sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.180 Å
X-ray
2003-07-23
| Name: | Chloramphenicol acetyltransferase |
|---|---|
| ID: | CAT_ECOLX |
| AC: | P62577 |
| Organism: | Escherichia coli |
| Reign: | Bacteria |
| TaxID: | 562 |
| EC Number: | 2.3.1.28 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| G | 68 % |
| H | 32 % |
| B-Factor: | 26.855 |
|---|---|
| Number of residues: | 35 |
| Including | |
| Standard Amino Acids: | 34 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.343 | 1319.625 |
| % Hydrophobic | % Polar |
|---|---|
| 55.24 | 44.76 |
| According to VolSite | |
| HET Code: | FUA |
|---|---|
| Formula: | C31H47O6 |
| Molecular weight: | 515.701 g/mol |
| DrugBank ID: | DB02703 |
| Buried Surface Area: | 59.77 % |
| Polar Surface area: | 106.89 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 6 |
| H-Bond Donors: | 2 |
| Rings: | 4 |
| Aromatic rings: | 0 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| -34.8763 | 29.6456 | 63.6317 |
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 | CE2 | PHE- 25 | 3.63 | 0 | Hydrophobic |
| C27 | CG2 | VAL- 28 | 3.74 | 0 | Hydrophobic |
| C28 | CG2 | VAL- 28 | 3.88 | 0 | Hydrophobic |
| C16 | CB | ALA- 29 | 3.96 | 0 | Hydrophobic |
| C28 | CB | ALA- 29 | 4.36 | 0 | Hydrophobic |
| C7 | SG | CYS- 31 | 4.48 | 0 | Hydrophobic |
| C20 | SG | CYS- 31 | 4.09 | 0 | Hydrophobic |
| C3 | CG2 | THR- 93 | 4.39 | 0 | Hydrophobic |
| C2 | CG2 | THR- 93 | 3.4 | 0 | Hydrophobic |
| C2 | CE1 | PHE- 102 | 3.63 | 0 | Hydrophobic |
| O1 | OG | SER- 104 | 3.02 | 138.3 | H-Bond (Protein Donor) |
| C28 | CE2 | TYR- 133 | 4.15 | 0 | Hydrophobic |
| O1 | OH | TYR- 133 | 2.8 | 170.84 | H-Bond (Ligand Donor) |
| C28 | CE1 | PHE- 134 | 4.38 | 0 | Hydrophobic |
| C12 | CZ | PHE- 134 | 4.09 | 0 | Hydrophobic |
| C24 | CZ | PHE- 134 | 3.56 | 0 | Hydrophobic |
| C27 | CE2 | PHE- 138 | 3.6 | 0 | Hydrophobic |
| C11 | CD2 | PHE- 144 | 4.22 | 0 | Hydrophobic |
| C12 | CE2 | PHE- 144 | 3.78 | 0 | Hydrophobic |
| C13 | CZ | PHE- 144 | 4.22 | 0 | Hydrophobic |
| C19 | CB | PHE- 144 | 4.31 | 0 | Hydrophobic |
| C21 | CD1 | PHE- 144 | 4.08 | 0 | Hydrophobic |
| C23 | CZ | PHE- 144 | 3.66 | 0 | Hydrophobic |
| C3 | CB | SER- 146 | 3.66 | 0 | Hydrophobic |
| C18 | CZ | PHE- 156 | 3.53 | 0 | Hydrophobic |
| C6 | CD2 | LEU- 158 | 3.67 | 0 | Hydrophobic |
| C7 | CD1 | LEU- 158 | 3.3 | 0 | Hydrophobic |
| C21 | CD1 | LEU- 158 | 4.32 | 0 | Hydrophobic |
| C15 | CG2 | VAL- 160 | 4.1 | 0 | Hydrophobic |
| C32 | CG1 | VAL- 160 | 4.33 | 0 | Hydrophobic |
| C15 | CZ | PHE- 166 | 4.42 | 0 | Hydrophobic |
| C21 | CZ | PHE- 166 | 3.32 | 0 | Hydrophobic |
| C32 | CD1 | PHE- 166 | 3.83 | 0 | Hydrophobic |
| C19 | CG1 | VAL- 170 | 4.37 | 0 | Hydrophobic |
| C21 | CG2 | VAL- 170 | 4 | 0 | Hydrophobic |
| O6 | NE2 | HIS- 193 | 2.94 | 155.33 | H-Bond (Ligand Donor) |
