sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.980 Å
X-ray
2010-05-06
| Name: | Calmodulin-domain protein kinase 1, putative |
|---|---|
| ID: | A3FQ16_CRYPI |
| AC: | A3FQ16 |
| Organism: | Cryptosporidium parvum |
| Reign: | Eukaryota |
| TaxID: | 353152 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 48.349 |
|---|---|
| Number of residues: | 31 |
| Including | |
| Standard Amino Acids: | 30 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.940 | 745.875 |
| % Hydrophobic | % Polar |
|---|---|
| 48.87 | 51.13 |
| According to VolSite | |
| HET Code: | BK3 |
|---|---|
| Formula: | C22H25N6 |
| Molecular weight: | 373.474 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 64.44 % |
| Polar Surface area: | 86.23 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 4 |
| H-Bond Donors: | 2 |
| Rings: | 5 |
| Aromatic rings: | 4 |
| Anionic atoms: | 0 |
| Cationic atoms: | 1 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 4 |
| X | Y | Z |
|---|---|---|
| 25.4027 | 9.56789 | 5.07086 |
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 |
| CAO | CB | LEU- 82 | 4.41 | 0 | Hydrophobic |
| C5 | CG1 | VAL- 90 | 4.26 | 0 | Hydrophobic |
| CAO | CG1 | VAL- 90 | 4.11 | 0 | Hydrophobic |
| CAU | CG2 | VAL- 90 | 4.42 | 0 | Hydrophobic |
| CAE | CG1 | VAL- 90 | 3.94 | 0 | Hydrophobic |
| C5 | CB | ALA- 103 | 4.29 | 0 | Hydrophobic |
| CAE | CB | ALA- 103 | 3.72 | 0 | Hydrophobic |
| CAB | CD | LYS- 105 | 4.31 | 0 | Hydrophobic |
| CAH | CB | LYS- 105 | 3.67 | 0 | Hydrophobic |
| CAW | CB | LYS- 105 | 3.91 | 0 | Hydrophobic |
| DuAr | NZ | LYS- 105 | 3.8 | 153.78 | Pi/Cation |
| CAU | SD | MET- 136 | 3.63 | 0 | Hydrophobic |
| CAX | SD | MET- 136 | 3.72 | 0 | Hydrophobic |
| CAG | CD2 | LEU- 138 | 3.71 | 0 | Hydrophobic |
| CAW | CD2 | LEU- 138 | 4.02 | 0 | Hydrophobic |
| CAG | CG2 | ILE- 150 | 3.78 | 0 | Hydrophobic |
| NAA | O | GLU- 153 | 3.02 | 148.57 | H-Bond (Ligand Donor) |
| N1 | N | TYR- 155 | 3.13 | 172.32 | H-Bond (Protein Donor) |
| NAS | OE2 | GLU- 159 | 2.69 | 174.08 | H-Bond (Ligand Donor) |
| NAS | OE2 | GLU- 159 | 2.69 | 0 | Ionic (Ligand Cationic) |
| C5 | CD1 | LEU- 205 | 3.74 | 0 | Hydrophobic |
| CAM | CD2 | LEU- 205 | 4.13 | 0 | Hydrophobic |
| CAM | CD1 | ILE- 218 | 3.9 | 0 | Hydrophobic |
| CAN | CD1 | ILE- 218 | 3.85 | 0 | Hydrophobic |
| CAB | CD1 | LEU- 222 | 4.16 | 0 | Hydrophobic |
| NAR | O | HOH- 630 | 2.83 | 179.96 | H-Bond (Protein Donor) |
