sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.650 Å
X-ray
2007-11-19
| Name: | Putative NAD(P)H nitroreductase MhqN |
|---|---|
| ID: | MHQN_BACSU |
| AC: | P96692 |
| Organism: | Bacillus subtilis |
| Reign: | Bacteria |
| TaxID: | 224308 |
| EC Number: | 1 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 61 % |
| B | 39 % |
| B-Factor: | 19.201 |
|---|---|
| Number of residues: | 33 |
| Including | |
| Standard Amino Acids: | 33 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.992 | 786.375 |
| % Hydrophobic | % Polar |
|---|---|
| 49.79 | 50.21 |
| According to VolSite | |
| HET Code: | FMN |
|---|---|
| Formula: | C17H19N4O9P |
| Molecular weight: | 454.328 g/mol |
| DrugBank ID: | DB03247 |
| Buried Surface Area: | 67.48 % |
| Polar Surface area: | 217.05 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 12 |
| H-Bond Donors: | 4 |
| Rings: | 3 |
| Aromatic rings: | 1 |
| Anionic atoms: | 2 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 7 |
| X | Y | Z |
|---|---|---|
| 9.36874 | 10.0203 | 58.9652 |
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 |
| O3P | NH2 | ARG- 11 | 2.91 | 169.07 | H-Bond (Protein Donor) |
| O3P | NH1 | ARG- 11 | 3.45 | 134.9 | H-Bond (Protein Donor) |
| O3P | CZ | ARG- 11 | 3.63 | 0 | Ionic (Protein Cationic) |
| O1P | NE | ARG- 12 | 3.03 | 164.68 | H-Bond (Protein Donor) |
| O1P | CZ | ARG- 12 | 3.99 | 0 | Ionic (Protein Cationic) |
| C1' | CB | SER- 13 | 4.16 | 0 | Hydrophobic |
| C3' | CB | SER- 13 | 4.04 | 0 | Hydrophobic |
| O3' | OG | SER- 13 | 3.14 | 127.31 | H-Bond (Protein Donor) |
| O1P | N | SER- 13 | 2.78 | 158.26 | H-Bond (Protein Donor) |
| O3P | OG | SER- 13 | 2.9 | 144.82 | H-Bond (Protein Donor) |
| C8M | CB | PRO- 39 | 4.01 | 0 | Hydrophobic |
| O3' | N | SER- 40 | 3.5 | 127.55 | H-Bond (Protein Donor) |
| C7 | CB | ALA- 41 | 3.41 | 0 | Hydrophobic |
| C4' | CB | ASN- 43 | 4.03 | 0 | Hydrophobic |
| N3 | OE1 | GLN- 68 | 3.28 | 158.37 | H-Bond (Ligand Donor) |
| C7M | CD | ARG- 133 | 4.11 | 0 | Hydrophobic |
| C7M | CD1 | LEU- 137 | 4.18 | 0 | Hydrophobic |
| C8M | CD1 | LEU- 137 | 3.38 | 0 | Hydrophobic |
| C1' | SG | CYS- 154 | 4.23 | 0 | Hydrophobic |
| C1' | CG | PRO- 155 | 4.25 | 0 | Hydrophobic |
| C8M | CG | PRO- 155 | 3.85 | 0 | Hydrophobic |
| C9 | CG | PRO- 155 | 3.53 | 0 | Hydrophobic |
| O4 | N | ILE- 157 | 3.29 | 129.94 | H-Bond (Protein Donor) |
| N5 | N | ILE- 157 | 2.95 | 141.45 | H-Bond (Protein Donor) |
| C6 | CG2 | ILE- 157 | 3.58 | 0 | Hydrophobic |
| O4 | N | GLY- 158 | 3.06 | 147.78 | H-Bond (Protein Donor) |
| C7M | SD | MET- 178 | 4.36 | 0 | Hydrophobic |
| O2P | CZ | ARG- 193 | 3.87 | 0 | Ionic (Protein Cationic) |
| O2P | NH1 | ARG- 193 | 2.79 | 150.44 | H-Bond (Protein Donor) |
| O2P | CZ | ARG- 196 | 3.45 | 0 | Ionic (Protein Cationic) |
| O2P | NH1 | ARG- 196 | 3.25 | 132.5 | H-Bond (Protein Donor) |
| O2P | NH2 | ARG- 196 | 2.83 | 151.64 | H-Bond (Protein Donor) |
