sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.210 Å
X-ray
2011-07-06
| Name: | Glutathione reductase, mitochondrial |
|---|---|
| ID: | GSHR_HUMAN |
| AC: | P00390 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 1.8.1.7 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 94 % |
| B | 6 % |
| B-Factor: | 16.326 |
|---|---|
| Number of residues: | 74 |
| Including | |
| Standard Amino Acids: | 66 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 8 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.905 | 1640.250 |
| % Hydrophobic | % Polar |
|---|---|
| 37.45 | 62.55 |
| According to VolSite | |
| HET Code: | FAD |
|---|---|
| Formula: | C27H31N9O15P2 |
| Molecular weight: | 783.534 g/mol |
| DrugBank ID: | DB03147 |
| Buried Surface Area: | 77.68 % |
| Polar Surface area: | 381.7 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 22 |
| H-Bond Donors: | 7 |
| Rings: | 6 |
| Aromatic rings: | 3 |
| Anionic atoms: | 2 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 3 |
| Rotatable Bonds: | 13 |
| X | Y | Z |
|---|---|---|
| -22.0117 | -16.5346 | -20.1393 |
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 |
| O1A | N | SER- 30 | 3.35 | 158.14 | H-Bond (Protein Donor) |
| C4' | CB | SER- 30 | 4.32 | 0 | Hydrophobic |
| O1P | N | GLY- 31 | 2.78 | 150.51 | H-Bond (Protein Donor) |
| O3B | OE1 | GLU- 50 | 2.74 | 173.6 | H-Bond (Ligand Donor) |
| O3B | OE2 | GLU- 50 | 2.98 | 122.12 | H-Bond (Ligand Donor) |
| O2B | OE2 | GLU- 50 | 2.76 | 165.68 | H-Bond (Ligand Donor) |
| N3A | N | SER- 51 | 3.19 | 133.77 | H-Bond (Protein Donor) |
| O1A | N | THR- 57 | 3.16 | 136.9 | H-Bond (Protein Donor) |
| O2A | N | THR- 57 | 3.17 | 149.49 | H-Bond (Protein Donor) |
| O2A | OG1 | THR- 57 | 2.68 | 160.6 | H-Bond (Protein Donor) |
| C8M | CG2 | THR- 57 | 3.79 | 0 | Hydrophobic |
| O4' | N | CYS- 58 | 3.37 | 138.01 | H-Bond (Protein Donor) |
| C9A | SG | CYS- 63 | 4.32 | 0 | Hydrophobic |
| C1' | SG | CYS- 63 | 4.38 | 0 | Hydrophobic |
| N5 | NZ | LYS- 66 | 2.95 | 162.38 | H-Bond (Protein Donor) |
| C6 | CB | LYS- 66 | 4.28 | 0 | Hydrophobic |
| N6A | O | ALA- 130 | 2.92 | 169.13 | H-Bond (Ligand Donor) |
| N1A | N | ALA- 130 | 2.82 | 170.06 | H-Bond (Protein Donor) |
| C7M | CB | SER- 177 | 3.58 | 0 | Hydrophobic |
| C7M | CE2 | PHE- 181 | 4.02 | 0 | Hydrophobic |
| C7M | CG2 | ILE- 198 | 4.24 | 0 | Hydrophobic |
| C9 | CD1 | ILE- 198 | 4.42 | 0 | Hydrophobic |
| C8 | CD1 | ILE- 198 | 3.94 | 0 | Hydrophobic |
| C8M | CD | ARG- 291 | 4.45 | 0 | Hydrophobic |
| O3' | OD2 | ASP- 331 | 2.8 | 173.84 | H-Bond (Ligand Donor) |
| O3' | OD1 | ASP- 331 | 3.25 | 126.29 | H-Bond (Ligand Donor) |
| C5' | CB | ASP- 331 | 4.32 | 0 | Hydrophobic |
| O2P | N | ASP- 331 | 2.95 | 148.48 | H-Bond (Protein Donor) |
| N1 | N | THR- 339 | 3.3 | 153.55 | H-Bond (Protein Donor) |
| O2 | N | THR- 339 | 2.81 | 138.53 | H-Bond (Protein Donor) |
| C4' | CB | THR- 339 | 4.41 | 0 | Hydrophobic |
| C5' | CB | ALA- 342 | 4.22 | 0 | Hydrophobic |
| N3 | O | HIS- 467 | 2.53 | 149.14 | H-Bond (Ligand Donor) |
| O2A | O | HOH- 504 | 3.09 | 179.97 | H-Bond (Protein Donor) |
