1.900 Å
X-ray
2001-03-19
Name: | Glutamate mutase epsilon subunit |
---|---|
ID: | GLME_CLOCO |
AC: | P80077 |
Organism: | Clostridium cochlearium |
Reign: | Bacteria |
TaxID: | 1494 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 4 % |
B | 96 % |
B-Factor: | 7.762 |
---|---|
Number of residues: | 26 |
Including | |
Standard Amino Acids: | 25 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.424 | 2136.375 |
% Hydrophobic | % Polar |
---|---|
47.55 | 52.45 |
According to VolSite |
HET Code: | 5AD |
---|---|
Formula: | C10H13N5O3 |
Molecular weight: | 251.242 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 59.1 % |
Polar Surface area: | 119.31 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 1 |
X | Y | Z |
---|---|---|
6.84189 | -2.891 | 85.0499 |
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 |
C1' | CD | ARG- 66 | 3.29 | 0 | Hydrophobic |
C4' | CD | ARG- 66 | 3.79 | 0 | Hydrophobic |
N6 | O | GLY- 68 | 3.18 | 160.06 | H-Bond (Ligand Donor) |
N6 | O | ASN- 123 | 2.7 | 150.14 | H-Bond (Ligand Donor) |
C5' | CE | MET- 294 | 4.18 | 0 | Hydrophobic |
O2' | OE2 | GLU- 330 | 3.3 | 148.28 | H-Bond (Ligand Donor) |
O3' | OE2 | GLU- 330 | 2.71 | 151.33 | H-Bond (Ligand Donor) |
C5' | CG | GLU- 1305 | 3.29 | 0 | Hydrophobic |