sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.200 Å
X-ray
1997-07-01
| Name: | Peptidyl-prolyl cis-trans isomerase FKBP1A | Serine/threonine-protein kinase mTOR |
|---|---|---|
| ID: | FKB1A_HUMAN | MTOR_HUMAN |
| AC: | P62942 | P42345 |
| Organism: | Homo sapiens | |
| Reign: | Eukaryota | |
| TaxID: | 9606 | |
| EC Number: | 5.2.1.8 | 2.7.11.1 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 55 % |
| B | 45 % |
| B-Factor: | 13.421 |
|---|---|
| Number of residues: | 46 |
| Including | |
| Standard Amino Acids: | 44 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 2 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.656 | 1788.750 |
| % Hydrophobic | % Polar |
|---|---|
| 45.85 | 54.15 |
| According to VolSite | |
| HET Code: | RAD |
|---|---|
| Formula: | C52H81NO13 |
| Molecular weight: | 928.198 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 64.71 % |
| Polar Surface area: | 195.42 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 13 |
| H-Bond Donors: | 3 |
| Rings: | 4 |
| Aromatic rings: | 0 |
| Anionic atoms: | 0 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 3 |
| Rotatable Bonds: | 7 |
| X | Y | Z |
|---|---|---|
| -9.30591 | 26.7831 | 36.6927 |
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 | CZ | TYR- 26 | 3.81 | 0 | Hydrophobic |
| C9 | CE1 | PHE- 36 | 4.47 | 0 | Hydrophobic |
| C42 | CE1 | PHE- 36 | 3.73 | 0 | Hydrophobic |
| C9 | CB | ASP- 37 | 4.36 | 0 | Hydrophobic |
| O6 | OD2 | ASP- 37 | 2.74 | 176.14 | H-Bond (Ligand Donor) |
| C4 | CE2 | PHE- 46 | 3.71 | 0 | Hydrophobic |
| C5 | CZ | PHE- 46 | 3.99 | 0 | Hydrophobic |
| C47 | CE1 | PHE- 46 | 4.03 | 0 | Hydrophobic |
| O13 | O | GLN- 53 | 2.65 | 159.62 | H-Bond (Ligand Donor) |
| O10 | O | GLU- 54 | 2.82 | 157.09 | H-Bond (Ligand Donor) |
| C4 | CG1 | VAL- 55 | 3.96 | 0 | Hydrophobic |
| O2 | N | ILE- 56 | 3 | 160.2 | H-Bond (Protein Donor) |
| C3 | CG1 | ILE- 56 | 4.42 | 0 | Hydrophobic |
| C41 | CG2 | ILE- 56 | 3.83 | 0 | Hydrophobic |
| C3 | CE2 | TRP- 59 | 3.35 | 0 | Hydrophobic |
| C4 | CZ2 | TRP- 59 | 3.71 | 0 | Hydrophobic |
| O3 | OH | TYR- 82 | 2.75 | 164.58 | H-Bond (Protein Donor) |
| C34 | CE1 | TYR- 82 | 3.94 | 0 | Hydrophobic |
| C11 | CD1 | ILE- 90 | 4.31 | 0 | Hydrophobic |
| C42 | CG2 | ILE- 90 | 3.82 | 0 | Hydrophobic |
| C42 | CG1 | ILE- 91 | 3.89 | 0 | Hydrophobic |
| C3 | CZ | PHE- 99 | 4.46 | 0 | Hydrophobic |
| C44 | CB | LEU- 2031 | 3.93 | 0 | Hydrophobic |
| C50 | CG | GLU- 2032 | 4.35 | 0 | Hydrophobic |
| C26 | CB | SER- 2035 | 4.4 | 0 | Hydrophobic |
| C46 | CB | SER- 2035 | 4.09 | 0 | Hydrophobic |
| C22 | CB | SER- 2035 | 4.12 | 0 | Hydrophobic |
| C50 | CB | ARG- 2036 | 3.84 | 0 | Hydrophobic |
| C12 | CE1 | PHE- 2039 | 3.83 | 0 | Hydrophobic |
| C15 | CZ | PHE- 2039 | 4.12 | 0 | Hydrophobic |
| C35 | CB | PHE- 2039 | 3.84 | 0 | Hydrophobic |
| C37 | CB | PHE- 2039 | 4.4 | 0 | Hydrophobic |
| C46 | CD2 | PHE- 2039 | 3.7 | 0 | Hydrophobic |
| C48 | CD1 | PHE- 2039 | 3.49 | 0 | Hydrophobic |
| C49 | CB | THR- 2098 | 4.25 | 0 | Hydrophobic |
| C44 | CZ3 | TRP- 2101 | 4.19 | 0 | Hydrophobic |
| C49 | CB | TRP- 2101 | 4.46 | 0 | Hydrophobic |
| C52 | CB | ASP- 2102 | 3.82 | 0 | Hydrophobic |
| C22 | CD1 | TYR- 2105 | 4.45 | 0 | Hydrophobic |
| C43 | CD2 | TYR- 2105 | 3.8 | 0 | Hydrophobic |
| C47 | CZ | TYR- 2105 | 4.21 | 0 | Hydrophobic |
| C22 | CD2 | PHE- 2108 | 3.94 | 0 | Hydrophobic |
| C23 | CE2 | PHE- 2108 | 3.98 | 0 | Hydrophobic |
| C44 | CD1 | PHE- 2108 | 3.74 | 0 | Hydrophobic |
| C45 | CE2 | PHE- 2108 | 4.32 | 0 | Hydrophobic |
