sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.100 Å
X-ray
1996-05-31
| Name: | Candidapepsin-2 |
|---|---|
| ID: | CARP2_CANAX |
| AC: | P0CS83 |
| Organism: | Candida albicans |
| Reign: | Eukaryota |
| TaxID: | 5476 |
| EC Number: | 3.4.23.24 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 26.395 |
|---|---|
| Number of residues: | 51 |
| Including | |
| Standard Amino Acids: | 47 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 4 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.672 | 843.750 |
| % Hydrophobic | % Polar |
|---|---|
| 33.20 | 66.80 |
| According to VolSite | |
| HET Code: | A70 |
|---|---|
| Formula: | C42H71N6O5 |
| Molecular weight: | 740.050 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 56.66 % |
| Polar Surface area: | 126.73 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 5 |
| H-Bond Donors: | 4 |
| Rings: | 4 |
| Aromatic rings: | 1 |
| Anionic atoms: | 0 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 2 |
| Rotatable Bonds: | 18 |
| X | Y | Z |
|---|---|---|
| 41.6946 | 24.9065 | 13.6269 |
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 |
| C5' | CG2 | VAL- 12 | 3.77 | 0 | Hydrophobic |
| C3' | CB | THR- 13 | 3.71 | 0 | Hydrophobic |
| C3'1 | CD1 | ILE- 30 | 3.98 | 0 | Hydrophobic |
| O11 | OD1 | ASP- 32 | 2.54 | 151.86 | H-Bond (Ligand Donor) |
| O11 | OD2 | ASP- 32 | 3.39 | 149.2 | H-Bond (Ligand Donor) |
| N3 | O | GLY- 34 | 2.93 | 153.17 | H-Bond (Ligand Donor) |
| C25 | CB | SER- 35 | 4.12 | 0 | Hydrophobic |
| C42 | CD1 | ILE- 82 | 3.38 | 0 | Hydrophobic |
| C12 | CD1 | TYR- 84 | 4.05 | 0 | Hydrophobic |
| C33 | CD1 | TYR- 84 | 4.21 | 0 | Hydrophobic |
| C5'1 | CB | TYR- 84 | 4.38 | 0 | Hydrophobic |
| C6'1 | CG | TYR- 84 | 3.61 | 0 | Hydrophobic |
| O3 | N | GLY- 85 | 3 | 137.13 | H-Bond (Protein Donor) |
| C5'1 | CB | SER- 88 | 4.17 | 0 | Hydrophobic |
| C4'1 | CG2 | ILE- 119 | 3.69 | 0 | Hydrophobic |
| C5'1 | CD1 | ILE- 119 | 4.13 | 0 | Hydrophobic |
| C2'1 | CD1 | ILE- 123 | 3.79 | 0 | Hydrophobic |
| C42 | CB | ALA- 133 | 3.83 | 0 | Hydrophobic |
| C2'2 | CD2 | LEU- 216 | 3.67 | 0 | Hydrophobic |
| O11 | OD2 | ASP- 218 | 2.51 | 170.86 | H-Bond (Protein Donor) |
| N21 | O | GLY- 220 | 3.35 | 150.7 | H-Bond (Ligand Donor) |
| C32 | CG2 | THR- 221 | 4.22 | 0 | Hydrophobic |
| O1 | N | THR- 222 | 3.4 | 156.12 | H-Bond (Protein Donor) |
| C' | CB | THR- 222 | 4.15 | 0 | Hydrophobic |
| C32 | CE1 | TYR- 225 | 4.36 | 0 | Hydrophobic |
| C51 | CD1 | TYR- 225 | 3.65 | 0 | Hydrophobic |
| C51 | CB | ASN- 301 | 3.64 | 0 | Hydrophobic |
| C51 | CB | ALA- 303 | 4.19 | 0 | Hydrophobic |
| C32 | CD1 | ILE- 305 | 3.91 | 0 | Hydrophobic |
| C3'2 | CD1 | ILE- 305 | 4.1 | 0 | Hydrophobic |
