2.050 Å
X-ray
2015-08-21
Name: | Uric acid degradation bifunctional protein |
---|---|
ID: | PUCL_BACSB |
AC: | Q45697 |
Organism: | Bacillus sp. |
Reign: | Bacteria |
TaxID: | 36824 |
EC Number: | 1.7.3.3 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 58 % |
B | 42 % |
B-Factor: | 26.356 |
---|---|
Number of residues: | 27 |
Including | |
Standard Amino Acids: | 24 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.112 | 654.750 |
% Hydrophobic | % Polar |
---|---|
34.02 | 65.98 |
According to VolSite |
HET Code: | MUA |
---|---|
Formula: | C6H6N4O3 |
Molecular weight: | 182.137 g/mol |
DrugBank ID: | DB03293 |
Buried Surface Area: | 76.79 % |
Polar Surface area: | 90.54 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 3 |
H-Bond Donors: | 3 |
Rings: | 2 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 0 |
X | Y | Z |
---|---|---|
14.5764 | 28.2961 | 68.9665 |
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 |
N7 | N | THR- 73 | 3.07 | 166.02 | H-Bond (Protein Donor) |
N7 | OG1 | THR- 73 | 3.13 | 127.1 | H-Bond (Protein Donor) |
O8 | OG1 | THR- 73 | 3.26 | 163.96 | H-Bond (Protein Donor) |
O8 | N | ASP- 74 | 3.07 | 154.02 | H-Bond (Protein Donor) |
C10 | CD2 | PHE- 184 | 3.84 | 0 | Hydrophobic |
C10 | CD2 | LEU- 195 | 3.69 | 0 | Hydrophobic |
O2 | NH2 | ARG- 201 | 2.67 | 156.45 | H-Bond (Protein Donor) |
O2 | N | ILE- 249 | 2.6 | 153.73 | H-Bond (Protein Donor) |
N1 | OE1 | GLN- 250 | 2.84 | 179.3 | H-Bond (Ligand Donor) |
O6 | NE2 | GLN- 250 | 2.94 | 161.06 | H-Bond (Protein Donor) |