sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.400 Å
X-ray
2011-11-01
| Name: | Acetylserotonin O-methyltransferase |
|---|---|
| ID: | ASMT_HUMAN |
| AC: | P46597 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 2.1.1.4 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 76.529 |
|---|---|
| Number of residues: | 34 |
| Including | |
| Standard Amino Acids: | 33 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.772 | 634.500 |
| % Hydrophobic | % Polar |
|---|---|
| 54.26 | 45.74 |
| According to VolSite | |
| HET Code: | SAM |
|---|---|
| Formula: | C15H23N6O5S |
| Molecular weight: | 399.445 g/mol |
| DrugBank ID: | DB00118 |
| Buried Surface Area: | 75.94 % |
| Polar Surface area: | 189.77 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 9 |
| H-Bond Donors: | 4 |
| Rings: | 3 |
| Aromatic rings: | 2 |
| Anionic atoms: | 1 |
| Cationic atoms: | 2 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 7 |
| X | Y | Z |
|---|---|---|
| -2.41159 | 23.5407 | 40.1533 |
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 |
| CE | CZ | PHE- 143 | 4.22 | 0 | Hydrophobic |
| C5' | CZ | PHE- 143 | 3.76 | 0 | Hydrophobic |
| C2' | CE1 | PHE- 143 | 3.79 | 0 | Hydrophobic |
| C2' | CZ | TYR- 147 | 4.2 | 0 | Hydrophobic |
| O2' | OH | TYR- 147 | 2.72 | 171.2 | H-Bond (Protein Donor) |
| SD | CE2 | PHE- 156 | 4.09 | 0 | Hydrophobic |
| CE | CZ | PHE- 156 | 4.13 | 0 | Hydrophobic |
| CG | CD2 | LEU- 160 | 3.72 | 0 | Hydrophobic |
| CE | CD2 | LEU- 160 | 3.56 | 0 | Hydrophobic |
| O | NE1 | TRP- 164 | 3.27 | 134.38 | H-Bond (Protein Donor) |
| OXT | NE1 | TRP- 164 | 2.81 | 168.18 | H-Bond (Protein Donor) |
| N | O | GLY- 187 | 2.8 | 164.81 | H-Bond (Ligand Donor) |
| O3' | OD2 | ASP- 210 | 2.82 | 166.84 | H-Bond (Ligand Donor) |
| O2' | OD1 | ASP- 210 | 2.63 | 166.95 | H-Bond (Ligand Donor) |
| N6 | OD1 | ASP- 236 | 2.6 | 169.7 | H-Bond (Ligand Donor) |
| N1 | N | PHE- 237 | 2.9 | 164.66 | H-Bond (Protein Donor) |
| DuAr | DuAr | PHE- 237 | 3.53 | 0 | Aromatic Face/Face |
| N | O | ALA- 251 | 2.79 | 159.74 | H-Bond (Ligand Donor) |
| O | NH1 | ARG- 252 | 3.15 | 159.02 | H-Bond (Protein Donor) |
| CG | CB | ARG- 252 | 4.03 | 0 | Hydrophobic |
| CE | CB | ARG- 252 | 4.29 | 0 | Hydrophobic |
| C5' | CG2 | VAL- 253 | 4.36 | 0 | Hydrophobic |
