2.300 Å
X-ray
2013-04-29
Name: | Enoyl-[acyl-carrier-protein] reductase [NADH] |
---|---|
ID: | FABV_YERPE |
AC: | Q8Z9U1 |
Organism: | Yersinia pestis |
Reign: | Bacteria |
TaxID: | 632 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 58.241 |
---|---|
Number of residues: | 55 |
Including | |
Standard Amino Acids: | 54 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.557 | 1107.000 |
% Hydrophobic | % Polar |
---|---|
50.91 | 49.09 |
According to VolSite |
HET Code: | NAI |
---|---|
Formula: | C21H27N7O14P2 |
Molecular weight: | 663.425 g/mol |
DrugBank ID: | DB00157 |
Buried Surface Area: | 74.17 % |
Polar Surface area: | 342.9 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 19 |
H-Bond Donors: | 6 |
Rings: | 5 |
Aromatic rings: | 2 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 11 |
X | Y | Z |
---|---|---|
13.5859 | -23.7692 | -8.18666 |
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 |
O3B | N | SER- 73 | 3.15 | 151.84 | H-Bond (Protein Donor) |
O3B | OG | SER- 73 | 2.68 | 175.22 | H-Bond (Ligand Donor) |
O1A | OG1 | THR- 74 | 2.75 | 167.86 | H-Bond (Protein Donor) |
O1N | N | TYR- 76 | 2.83 | 162.48 | H-Bond (Protein Donor) |
C4N | CE2 | TYR- 76 | 3.73 | 0 | Hydrophobic |
O2B | N | PHE- 97 | 3.47 | 164.99 | H-Bond (Protein Donor) |
O2B | OE2 | GLU- 98 | 2.87 | 159.82 | H-Bond (Ligand Donor) |
N6A | OD1 | ASP- 134 | 2.91 | 170.86 | H-Bond (Ligand Donor) |
N1A | N | ALA- 135 | 2.85 | 167.46 | H-Bond (Protein Donor) |
C5D | CB | SER- 161 | 4.49 | 0 | Hydrophobic |
C1B | CD2 | LEU- 162 | 3.89 | 0 | Hydrophobic |
C5D | CB | ALA- 163 | 4.15 | 0 | Hydrophobic |
C3D | CB | ALA- 163 | 4.22 | 0 | Hydrophobic |
C5B | CB | ALA- 163 | 4.03 | 0 | Hydrophobic |
C3D | CE | MET- 219 | 4.26 | 0 | Hydrophobic |
C4D | CB | PHE- 246 | 4.06 | 0 | Hydrophobic |
C1D | CB | PHE- 246 | 3.93 | 0 | Hydrophobic |
C6N | CB | PHE- 246 | 4.42 | 0 | Hydrophobic |
C5N | CB | TYR- 248 | 3.4 | 0 | Hydrophobic |
O3D | NZ | LYS- 267 | 2.84 | 127.45 | H-Bond (Protein Donor) |
O2D | NZ | LYS- 267 | 3.12 | 137.3 | H-Bond (Protein Donor) |
C5N | CB | LEU- 294 | 3.82 | 0 | Hydrophobic |
O7N | N | VAL- 297 | 2.89 | 165.26 | H-Bond (Protein Donor) |
O2N | OG1 | THR- 299 | 2.6 | 144.63 | H-Bond (Protein Donor) |