sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
Å
NMR
2014-03-07
| Name: | Gastrotropin |
|---|---|
| ID: | FABP6_HUMAN |
| AC: | P51161 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 0.569 |
|---|---|
| Number of residues: | 45 |
| Including | |
| Standard Amino Acids: | 44 |
| Non Standard Amino Acids: | 1 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.542 | 273.375 |
| % Hydrophobic | % Polar |
|---|---|
| 56.79 | 43.21 |
| According to VolSite | |
| HET Code: | GCH |
|---|---|
| Formula: | C26H42NO6 |
| Molecular weight: | 464.615 g/mol |
| DrugBank ID: | DB02691 |
| Buried Surface Area: | 84.3 % |
| Polar Surface area: | 129.92 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 6 |
| H-Bond Donors: | 4 |
| Rings: | 4 |
| Aromatic rings: | 0 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| -28.3006 | 24.4435 | 11.3343 |
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 |
| C | CG | PHE- 2 | 3.44 | 0 | Hydrophobic |
| C2 | CD1 | PHE- 2 | 3.94 | 0 | Hydrophobic |
| C4 | CB | PHE- 2 | 3.91 | 0 | Hydrophobic |
| C6 | CE2 | PHE- 6 | 3.86 | 0 | Hydrophobic |
| C23 | CB | PHE- 6 | 3.65 | 0 | Hydrophobic |
| C16 | CB | MET- 8 | 4.1 | 0 | Hydrophobic |
| C19 | CB | MET- 8 | 3.94 | 0 | Hydrophobic |
| C21 | SD | MET- 8 | 4.13 | 0 | Hydrophobic |
| C21 | CB | ILE- 36 | 4.32 | 0 | Hydrophobic |
| C20 | CB | ILE- 36 | 3.81 | 0 | Hydrophobic |
| C19 | CB | THR- 38 | 3.87 | 0 | Hydrophobic |
| C23 | CG2 | THR- 38 | 3.37 | 0 | Hydrophobic |
| C5 | CG1 | VAL- 40 | 4.24 | 0 | Hydrophobic |
| C11 | CG2 | VAL- 40 | 3.99 | 0 | Hydrophobic |
| C4 | CG2 | VAL- 40 | 3.62 | 0 | Hydrophobic |
| C5 | CE1 | PHE- 47 | 3.5 | 0 | Hydrophobic |
| C10 | CZ3 | TRP- 49 | 3.86 | 0 | Hydrophobic |
| C11 | CE3 | TRP- 49 | 3.63 | 0 | Hydrophobic |
| C12 | CZ3 | TRP- 49 | 4.26 | 0 | Hydrophobic |
| C5 | CE3 | TRP- 49 | 3.79 | 0 | Hydrophobic |
| C20 | CG | GLN- 51 | 4.11 | 0 | Hydrophobic |
| O3 | NE2 | GLN- 51 | 3.14 | 147.6 | H-Bond (Protein Donor) |
| C21 | CE | MET- 74 | 3.86 | 0 | Hydrophobic |
| O1 | OG | SER- 101 | 2.84 | 163.56 | H-Bond (Protein Donor) |
| C1 | CB | SER- 101 | 3.47 | 0 | Hydrophobic |
| C6 | CD1 | LEU- 108 | 3.71 | 0 | Hydrophobic |
| C7 | CD1 | LEU- 108 | 3.95 | 0 | Hydrophobic |
| C9 | CB | LEU- 108 | 4.42 | 0 | Hydrophobic |
| C8 | CB | GLU- 110 | 3.93 | 0 | Hydrophobic |
| O1 | OE1 | GLU- 110 | 2.69 | 126.12 | H-Bond (Ligand Donor) |
| C21 | CD | ARG- 121 | 4.08 | 0 | Hydrophobic |
| C16 | CD | ARG- 121 | 3.35 | 0 | Hydrophobic |
| O5 | NH2 | ARG- 121 | 2.66 | 129.24 | H-Bond (Protein Donor) |
| O5 | CZ | ARG- 121 | 3.3 | 0 | Ionic (Protein Cationic) |
| C23 | CB | SER- 123 | 4.06 | 0 | Hydrophobic |
| C16 | CB | SER- 123 | 3.64 | 0 | Hydrophobic |
