2.090 Å
X-ray
2013-03-27
Name: | Camphor 5-monooxygenase |
---|---|
ID: | CPXA_PSEPU |
AC: | P00183 |
Organism: | Pseudomonas putida |
Reign: | Bacteria |
TaxID: | 303 |
EC Number: | 1.14.15.1 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 16.741 |
---|---|
Number of residues: | 20 |
Including | |
Standard Amino Acids: | 17 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.874 | 1748.250 |
% Hydrophobic | % Polar |
---|---|
54.83 | 45.17 |
According to VolSite |
HET Code: | CAH |
---|---|
Formula: | C10H16O2 |
Molecular weight: | 168.233 g/mol |
DrugBank ID: | DB02817 |
Buried Surface Area: | 64.86 % |
Polar Surface area: | 37.29 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 2 |
H-Bond Donors: | 1 |
Rings: | 2 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 0 |
X | Y | Z |
---|---|---|
-81.4023 | 5.88325 | 0.769833 |
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 |
C3 | CZ | PHE- 87 | 4.04 | 0 | Hydrophobic |
C8 | CE1 | PHE- 87 | 4.28 | 0 | Hydrophobic |
O2 | OH | TYR- 96 | 3.48 | 135.89 | H-Bond (Protein Donor) |
C3 | CZ | TYR- 96 | 4.44 | 0 | Hydrophobic |
C3 | CG2 | THR- 101 | 4.39 | 0 | Hydrophobic |
C5 | CD1 | LEU- 244 | 4.09 | 0 | Hydrophobic |
C9 | CG2 | THR- 252 | 4.33 | 0 | Hydrophobic |
C8 | CG1 | VAL- 295 | 4.06 | 0 | Hydrophobic |
C9 | CG1 | VAL- 295 | 3.98 | 0 | Hydrophobic |
C8 | CB | ASP- 297 | 4.34 | 0 | Hydrophobic |
C8 | CG2 | ILE- 395 | 4.21 | 0 | Hydrophobic |
C10 | CG2 | ILE- 395 | 4.26 | 0 | Hydrophobic |