sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
1.900 Å
X-ray
1998-07-23
| Name: | Peptidyl-prolyl cis-trans isomerase FKBP1A |
|---|---|
| ID: | FKB1A_HUMAN |
| AC: | P62942 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 5.2.1.8 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 4 % |
| B | 96 % |
| B-Factor: | 15.852 |
|---|---|
| Number of residues: | 28 |
| Including | |
| Standard Amino Acids: | 27 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.866 | 286.875 |
| % Hydrophobic | % Polar |
|---|---|
| 52.94 | 47.06 |
| According to VolSite | |
| HET Code: | AP1 |
|---|---|
| Formula: | C38H46NO11 |
| Molecular weight: | 692.772 g/mol |
| DrugBank ID: | DB01723 |
| Buried Surface Area: | 50.33 % |
| Polar Surface area: | 142.12 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 11 |
| H-Bond Donors: | 0 |
| Rings: | 4 |
| Aromatic rings: | 3 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 2 |
| Rotatable Bonds: | 18 |
| X | Y | Z |
|---|---|---|
| 11.5566 | 14.5044 | 21.9435 |
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 | CE2 | TYR- 26 | 3.53 | 0 | Hydrophobic |
| C16 | CE1 | TYR- 26 | 4.45 | 0 | Hydrophobic |
| C16 | CG2 | VAL- 36 | 3.43 | 0 | Hydrophobic |
| C16 | CB | ASP- 37 | 4.06 | 0 | Hydrophobic |
| C4 | CE2 | PHE- 46 | 3.63 | 0 | Hydrophobic |
| C5 | CZ | PHE- 46 | 3.83 | 0 | Hydrophobic |
| C37 | CZ | PHE- 46 | 3.82 | 0 | Hydrophobic |
| C24 | CE1 | PHE- 46 | 3.5 | 0 | Hydrophobic |
| C4 | CG1 | VAL- 55 | 4.03 | 0 | Hydrophobic |
| C41 | CG1 | VAL- 55 | 4.26 | 0 | Hydrophobic |
| C3 | CG1 | ILE- 56 | 4.28 | 0 | Hydrophobic |
| C42 | CG2 | ILE- 56 | 3.68 | 0 | Hydrophobic |
| C31 | CG2 | ILE- 56 | 4.1 | 0 | Hydrophobic |
| O44 | N | ILE- 56 | 2.9 | 157.87 | H-Bond (Protein Donor) |
| C5 | CZ2 | TRP- 59 | 3.96 | 0 | Hydrophobic |
| C3 | CE2 | TRP- 59 | 3.38 | 0 | Hydrophobic |
| C20 | CE1 | TYR- 82 | 3.87 | 0 | Hydrophobic |
| C27 | CZ | TYR- 82 | 4.45 | 0 | Hydrophobic |
| C42 | CE1 | TYR- 82 | 3.73 | 0 | Hydrophobic |
| O45 | OH | TYR- 82 | 2.7 | 156.35 | H-Bond (Protein Donor) |
| C20 | CB | HIS- 87 | 4.03 | 0 | Hydrophobic |
| C11 | CG2 | ILE- 90 | 4.43 | 0 | Hydrophobic |
| C12 | CD1 | ILE- 90 | 4.21 | 0 | Hydrophobic |
| C19 | CD1 | ILE- 90 | 4.08 | 0 | Hydrophobic |
| C20 | CD1 | ILE- 90 | 4.1 | 0 | Hydrophobic |
| C46 | CG2 | ILE- 90 | 4.46 | 0 | Hydrophobic |
| C46 | CD1 | ILE- 91 | 4.25 | 0 | Hydrophobic |
| C3 | CE2 | PHE- 99 | 4.17 | 0 | Hydrophobic |
| C16 | CE2 | PHE- 99 | 3.64 | 0 | Hydrophobic |
