2.250 Å
X-ray
2000-09-27
Name: | Penicillin G acylase |
---|---|
ID: | PAC_ECOLX |
AC: | P06875 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 562 |
EC Number: | 3.5.1.11 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 23 % |
B | 77 % |
B-Factor: | 13.326 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.023 | 482.625 |
% Hydrophobic | % Polar |
---|---|
49.65 | 50.35 |
According to VolSite |
HET Code: | PNN |
---|---|
Formula: | C16H17N2O4S |
Molecular weight: | 333.382 g/mol |
DrugBank ID: | DB01053 |
Buried Surface Area: | 46.69 % |
Polar Surface area: | 114.84 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 1 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 1 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 4 |
X | Y | Z |
---|---|---|
-0.00386957 | -0.132087 | -1.75704 |
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 |
O16 | N | SER- 1 | 2.81 | 141.12 | H-Bond (Protein Donor) |
C17 | CB | SER- 1 | 3.3 | 0 | Hydrophobic |
C22 | CB | SER- 67 | 4.49 | 0 | Hydrophobic |
S1 | CB | ALA- 69 | 3.87 | 0 | Hydrophobic |
C19 | CB | ALA- 69 | 3.45 | 0 | Hydrophobic |
S1 | CZ | PHE- 71 | 3.22 | 0 | Hydrophobic |
C20 | SD | MET- 142 | 3.58 | 0 | Hydrophobic |
C21 | CE | MET- 142 | 3.41 | 0 | Hydrophobic |
C10 | CD1 | PHE- 146 | 3.21 | 0 | Hydrophobic |
C20 | CB | PHE- 146 | 3.74 | 0 | Hydrophobic |
C21 | CD1 | ILE- 177 | 4.41 | 0 | Hydrophobic |