1.440 Å
X-ray
2012-01-19
Name: | Beta-lactamase |
---|---|
ID: | Q9L5C8_ECOLX |
AC: | Q9L5C8 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 562 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 8.279 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 24 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 4 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.411 | 313.875 |
% Hydrophobic | % Polar |
---|---|
32.26 | 67.74 |
According to VolSite |
HET Code: | DN8 |
---|---|
Formula: | C14H9BrN5O |
Molecular weight: | 343.158 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 59.45 % |
Polar Surface area: | 81.87 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 1 |
Rings: | 3 |
Aromatic rings: | 3 |
Anionic atoms: | 1 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 3 |
X | Y | Z |
---|---|---|
-6.73876 | 55.3445 | 11.9938 |
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 |
O21 | ND2 | ASN- 104 | 3.04 | 168.44 | H-Bond (Protein Donor) |
C13 | CB | TYR- 105 | 3.83 | 0 | Hydrophobic |
C12 | CB | SER- 130 | 3.88 | 0 | Hydrophobic |
O21 | ND2 | ASN- 132 | 3.11 | 136.69 | H-Bond (Protein Donor) |
C5 | CB | PRO- 167 | 4.18 | 0 | Hydrophobic |
C5 | CB | ASN- 170 | 3.54 | 0 | Hydrophobic |
BR1 | CG2 | THR- 171 | 3.91 | 0 | Hydrophobic |
N18 | OG1 | THR- 235 | 3.42 | 149.44 | H-Bond (Protein Donor) |
N17 | OG1 | THR- 235 | 2.67 | 173.98 | H-Bond (Protein Donor) |
N19 | OG | SER- 237 | 2.8 | 175.74 | H-Bond (Protein Donor) |
C1 | CB | ASP- 240 | 4.25 | 0 | Hydrophobic |