2.250 Å
X-ray
2012-02-18
Name: | Uncharacterized protein |
---|---|
ID: | Q4E1W2_TRYCC |
AC: | Q4E1W2 |
Organism: | Trypanosoma cruzi |
Reign: | Eukaryota |
TaxID: | 353153 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 24.489 |
---|---|
Number of residues: | 65 |
Including | |
Standard Amino Acids: | 59 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 5 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.200 | 1211.625 |
% Hydrophobic | % Polar |
---|---|
41.50 | 58.50 |
According to VolSite |
HET Code: | FAD |
---|---|
Formula: | C27H31N9O15P2 |
Molecular weight: | 783.534 g/mol |
DrugBank ID: | DB03147 |
Buried Surface Area: | 68.83 % |
Polar Surface area: | 381.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 22 |
H-Bond Donors: | 7 |
Rings: | 6 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
70.009 | -15.7632 | -28.8423 |
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' | CG | PRO- 16 | 3.79 | 0 | Hydrophobic |
O1P | OG1 | THR- 17 | 2.59 | 166.18 | H-Bond (Protein Donor) |
O2P | N | THR- 17 | 3.17 | 150.73 | H-Bond (Protein Donor) |
O3B | OE1 | GLU- 37 | 2.66 | 161.97 | H-Bond (Ligand Donor) |
O3B | OE2 | GLU- 37 | 3.23 | 128.5 | H-Bond (Ligand Donor) |
O2B | OE2 | GLU- 37 | 2.65 | 158.21 | H-Bond (Ligand Donor) |
O2A | N | LEU- 45 | 3.02 | 166.47 | H-Bond (Protein Donor) |
C2' | CB | LEU- 45 | 4.48 | 0 | Hydrophobic |
O4' | OG | SER- 46 | 3.1 | 152.8 | H-Bond (Protein Donor) |
DuAr | DuAr | HIS- 62 | 3.92 | 0 | Aromatic Face/Face |
N3 | O | VAL- 63 | 2.78 | 150.85 | H-Bond (Ligand Donor) |
O4 | N | VAL- 63 | 2.86 | 163.67 | H-Bond (Protein Donor) |
N6A | O | ALA- 236 | 2.99 | 162.19 | H-Bond (Ligand Donor) |
N1A | N | ALA- 236 | 2.9 | 157.74 | H-Bond (Protein Donor) |
C7M | CG2 | THR- 295 | 3.93 | 0 | Hydrophobic |
C7M | CE2 | TYR- 395 | 4.38 | 0 | Hydrophobic |
C1' | CD | ARG- 423 | 4.27 | 0 | Hydrophobic |
C3' | CD | ARG- 423 | 3.93 | 0 | Hydrophobic |
C5' | CB | ARG- 423 | 3.78 | 0 | Hydrophobic |
O1P | N | ARG- 423 | 2.91 | 150.69 | H-Bond (Protein Donor) |
O3' | O | GLY- 432 | 2.63 | 163.23 | H-Bond (Ligand Donor) |
N1 | N | GLN- 434 | 3.36 | 130.33 | H-Bond (Protein Donor) |
O2 | N | GLN- 434 | 2.76 | 164.96 | H-Bond (Protein Donor) |
C2' | CG | GLN- 434 | 4 | 0 | Hydrophobic |
O3' | OG | SER- 437 | 3.22 | 156.26 | H-Bond (Protein Donor) |
C5' | CB | SER- 437 | 3.88 | 0 | Hydrophobic |
O3B | O | HOH- 603 | 2.94 | 135.87 | H-Bond (Protein Donor) |
O2P | O | HOH- 620 | 2.75 | 179.98 | H-Bond (Protein Donor) |
O1P | O | HOH- 622 | 2.84 | 179.96 | H-Bond (Protein Donor) |