2.500 Å
X-ray
2008-09-05
Name: | Pantothenate kinase |
---|---|
ID: | COAA_MYCTU |
AC: | P9WPA7 |
Organism: | Mycobacterium tuberculosis |
Reign: | Bacteria |
TaxID: | 83332 |
EC Number: | 2.7.1.33 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 43.559 |
---|---|
Number of residues: | 47 |
Including | |
Standard Amino Acids: | 46 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.947 | 1080.000 |
% Hydrophobic | % Polar |
---|---|
49.06 | 50.94 |
According to VolSite |
HET Code: | COA |
---|---|
Formula: | C21H32N7O16P3S |
Molecular weight: | 763.502 g/mol |
DrugBank ID: | DB01992 |
Buried Surface Area: | 61.95 % |
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 |
---|---|---|
45.0671 | 36.4055 | 29.2733 |
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 |
CAP | CG2 | VAL- 99 | 4.13 | 0 | Hydrophobic |
O1A | N | ALA- 100 | 2.56 | 151.72 | H-Bond (Protein Donor) |
O2A | NZ | LYS- 103 | 2.91 | 148.62 | H-Bond (Protein Donor) |
O4A | NZ | LYS- 103 | 2.53 | 136.68 | H-Bond (Protein Donor) |
O2A | NZ | LYS- 103 | 2.91 | 0 | Ionic (Protein Cationic) |
O4A | NZ | LYS- 103 | 2.53 | 0 | Ionic (Protein Cationic) |
O7A | OG | SER- 104 | 2.8 | 159.28 | H-Bond (Protein Donor) |
O8A | OG | SER- 104 | 3.16 | 126.76 | H-Bond (Protein Donor) |
C5B | CB | SER- 104 | 4.42 | 0 | Hydrophobic |
O7A | CZ | ARG- 108 | 3.49 | 0 | Ionic (Protein Cationic) |
O9A | CZ | ARG- 108 | 3.93 | 0 | Ionic (Protein Cationic) |
O7A | NH1 | ARG- 108 | 2.63 | 159.76 | H-Bond (Protein Donor) |
O8A | NH2 | ARG- 108 | 3.37 | 162.79 | H-Bond (Protein Donor) |
O5A | OD2 | ASP- 129 | 3.16 | 163.72 | H-Bond (Protein Donor) |
CDP | CD1 | LEU- 132 | 4.37 | 0 | Hydrophobic |
CEP | CD1 | LEU- 132 | 4.48 | 0 | Hydrophobic |
CDP | CG | LYS- 147 | 4.49 | 0 | Hydrophobic |
CEP | CZ | TYR- 177 | 4.05 | 0 | Hydrophobic |
O5A | NE2 | HIS- 179 | 3.16 | 156.96 | H-Bond (Protein Donor) |
CEP | CE1 | TYR- 182 | 4.29 | 0 | Hydrophobic |
C6P | CZ | TYR- 182 | 4.32 | 0 | Hydrophobic |
CDP | CD1 | LEU- 203 | 4.11 | 0 | Hydrophobic |
O1A | NH1 | ARG- 238 | 3.38 | 136.4 | H-Bond (Protein Donor) |
O1A | NH2 | ARG- 238 | 2.92 | 164.53 | H-Bond (Protein Donor) |
O1A | CZ | ARG- 238 | 3.59 | 0 | Ionic (Protein Cationic) |
S1P | CE1 | PHE- 239 | 3.88 | 0 | Hydrophobic |
C1B | CE | MET- 242 | 4.38 | 0 | Hydrophobic |
S1P | CZ | PHE- 247 | 3.6 | 0 | Hydrophobic |
C2P | CZ | PHE- 254 | 3.24 | 0 | Hydrophobic |
S1P | CE2 | PHE- 254 | 3.93 | 0 | Hydrophobic |
S1P | CE1 | TYR- 257 | 4.37 | 0 | Hydrophobic |
C6P | CG2 | ILE- 276 | 4.35 | 0 | Hydrophobic |
O5P | ND2 | ASN- 277 | 3.39 | 154.24 | H-Bond (Protein Donor) |
O5A | O | HOH- 445 | 3.35 | 179.98 | H-Bond (Protein Donor) |