3 | 0 | Ionic (Protein Cationic) |
| O33 | NZ | LYS- 101 | 3 | 141.65 | H-Bond (Protein Donor) |
| S | CE | MET- 103 | 3.98 | 0 | Hydrophobic |
| CPB | CE2 | TYR- 137 | 3.82 | 0 | Hydrophobic |
| CP8 | CD2 | TYR- 137 | 3.93 | 0 | Hydrophobic |
| CP9 | CZ | TYR- 137 | 4.43 | 0 | Hydrophobic |
| CP8 | CD1 | LEU- 139 | 3.54 | 0 | Hydrophobic |
| CP4 | CD1 | LEU- 139 | 4.25 | 0 | Hydrophobic |
| OM2 | N | GLY- 141 | 2.78 | 167.41 | H-Bond (Protein Donor) |
| CP4 | CG | PRO- 163 | 3.99 | 0 | Hydrophobic |
| S | CG | GLU- 164 | 3.86 | 0 | Hydrophobic |
| S | CD1 | LEU- 167 | 3.57 | 0 | Hydrophobic |
| C2' | CZ | PHE- 279 | 4.23 | 0 | Hydrophobic |
| O32 | NZ | LYS- 282 | 3 | 152.74 | H-Bond (Protein Donor) |
| O33 | NZ | LYS- 282 | 2.76 | 130.3 | H-Bond (Protein Donor) |
| O32 | NZ | LYS- 282 | 3 | 0 | Ionic (Protein Cationic) |
| O33 | NZ | LYS- 282 | 2.76 | 0 | Ionic (Protein Cationic) |
| O2' | O | HOH- 1098 | 3.14 | 135.77 | H-Bond (Protein Donor) |
