sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.400 Å
X-ray
2011-01-04
| 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: | 10.203 |
|---|---|
| Number of residues: | 41 |
| Including | |
| Standard Amino Acids: | 38 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 3 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.842 | 722.250 |
| % Hydrophobic | % Polar |
|---|---|
| 34.58 | 65.42 |
| According to VolSite | |
| HET Code: | RIT |
|---|---|
| Formula: | C37H48N6O5S2 |
| Molecular weight: | 720.944 g/mol |
| DrugBank ID: | DB00503 |
| Buried Surface Area: | 52.95 % |
| Polar Surface area: | 202.26 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 7 |
| H-Bond Donors: | 4 |
| Rings: | 4 |
| Aromatic rings: | 4 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 2 |
| Rotatable Bonds: | 18 |
| X | Y | Z |
|---|---|---|
| -24.1441 | -13.3872 | 21.6952 |
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 |
| C90 | CG2 | VAL- 12 | 4.12 | 0 | Hydrophobic |
| S81 | CB | THR- 13 | 3.71 | 0 | Hydrophobic |
| S81 | CD1 | ILE- 30 | 4.49 | 0 | Hydrophobic |
| C86 | CD1 | ILE- 30 | 3.95 | 0 | Hydrophobic |
| O41 | OD1 | ASP- 32 | 2.66 | 167.31 | H-Bond (Protein Donor) |
| N11 | O | GLY- 34 | 3.16 | 131.76 | H-Bond (Ligand Donor) |
| S3 | CB | SER- 35 | 4.08 | 0 | Hydrophobic |
| C6 | CB | SER- 35 | 4.15 | 0 | Hydrophobic |
| C6 | CD1 | ILE- 82 | 4.24 | 0 | Hydrophobic |
| C6 | CD1 | TYR- 84 | 3.46 | 0 | Hydrophobic |
| C14 | CD1 | TYR- 84 | 4.11 | 0 | Hydrophobic |
| C44 | CD1 | TYR- 84 | 4.27 | 0 | Hydrophobic |
| C52 | CG | TYR- 84 | 3.38 | 0 | Hydrophobic |
| O61 | N | GLY- 85 | 3.01 | 137.31 | H-Bond (Protein Donor) |
| C50 | CB | SER- 88 | 3.94 | 0 | Hydrophobic |
| C50 | CG1 | ILE- 119 | 4.3 | 0 | Hydrophobic |
| C86 | CG2 | ILE- 119 | 3.98 | 0 | Hydrophobic |
| C51 | CD1 | ILE- 119 | 3.67 | 0 | Hydrophobic |
| C52 | CD1 | ILE- 123 | 4.09 | 0 | Hydrophobic |
| C26 | CD2 | LEU- 216 | 4.05 | 0 | Hydrophobic |
| O41 | OD1 | ASP- 218 | 3.02 | 121.81 | H-Bond (Ligand Donor) |
| N58 | O | GLY- 220 | 2.95 | 143.17 | H-Bond (Ligand Donor) |
| C68 | CG2 | THR- 221 | 4.07 | 0 | Hydrophobic |
| O76 | N | THR- 222 | 3.13 | 160.91 | H-Bond (Protein Donor) |
| C68 | CE1 | TYR- 225 | 3.61 | 0 | Hydrophobic |
| C31 | CD1 | ILE- 305 | 4.36 | 0 | Hydrophobic |
| C64 | CD1 | ILE- 305 | 3.6 | 0 | Hydrophobic |
