2.220 Å
X-ray
2013-02-20
Name: | Muconolactone Delta-isomerase |
---|---|
ID: | Q8G9L0_RHOOP |
AC: | Q8G9L0 |
Organism: | Rhodococcus opacus |
Reign: | Bacteria |
TaxID: | 37919 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
H | 14 % |
J | 86 % |
B-Factor: | 33.428 |
---|---|
Number of residues: | 26 |
Including | |
Standard Amino Acids: | 24 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | CL |
Ligandability | Volume (Å3) |
---|---|
0.878 | 394.875 |
% Hydrophobic | % Polar |
---|---|
68.38 | 31.62 |
According to VolSite |
HET Code: | K6H |
---|---|
Formula: | C6H4ClO4 |
Molecular weight: | 175.547 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 69.48 % |
Polar Surface area: | 66.43 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 4 |
H-Bond Donors: | 0 |
Rings: | 1 |
Aromatic rings: | 0 |
Anionic atoms: | 1 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
41.6351 | 45.8944 | 37.7455 |
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 |
CLAD | CB | MET- 7 | 4.36 | 0 | Hydrophobic |
CLAD | CG2 | VAL- 9 | 3.56 | 0 | Hydrophobic |
CAK | CB | ALA- 27 | 4.07 | 0 | Hydrophobic |
OAC | CZ | ARG- 45 | 3.87 | 0 | Ionic (Protein Cationic) |
OAC | NH1 | ARG- 45 | 3.02 | 152.08 | H-Bond (Protein Donor) |
OAA | ND2 | ASN- 52 | 2.9 | 166.34 | H-Bond (Protein Donor) |
CLAD | CD2 | PHE- 73 | 4.34 | 0 | Hydrophobic |
CAK | CD2 | PHE- 73 | 3.42 | 0 | Hydrophobic |
CLAD | CD2 | LEU- 77 | 3.88 | 0 | Hydrophobic |
OAA | NE2 | HIS- 87 | 2.91 | 153.17 | H-Bond (Protein Donor) |
OAC | NE2 | HIS- 87 | 3.48 | 135.77 | H-Bond (Protein Donor) |