1.950 Å
X-ray
2011-03-10
Name: | N-acetyltransferase Eis |
---|---|
ID: | EIS_MYCTU |
AC: | P9WFK7 |
Organism: | Mycobacterium tuberculosis |
Reign: | Bacteria |
TaxID: | 83332 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 29.811 |
---|---|
Number of residues: | 32 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.061 | 1238.625 |
% Hydrophobic | % Polar |
---|---|
46.05 | 53.95 |
According to VolSite |
HET Code: | COA |
---|---|
Formula: | C21H32N7O16P3S |
Molecular weight: | 763.502 g/mol |
DrugBank ID: | DB01992 |
Buried Surface Area: | 54.59 % |
Polar Surface area: | 426.11 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 21 |
H-Bond Donors: | 6 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 18 |
X | Y | Z |
---|---|---|
19.8704 | -24.4243 | 50.2899 |
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 |
C6P | CB | SER- 23 | 4.14 | 0 | Hydrophobic |
C6P | CE2 | PHE- 24 | 3.84 | 0 | Hydrophobic |
C2P | CE2 | PHE- 24 | 4.28 | 0 | Hydrophobic |
CDP | CG1 | VAL- 85 | 4.29 | 0 | Hydrophobic |
C2P | CB | VAL- 85 | 4.46 | 0 | Hydrophobic |
N4P | O | VAL- 85 | 2.98 | 134.31 | H-Bond (Ligand Donor) |
CDP | CG2 | VAL- 87 | 4.25 | 0 | Hydrophobic |
O9P | N | VAL- 87 | 2.72 | 174.14 | H-Bond (Protein Donor) |
C2B | CD | ARG- 93 | 4.11 | 0 | Hydrophobic |
O4A | N | ARG- 93 | 2.73 | 173.01 | H-Bond (Protein Donor) |
O4A | NE | ARG- 93 | 3.08 | 144.67 | H-Bond (Protein Donor) |
O4A | NH2 | ARG- 93 | 3.22 | 134.91 | H-Bond (Protein Donor) |
O4A | CZ | ARG- 93 | 3.57 | 0 | Ionic (Protein Cationic) |
O1A | N | GLY- 95 | 2.86 | 147.75 | H-Bond (Protein Donor) |
O5A | N | LEU- 97 | 3.2 | 159.43 | H-Bond (Protein Donor) |
CDP | CD1 | LEU- 97 | 4.19 | 0 | Hydrophobic |
CCP | CD2 | LEU- 97 | 3.86 | 0 | Hydrophobic |
O9A | CZ | ARG- 98 | 3.7 | 0 | Ionic (Protein Cationic) |
O9A | NH2 | ARG- 98 | 2.94 | 147.4 | H-Bond (Protein Donor) |
O2A | N | ARG- 98 | 3.03 | 161.9 | H-Bond (Protein Donor) |
O5P | OG | SER- 121 | 2.79 | 166.23 | H-Bond (Protein Donor) |
C2P | CB | SER- 121 | 3.73 | 0 | Hydrophobic |
N6A | OE2 | GLU- 122 | 2.91 | 163.24 | H-Bond (Ligand Donor) |
CEP | CD1 | ILE- 125 | 3.85 | 0 | Hydrophobic |
S1P | CE2 | TYR- 126 | 3.57 | 0 | Hydrophobic |
C4B | CD | ARG- 128 | 3.8 | 0 | Hydrophobic |
C5B | CZ | PHE- 129 | 4.43 | 0 | Hydrophobic |
O5A | O | HOH- 421 | 2.59 | 152.95 | H-Bond (Protein Donor) |