2.690 Å
X-ray
2012-05-05
Name: | Interleukin enhancer-binding factor 2 |
---|---|
ID: | ILF2_MOUSE |
AC: | Q9CXY6 |
Organism: | Mus musculus |
Reign: | Eukaryota |
TaxID: | 10090 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 23.059 |
---|---|
Number of residues: | 28 |
Including | |
Standard Amino Acids: | 27 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.637 | 762.750 |
% Hydrophobic | % Polar |
---|---|
52.65 | 47.35 |
According to VolSite |
HET Code: | ATP |
---|---|
Formula: | C10H12N5O13P3 |
Molecular weight: | 503.149 g/mol |
DrugBank ID: | DB00171 |
Buried Surface Area: | 43.87 % |
Polar Surface area: | 319.88 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
4.75119 | 0.260677 | -66.0367 |
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 |
O1B | N | SER- 107 | 2.97 | 164.16 | H-Bond (Protein Donor) |
O2B | NZ | LYS- 110 | 3.93 | 0 | Ionic (Protein Cationic) |
O3' | NZ | LYS- 110 | 3.05 | 138.68 | H-Bond (Protein Donor) |
C4' | CB | ALA- 204 | 3.98 | 0 | Hydrophobic |
O2' | ND1 | HIS- 207 | 2.74 | 162.36 | H-Bond (Protein Donor) |
O1G | NZ | LYS- 228 | 3.73 | 0 | Ionic (Protein Cationic) |
O2G | NZ | LYS- 228 | 3.19 | 0 | Ionic (Protein Cationic) |
O3G | MG | MG- 1361 | 2.21 | 0 | Metal Acceptor |
O1B | MG | MG- 1361 | 2.58 | 0 | Metal Acceptor |
O1A | MG | MG- 1361 | 2.64 | 0 | Metal Acceptor |