2.500 Å
X-ray
2007-10-30
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 |
---|---|
A | 100 % |
B-Factor: | 21.836 |
---|---|
Number of residues: | 27 |
Including | |
Standard Amino Acids: | 25 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.145 | 992.250 |
% Hydrophobic | % Polar |
---|---|
48.30 | 51.70 |
According to VolSite |
HET Code: | CNI |
---|---|
Formula: | C9H2N4O4 |
Molecular weight: | 230.137 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 69.81 % |
Polar Surface area: | 128.46 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 0 |
Rings: | 2 |
Aromatic rings: | 0 |
Anionic atoms: | 1 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 1 |
X | Y | Z |
---|---|---|
-30.2131 | 14.4711 | -39.1787 |
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 |
C4 | CZ | TYR- 61 | 3.4 | 0 | Hydrophobic |
C6 | CB | PRO- 89 | 4.34 | 0 | Hydrophobic |
N2 | O | PRO- 89 | 2.84 | 164.99 | H-Bond (Ligand Donor) |
O2 | N | THR- 91 | 2.88 | 176.34 | H-Bond (Protein Donor) |
O1 | NH2 | ARG- 96 | 2.99 | 160.16 | H-Bond (Protein Donor) |
O2 | NH2 | ARG- 96 | 3.45 | 123.89 | H-Bond (Protein Donor) |
O2 | NH1 | ARG- 96 | 2.79 | 143.54 | H-Bond (Protein Donor) |
O3 | OG1 | THR- 174 | 3.46 | 124.61 | H-Bond (Protein Donor) |
C5 | CG | GLU- 193 | 4.36 | 0 | Hydrophobic |
C8 | CG | GLU- 193 | 4.21 | 0 | Hydrophobic |