2.300 Å
X-ray
2010-06-28
Name: | Acetylcholinesterase |
---|---|
ID: | ACES_TETCF |
AC: | P04058 |
Organism: | Tetronarce californica |
Reign: | Eukaryota |
TaxID: | 7787 |
EC Number: | 3.1.1.7 |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 35.749 |
---|---|
Number of residues: | 21 |
Including | |
Standard Amino Acids: | 20 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.178 | 654.750 |
% Hydrophobic | % Polar |
---|---|
53.61 | 46.39 |
According to VolSite |
HET Code: | AFT |
---|---|
Formula: | C17H12O6 |
Molecular weight: | 312.274 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 61.33 % |
Polar Surface area: | 71.06 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 6 |
H-Bond Donors: | 0 |
Rings: | 5 |
Aromatic rings: | 1 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 1 |
X | Y | Z |
---|---|---|
83.0148 | 55.5495 | 79.6963 |
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 |
C6A | CE1 | TYR- 70 | 3.82 | 0 | Hydrophobic |
C9A | CZ | TYR- 121 | 3.91 | 0 | Hydrophobic |
CM | CD2 | TRP- 279 | 3.83 | 0 | Hydrophobic |
C9A | CH2 | TRP- 279 | 4.47 | 0 | Hydrophobic |
C3 | CE3 | TRP- 279 | 3.73 | 0 | Hydrophobic |
C2A | CD1 | LEU- 282 | 3.93 | 0 | Hydrophobic |
O1 | OG | SER- 286 | 2.92 | 162.59 | H-Bond (Protein Donor) |
O11 | N | ARG- 289 | 3.32 | 137.52 | H-Bond (Protein Donor) |
O1 | N | ARG- 289 | 3.23 | 146.75 | H-Bond (Protein Donor) |
C6A | CD2 | TYR- 334 | 4.41 | 0 | Hydrophobic |