sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.700 Å
X-ray
2008-12-01
| Name: | Bleomycin acetyltransferase |
|---|---|
| ID: | Q53796_9ACTN |
| AC: | Q53796 |
| Organism: | Streptomyces verticillus |
| Reign: | Bacteria |
| TaxID: | 29309 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 87 % |
| C | 13 % |
| B-Factor: | 24.672 |
|---|---|
| Number of residues: | 39 |
| Including | |
| Standard Amino Acids: | 38 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 0 |
| Cofactors: | COA |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.883 | 1620.000 |
| % Hydrophobic | % Polar |
|---|---|
| 50.63 | 49.38 |
| According to VolSite | |
| HET Code: | COA |
|---|---|
| Formula: | C21H32N7O16P3S |
| Molecular weight: | 763.502 g/mol |
| DrugBank ID: | DB01992 |
| Buried Surface Area: | 61.16 % |
| Polar Surface area: | 426.11 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 21 |
| H-Bond Donors: | 6 |
| Rings: | 3 |
| Aromatic rings: | 2 |
| Anionic atoms: | 4 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 3 |
| Rotatable Bonds: | 18 |
| X | Y | Z |
|---|---|---|
| -55.8712 | 97.4614 | -41.7417 |
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 | CG1 | VAL- 40 | 4.45 | 0 | Hydrophobic |
| C6P | CZ3 | TRP- 44 | 4.08 | 0 | Hydrophobic |
| C2P | CZ3 | TRP- 44 | 3.72 | 0 | Hydrophobic |
| C2P | CG2 | THR- 96 | 4.43 | 0 | Hydrophobic |
| N4P | O | TRP- 97 | 3.15 | 162.28 | H-Bond (Ligand Donor) |
| S1P | CE2 | TRP- 97 | 4.3 | 0 | Hydrophobic |
| C6P | CB | LEU- 98 | 3.91 | 0 | Hydrophobic |
| CCP | CD1 | LEU- 99 | 4.14 | 0 | Hydrophobic |
| CDP | CG | LEU- 99 | 4.31 | 0 | Hydrophobic |
| O9P | N | LEU- 99 | 3.1 | 171.35 | H-Bond (Protein Donor) |
| CAP | CE2 | TRP- 104 | 3.51 | 0 | Hydrophobic |
| O9P | NE1 | TRP- 104 | 2.97 | 120.02 | H-Bond (Protein Donor) |
| O4A | N | GLY- 105 | 2.66 | 152.6 | H-Bond (Protein Donor) |
| O5B | N | GLY- 107 | 3.18 | 145.54 | H-Bond (Protein Donor) |
| O1A | N | ALA- 109 | 2.9 | 142.88 | H-Bond (Protein Donor) |
| CCP | CB | ALA- 109 | 3.72 | 0 | Hydrophobic |
| O2A | N | THR- 110 | 3.27 | 147.3 | H-Bond (Protein Donor) |
| S1P | CG1 | ILE- 133 | 4.2 | 0 | Hydrophobic |
| O5P | ND2 | ASN- 137 | 2.98 | 160.04 | H-Bond (Protein Donor) |
| O5A | NH1 | ARG- 139 | 2.53 | 131.38 | H-Bond (Protein Donor) |
| O5A | CZ | ARG- 139 | 3.61 | 0 | Ionic (Protein Cationic) |
| CEP | CB | ARG- 139 | 3.6 | 0 | Hydrophobic |
| CEP | CB | SER- 140 | 4.45 | 0 | Hydrophobic |
| CBP | CG2 | VAL- 143 | 4.31 | 0 | Hydrophobic |
| O2A | CZ | ARG- 146 | 3.98 | 0 | Ionic (Protein Cationic) |
| N6A | O2B | COA- 402 | 3.24 | 136.53 | H-Bond (Ligand Donor) |
| O2B | N7A | COA- 402 | 2.74 | 162.08 | H-Bond (Ligand Donor) |
| N7A | O2B | COA- 402 | 3.19 | 152.09 | H-Bond (Protein Donor) |
| O2B | N6A | COA- 402 | 2.88 | 140.97 | H-Bond (Protein Donor) |
