2.300 Å
X-ray
2011-09-24
Name: | Dihydropteroate synthase |
---|---|
ID: | Q81VW8_BACAN |
AC: | Q81VW8 |
Organism: | Bacillus anthracis |
Reign: | Bacteria |
TaxID: | 1392 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 76.692 |
---|---|
Number of residues: | 23 |
Including | |
Standard Amino Acids: | 22 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.048 | 556.875 |
% Hydrophobic | % Polar |
---|---|
32.73 | 67.27 |
According to VolSite |
HET Code: | XHP |
---|---|
Formula: | C7H7N5O |
Molecular weight: | 177.163 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 61.83 % |
Polar Surface area: | 92.19 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 2 |
Rings: | 2 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 0 |
X | Y | Z |
---|---|---|
-62.8732 | 59.3224 | 137.164 |
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 |
N1 | ND2 | ASN- 120 | 3.2 | 149.9 | H-Bond (Protein Donor) |
N2 | OD1 | ASN- 120 | 2.84 | 170.4 | H-Bond (Ligand Donor) |
N2 | OD1 | ASP- 184 | 2.89 | 144.42 | H-Bond (Ligand Donor) |
N3 | OD1 | ASP- 184 | 2.89 | 143.88 | H-Bond (Ligand Donor) |
C6A | CZ | PHE- 189 | 3.85 | 0 | Hydrophobic |
O4 | NZ | LYS- 220 | 2.69 | 153.62 | H-Bond (Protein Donor) |
DuAr | CZ | ARG- 254 | 3.58 | 168.11 | Pi/Cation |
O4 | O | HOH- 294 | 3.14 | 179.96 | H-Bond (Protein Donor) |