sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.550 Å
X-ray
2001-10-02
| Name: | Acetyltransferase |
|---|---|
| ID: | TTR_PSEAJ |
| AC: | P16966 |
| Organism: | Pseudomonas amygdali pv. tabaci |
| Reign: | Bacteria |
| TaxID: | 322 |
| EC Number: | 2.3.1 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 93 % |
| B | 7 % |
| B-Factor: | 16.203 |
|---|---|
| Number of residues: | 45 |
| Including | |
| Standard Amino Acids: | 43 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 2 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.799 | 732.375 |
| % Hydrophobic | % Polar |
|---|---|
| 47.00 | 53.00 |
| According to VolSite | |
| HET Code: | ACO |
|---|---|
| Formula: | C23H34N7O17P3S |
| Molecular weight: | 805.539 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 56.74 % |
| 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: | 20 |
| X | Y | Z |
|---|---|---|
| 5.004 | -22.4209 | 44.9717 |
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 |
| C6P | CG2 | THR- 39 | 3.65 | 0 | Hydrophobic |
| C6P | CB | ALA- 44 | 3.95 | 0 | Hydrophobic |
| C6P | CG1 | VAL- 46 | 4.41 | 0 | Hydrophobic |
| C2P | CG1 | VAL- 46 | 4.31 | 0 | Hydrophobic |
| CH3 | CG1 | VAL- 104 | 4.28 | 0 | Hydrophobic |
| CEP | CG | LEU- 107 | 3.39 | 0 | Hydrophobic |
| N4P | O | LEU- 107 | 3.1 | 155.33 | H-Bond (Ligand Donor) |
| O | N | LEU- 107 | 3.07 | 165.42 | H-Bond (Protein Donor) |
| CCP | CG2 | VAL- 109 | 4.39 | 0 | Hydrophobic |
| CEP | CG2 | VAL- 109 | 3.83 | 0 | Hydrophobic |
| CAP | CB | VAL- 109 | 4.24 | 0 | Hydrophobic |
| O9P | N | VAL- 109 | 2.92 | 154.98 | H-Bond (Protein Donor) |
| CAP | CD | ARG- 114 | 3.94 | 0 | Hydrophobic |
| O2A | N | GLY- 117 | 3.22 | 139.93 | H-Bond (Protein Donor) |
| O4A | N | GLY- 119 | 2.69 | 138.04 | H-Bond (Protein Donor) |
| C5B | CB | ARG- 120 | 4.48 | 0 | Hydrophobic |
| O1A | N | ARG- 120 | 3.02 | 147.99 | H-Bond (Protein Donor) |
| O8A | NZ | LYS- 132 | 2.88 | 135.97 | H-Bond (Protein Donor) |
| O8A | NZ | LYS- 132 | 2.88 | 0 | Ionic (Protein Cationic) |
| O9A | NZ | LYS- 132 | 3.39 | 0 | Ionic (Protein Cationic) |
| CH3 | CB | LEU- 140 | 3.78 | 0 | Hydrophobic |
| S1P | CB | THR- 142 | 3.46 | 0 | Hydrophobic |
| CDP | CB | ALA- 148 | 4.15 | 0 | Hydrophobic |
| C4B | CD1 | PHE- 151 | 4.49 | 0 | Hydrophobic |
| C5B | CE1 | PHE- 151 | 4.12 | 0 | Hydrophobic |
| CCP | CD1 | PHE- 151 | 3.63 | 0 | Hydrophobic |
| CDP | CG | PHE- 151 | 4.16 | 0 | Hydrophobic |
| S1P | CE1 | TYR- 152 | 4.34 | 0 | Hydrophobic |
| C4B | CB | ALA- 154 | 4.26 | 0 | Hydrophobic |
| C1B | CB | ALA- 154 | 3.94 | 0 | Hydrophobic |
