2.480 Å
X-ray
2012-11-26
Min | Mean | Median | Standard Deviation | Max | Count | |
---|---|---|---|---|---|---|
pChEMBL: | 7.100 | 7.100 | 7.100 | 0.000 | 7.100 | 2 |
Name: | Acetylcholine-binding protein |
---|---|
ID: | ACHP_LYMST |
AC: | P58154 |
Organism: | Lymnaea stagnalis |
Reign: | Eukaryota |
TaxID: | 6523 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
Q | 55 % |
R | 45 % |
B-Factor: | 19.155 |
---|---|
Number of residues: | 23 |
Including | |
Standard Amino Acids: | 21 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.027 | 489.375 |
% Hydrophobic | % Polar |
---|---|
53.10 | 46.90 |
According to VolSite |
HET Code: | XRX |
---|---|
Formula: | C9H21N2O2 |
Molecular weight: | 189.275 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 81.57 % |
Polar Surface area: | 33.98 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 2 |
H-Bond Donors: | 1 |
Rings: | 0 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 5 |
X | Y | Z |
---|---|---|
-56.4718 | -30.6022 | 79.7786 |
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 |
C11 | CH2 | TRP- 53 | 3.97 | 0 | Hydrophobic |
C11 | CE2 | TYR- 89 | 3.47 | 0 | Hydrophobic |
C2 | CB | MET- 114 | 3.99 | 0 | Hydrophobic |
C8 | SD | MET- 114 | 4.09 | 0 | Hydrophobic |
N1 | O | TRP- 143 | 2.93 | 134.12 | H-Bond (Ligand Donor) |
C2 | CE2 | TRP- 143 | 3.34 | 0 | Hydrophobic |
C8 | CZ2 | TRP- 143 | 3.7 | 0 | Hydrophobic |
C11 | CZ3 | TRP- 143 | 3.95 | 0 | Hydrophobic |
C11 | CD2 | TYR- 185 | 4.23 | 0 | Hydrophobic |
O6 | O | HOH- 2090 | 2.94 | 161.31 | H-Bond (Protein Donor) |