3.000 Å
X-ray
2006-02-11
Name: | Long-chain N-acyl amino acid synthase |
---|---|
ID: | Q8KNZ7_9BACT |
AC: | Q8KNZ7 |
Organism: | uncultured bacterium CSLC2 |
Reign: | Bacteria |
TaxID: | 1091571 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
E | 97 % |
F | 3 % |
B-Factor: | 40.370 |
---|---|
Number of residues: | 39 |
Including | |
Standard Amino Acids: | 39 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.575 | 651.375 |
% Hydrophobic | % Polar |
---|---|
66.84 | 33.16 |
According to VolSite |
HET Code: | NLT |
---|---|
Formula: | C21H32NO4 |
Molecular weight: | 362.483 g/mol |
DrugBank ID: | DB08275 |
Buried Surface Area: | 72.52 % |
Polar Surface area: | 89.46 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 4 |
H-Bond Donors: | 2 |
Rings: | 1 |
Aromatic rings: | 1 |
Anionic atoms: | 1 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 14 |
X | Y | Z |
---|---|---|
41.6765 | 97.054 | 29.8917 |
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 |
O2 | OH | TYR- 27 | 2.83 | 164.73 | H-Bond (Protein Donor) |
C5 | CD1 | ILE- 62 | 3.85 | 0 | Hydrophobic |
C7 | CG1 | VAL- 95 | 3.69 | 0 | Hydrophobic |
O | N | GLN- 97 | 3.31 | 156.71 | H-Bond (Protein Donor) |
OL | N | PHE- 98 | 3.25 | 141.71 | H-Bond (Protein Donor) |
C4 | CB | PHE- 98 | 3.78 | 0 | Hydrophobic |
C11 | CE2 | PHE- 116 | 3.93 | 0 | Hydrophobic |
C6 | CE2 | PHE- 122 | 3.85 | 0 | Hydrophobic |
C11 | CB | PHE- 122 | 4.33 | 0 | Hydrophobic |
C8 | CD2 | PHE- 122 | 3.69 | 0 | Hydrophobic |
C9 | CG1 | VAL- 125 | 4.16 | 0 | Hydrophobic |
C11 | CB | LEU- 126 | 4.41 | 0 | Hydrophobic |
C10 | CD2 | LEU- 137 | 4.21 | 0 | Hydrophobic |
C6 | CD1 | ILE- 139 | 3.71 | 0 | Hydrophobic |
C7 | CD1 | ILE- 139 | 3.7 | 0 | Hydrophobic |
N | O | SER- 140 | 3.07 | 144.78 | H-Bond (Ligand Donor) |
C2 | CG2 | ILE- 141 | 3.69 | 0 | Hydrophobic |
OH | ND2 | ASN- 142 | 2.78 | 128.38 | H-Bond (Protein Donor) |
CZ | CB | ASN- 142 | 3.9 | 0 | Hydrophobic |
C4 | CZ | TYR- 149 | 3.97 | 0 | Hydrophobic |
C6 | CE2 | TYR- 149 | 3.68 | 0 | Hydrophobic |
C8 | CZ | PHE- 154 | 4.12 | 0 | Hydrophobic |
C10 | CZ | PHE- 154 | 3.76 | 0 | Hydrophobic |
C12 | CE1 | PHE- 154 | 4.16 | 0 | Hydrophobic |
CB | CE2 | TYR- 163 | 4.12 | 0 | Hydrophobic |
CG | CG2 | VAL- 166 | 4.2 | 0 | Hydrophobic |
CE2 | CG1 | VAL- 166 | 3.7 | 0 | Hydrophobic |
CZ | CB | ALA- 168 | 4.06 | 0 | Hydrophobic |
OH | O | PRO- 169 | 2.96 | 152.69 | H-Bond (Ligand Donor) |
CE1 | CB | ALA- 170 | 4.07 | 0 | Hydrophobic |
C12 | CD2 | LEU- 175 | 3.85 | 0 | Hydrophobic |