1.950 Å
X-ray
2013-04-10
Name: | Enoyl-[acyl-carrier-protein] reductase [NADH] |
---|---|
ID: | INHA_MYCTU |
AC: | P9WGR1 |
Organism: | Mycobacterium tuberculosis |
Reign: | Bacteria |
TaxID: | 83332 |
EC Number: | 1.3.1.9 |
Chain Name: | Percentage of Residues within binding site |
---|---|
D | 100 % |
B-Factor: | 27.954 |
---|---|
Number of residues: | 43 |
Including | |
Standard Amino Acids: | 40 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.730 | 1019.250 |
% Hydrophobic | % Polar |
---|---|
58.94 | 41.06 |
According to VolSite |
HET Code: | PYW |
---|---|
Formula: | C27H32N4O8 |
Molecular weight: | 540.565 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 58.79 % |
Polar Surface area: | 177.03 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 10 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 5 |
X | Y | Z |
---|---|---|
34.1806 | 5.50218 | 27.3915 |
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 |
CAK | CG2 | ILE- 21 | 4.2 | 0 | Hydrophobic |
CAL | CB | SER- 94 | 4.33 | 0 | Hydrophobic |
CAB | CE | MET- 103 | 4.17 | 0 | Hydrophobic |
CAA | CE | MET- 103 | 4.31 | 0 | Hydrophobic |
CG2 | CE | MET- 103 | 3.49 | 0 | Hydrophobic |
CAL | CB | MET- 147 | 3.57 | 0 | Hydrophobic |
CAS | CD1 | PHE- 149 | 3.75 | 0 | Hydrophobic |
CBK | CE1 | PHE- 149 | 3.82 | 0 | Hydrophobic |
CBJ | CE2 | PHE- 149 | 4.04 | 0 | Hydrophobic |
CAD | CZ | PHE- 149 | 3.84 | 0 | Hydrophobic |
CAA | CB | ALA- 157 | 3.71 | 0 | Hydrophobic |
CG2 | CE1 | TYR- 158 | 4.36 | 0 | Hydrophobic |
CBJ | CE1 | TYR- 158 | 4.24 | 0 | Hydrophobic |
CAA | CD1 | TYR- 158 | 4.01 | 0 | Hydrophobic |
O | OH | TYR- 158 | 2.68 | 141.84 | H-Bond (Protein Donor) |
CG2 | CG | MET- 161 | 3.97 | 0 | Hydrophobic |
OAI | NZ | LYS- 165 | 2.68 | 151.59 | H-Bond (Protein Donor) |
CBF | CB | ALA- 191 | 4.48 | 0 | Hydrophobic |
CBK | CB | PRO- 193 | 4.32 | 0 | Hydrophobic |
CAD | CB | PRO- 193 | 4.46 | 0 | Hydrophobic |
CAO | CB | ILE- 194 | 4.07 | 0 | Hydrophobic |
CBF | CG1 | ILE- 194 | 4.45 | 0 | Hydrophobic |
OAJ | N | ILE- 194 | 3.14 | 159.15 | H-Bond (Protein Donor) |
CAD | CE | MET- 199 | 3.83 | 0 | Hydrophobic |
CAR | CG1 | ILE- 215 | 4.26 | 0 | Hydrophobic |
CAD | CD1 | LEU- 218 | 4.22 | 0 | Hydrophobic |