1.800 Å
X-ray
2000-09-12
Name: | Glutamate receptor 2 |
---|---|
ID: | GRIA2_RAT |
AC: | P19491 |
Organism: | Rattus norvegicus |
Reign: | Eukaryota |
TaxID: | 10116 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 10.699 |
---|---|
Number of residues: | 21 |
Including | |
Standard Amino Acids: | 21 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.422 | 718.875 |
% Hydrophobic | % Polar |
---|---|
41.31 | 58.69 |
According to VolSite |
HET Code: | DNQ |
---|---|
Formula: | C8H2N4O6 |
Molecular weight: | 250.125 g/mol |
DrugBank ID: | DB03759 |
Buried Surface Area: | 70.9 % |
Polar Surface area: | 150.49 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 8 |
H-Bond Donors: | 0 |
Rings: | 2 |
Aromatic rings: | 0 |
Anionic atoms: | 2 |
Cationic atoms: | 2 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
28.9009 | 5.64156 | 39.0357 |
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 |
N1 | O | PRO- 89 | 2.65 | 163.6 | H-Bond (Ligand Donor) |
C5 | CB | PRO- 89 | 4.2 | 0 | Hydrophobic |
O1 | N | THR- 91 | 3.02 | 161.57 | H-Bond (Protein Donor) |
O1 | NH1 | ARG- 96 | 2.71 | 139.53 | H-Bond (Protein Donor) |
O1 | NH2 | ARG- 96 | 3.34 | 121.81 | H-Bond (Protein Donor) |
O2 | NH2 | ARG- 96 | 2.92 | 156.57 | H-Bond (Protein Donor) |