1.800 Å
X-ray
2007-09-18
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: | 15.306 |
---|---|
Number of residues: | 20 |
Including | |
Standard Amino Acids: | 19 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.817 | 850.500 |
% Hydrophobic | % Polar |
---|---|
65.87 | 34.13 |
According to VolSite |
HET Code: | CAM |
---|---|
Formula: | C10H16O |
Molecular weight: | 152.233 g/mol |
DrugBank ID: | DB01744 |
Buried Surface Area: | 56.05 % |
Polar Surface area: | 17.07 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 1 |
H-Bond Donors: | 0 |
Rings: | 2 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 0 |
X | Y | Z |
---|---|---|
-15.0473 | -9.79718 | 7.30373 |
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 |
C8 | CZ | PHE- 87 | 4.25 | 0 | Hydrophobic |
O | OH | TYR- 96 | 2.85 | 141.99 | H-Bond (Protein Donor) |
C3 | CG2 | THR- 101 | 3.64 | 0 | Hydrophobic |
C10 | CG2 | THR- 185 | 4.35 | 0 | Hydrophobic |
C3 | CG | LEU- 244 | 4.27 | 0 | Hydrophobic |
C5 | CD1 | LEU- 244 | 3.53 | 0 | Hydrophobic |
C6 | CG1 | VAL- 247 | 3.45 | 0 | Hydrophobic |
C6 | CG2 | THR- 252 | 4.14 | 0 | Hydrophobic |
C9 | CG2 | THR- 252 | 4.02 | 0 | Hydrophobic |
C8 | CG1 | VAL- 295 | 3.99 | 0 | Hydrophobic |
C9 | CG2 | VAL- 295 | 3.88 | 0 | Hydrophobic |
C10 | CG2 | ILE- 395 | 4.5 | 0 | Hydrophobic |
C10 | CG2 | VAL- 396 | 3.9 | 0 | Hydrophobic |