sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.300 Å
X-ray
2000-02-29
| Name: | Aequorin-2 |
|---|---|
| ID: | AEQ2_AEQVI |
| AC: | P02592 |
| Organism: | Aequorea victoria |
| Reign: | Eukaryota |
| TaxID: | 6100 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 29.568 |
|---|---|
| Number of residues: | 40 |
| Including | |
| Standard Amino Acids: | 40 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 2.030 | 425.250 |
| % Hydrophobic | % Polar |
|---|---|
| 84.92 | 15.08 |
| According to VolSite | |
| HET Code: | CZH |
|---|---|
| Formula: | C26H22N3O5 |
| Molecular weight: | 456.470 g/mol |
| DrugBank ID: | DB02241 |
| Buried Surface Area: | 76.55 % |
| Polar Surface area: | 116.56 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 6 |
| H-Bond Donors: | 4 |
| Rings: | 5 |
| Aromatic rings: | 3 |
| Anionic atoms: | 0 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| 59.4315 | 22.3009 | 8.40506 |
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 |
| O25 | ND1 | HIS- 16 | 2.67 | 175.43 | H-Bond (Ligand Donor) |
| C19 | CE | MET- 19 | 3.49 | 0 | Hydrophobic |
| C22 | CB | MET- 19 | 3.5 | 0 | Hydrophobic |
| C23 | CG | MET- 19 | 3.67 | 0 | Hydrophobic |
| C26 | CE2 | PHE- 22 | 4.24 | 0 | Hydrophobic |
| C21 | CD1 | LEU- 23 | 3.81 | 0 | Hydrophobic |
| C32 | CD2 | LEU- 23 | 3.72 | 0 | Hydrophobic |
| C29 | CG | LYS- 39 | 4.15 | 0 | Hydrophobic |
| C31 | CD | LYS- 39 | 3.92 | 0 | Hydrophobic |
| C30 | CB | ALA- 40 | 3.85 | 0 | Hydrophobic |
| C29 | CD1 | ILE- 43 | 4 | 0 | Hydrophobic |
| C30 | CG1 | VAL- 62 | 4.34 | 0 | Hydrophobic |
| O25 | OH | TYR- 82 | 2.67 | 143.3 | H-Bond (Protein Donor) |
| C22 | CZ2 | TRP- 86 | 3.39 | 0 | Hydrophobic |
| C16 | CD1 | ILE- 105 | 3.7 | 0 | Hydrophobic |
| C10 | CE2 | TRP- 108 | 3.76 | 0 | Hydrophobic |
| C16 | CB | TRP- 108 | 4.36 | 0 | Hydrophobic |
| C26 | CH2 | TRP- 108 | 4.42 | 0 | Hydrophobic |
| C12 | CD2 | LEU- 112 | 3.58 | 0 | Hydrophobic |
| C13 | CE1 | PHE- 113 | 3.38 | 0 | Hydrophobic |
| N1 | OH | TYR- 132 | 2.53 | 166.17 | H-Bond (Protein Donor) |
| C10 | CZ | TYR- 132 | 3.92 | 0 | Hydrophobic |
| C13 | CG | MET- 165 | 3.89 | 0 | Hydrophobic |
| O18 | OH | TYR- 184 | 3.4 | 120.37 | H-Bond (Protein Donor) |
| O34 | OH | TYR- 184 | 2.59 | 155.78 | H-Bond (Protein Donor) |
