2.300 Å
X-ray
2012-08-24
Name: | Acetylcholinesterase |
---|---|
ID: | ACES_MOUSE |
AC: | P21836 |
Organism: | Mus musculus |
Reign: | Eukaryota |
TaxID: | 10090 |
EC Number: | 3.1.1.7 |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 40.252 |
---|---|
Number of residues: | 31 |
Including | |
Standard Amino Acids: | 29 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.170 | 563.625 |
% Hydrophobic | % Polar |
---|---|
53.89 | 46.11 |
According to VolSite |
HET Code: | Q4Q |
---|---|
Formula: | C14H25N2O2S |
Molecular weight: | 285.425 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 64.84 % |
Polar Surface area: | 58.99 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 2 |
H-Bond Donors: | 2 |
Rings: | 1 |
Aromatic rings: | 1 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
7.60289 | -4.73737 | -36.7655 |
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 |
C08 | CE2 | TYR- 72 | 4.3 | 0 | Hydrophobic |
C6 | CZ3 | TRP- 86 | 4.2 | 0 | Hydrophobic |
C14 | CE2 | TRP- 86 | 3.77 | 0 | Hydrophobic |
N1 | OH | TYR- 124 | 3.15 | 175.96 | H-Bond (Ligand Donor) |
C6 | CB | SER- 203 | 4.41 | 0 | Hydrophobic |
C08 | CZ2 | TRP- 286 | 3.89 | 0 | Hydrophobic |
C4 | CE1 | TYR- 337 | 3.62 | 0 | Hydrophobic |
C11 | CE1 | TYR- 337 | 4.14 | 0 | Hydrophobic |
C14 | CE2 | TYR- 337 | 3.64 | 0 | Hydrophobic |
C4 | CE2 | PHE- 338 | 3.47 | 0 | Hydrophobic |
C08 | CD1 | TYR- 341 | 3.84 | 0 | Hydrophobic |
C8 | CE1 | TYR- 341 | 3.38 | 0 | Hydrophobic |