sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.040 Å
X-ray
2013-06-24
| Name: | FAD-linked sulfhydryl oxidase ALR |
|---|---|
| ID: | ALR_HUMAN |
| AC: | P55789 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 1.8.3.2 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 26.042 |
|---|---|
| Number of residues: | 45 |
| Including | |
| Standard Amino Acids: | 41 |
| Non Standard Amino Acids: | 2 |
| Water Molecules: | 2 |
| Cofactors: | |
| Metals: | NA |
| Ligandability | Volume (Å3) |
|---|---|
| 1.066 | 519.750 |
| % Hydrophobic | % Polar |
|---|---|
| 62.34 | 37.66 |
| According to VolSite | |
| HET Code: | FAD |
|---|---|
| Formula: | C27H31N9O15P2 |
| Molecular weight: | 783.534 g/mol |
| DrugBank ID: | DB03147 |
| Buried Surface Area: | 64.11 % |
| 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 |
|---|---|---|
| -6.53526 | -11.8061 | -6.48777 |
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 |
| O2 | NE | ARG- 99 | 3.22 | 162.32 | H-Bond (Protein Donor) |
| C4' | CG | GLU- 100 | 4.26 | 0 | Hydrophobic |
| C5' | CB | GLU- 100 | 4.17 | 0 | Hydrophobic |
| C5' | CG | ARG- 104 | 3.93 | 0 | Hydrophobic |
| O2P | NE | ARG- 104 | 2.66 | 155.51 | H-Bond (Protein Donor) |
| O2P | CZ | ARG- 104 | 3.65 | 0 | Ionic (Protein Cationic) |
| C8M | CB | SER- 106 | 3.47 | 0 | Hydrophobic |
| C7M | CH2 | TRP- 107 | 3.85 | 0 | Hydrophobic |
| C8M | CD2 | TRP- 107 | 3.38 | 0 | Hydrophobic |
| C8 | CZ2 | TRP- 107 | 3.49 | 0 | Hydrophobic |
| O2' | NE1 | TRP- 107 | 2.99 | 166.59 | H-Bond (Protein Donor) |
| C7M | CE2 | PHE- 136 | 4.49 | 0 | Hydrophobic |
| C8M | CZ | TYR- 140 | 4.3 | 0 | Hydrophobic |
| C7M | CD2 | LEU- 149 | 3.64 | 0 | Hydrophobic |
| N6A | O | CYS- 171 | 2.81 | 154.49 | H-Bond (Ligand Donor) |
| O2A | NE2 | HIS- 174 | 2.92 | 173.83 | H-Bond (Protein Donor) |
| N6A | OD1 | ASN- 175 | 3.12 | 122.51 | H-Bond (Ligand Donor) |
| C9A | CG1 | VAL- 177 | 4.43 | 0 | Hydrophobic |
| C2' | CG1 | VAL- 177 | 4.46 | 0 | Hydrophobic |
| N7A | ND2 | ASN- 178 | 3.04 | 162.16 | H-Bond (Protein Donor) |
| O4 | NZ | LYS- 180 | 3.13 | 144.32 | H-Bond (Protein Donor) |
| C2' | CD1 | LEU- 181 | 3.9 | 0 | Hydrophobic |
| O5' | NZ | LYS- 183 | 3.19 | 132.37 | H-Bond (Protein Donor) |
| O1P | NZ | LYS- 183 | 2.76 | 144.72 | H-Bond (Protein Donor) |
| O1P | NZ | LYS- 183 | 2.76 | 0 | Ionic (Protein Cationic) |
| DuAr | DuAr | PHE- 186 | 3.99 | 0 | Aromatic Face/Face |
| C2B | CD1 | PHE- 186 | 4.16 | 0 | Hydrophobic |
| O2B | NE | ARG- 194 | 3.03 | 166.93 | H-Bond (Protein Donor) |
| C4B | CZ2 | TRP- 195 | 4.18 | 0 | Hydrophobic |
| C1B | CZ2 | TRP- 195 | 3.91 | 0 | Hydrophobic |
| N3A | NE1 | TRP- 195 | 2.91 | 178.57 | H-Bond (Protein Donor) |
