1.700 Å
X-ray
2011-11-14
Name: | ATP-dependent 6-phosphofructokinase isozyme 2 |
---|---|
ID: | PFKB_ECOLI |
AC: | P06999 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | 2.7.1.11 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 95 % |
B | 5 % |
B-Factor: | 22.265 |
---|---|
Number of residues: | 43 |
Including | |
Standard Amino Acids: | 38 |
Non Standard Amino Acids: | 3 |
Water Molecules: | 2 |
Cofactors: | ATP |
Metals: | MG MG |
Ligandability | Volume (Å3) |
---|---|
0.897 | 1542.375 |
% Hydrophobic | % Polar |
---|---|
39.61 | 60.39 |
According to VolSite |
HET Code: | ATP |
---|---|
Formula: | C10H12N5O13P3 |
Molecular weight: | 503.149 g/mol |
DrugBank ID: | DB00171 |
Buried Surface Area: | 68.73 % |
Polar Surface area: | 319.88 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
6.22713 | -20.2189 | 13.3105 |
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 |
O1G | NZ | LYS- 27 | 3.13 | 176.31 | H-Bond (Protein Donor) |
O1G | NZ | LYS- 27 | 3.13 | 0 | Ionic (Protein Cationic) |
O3G | NZ | LYS- 27 | 3.24 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 185 | 2.87 | 165.22 | H-Bond (Protein Donor) |
O2B | NZ | LYS- 185 | 2.87 | 0 | Ionic (Protein Cationic) |
O1B | ND2 | ASN- 187 | 2.97 | 171.34 | H-Bond (Protein Donor) |
O2A | OG | SER- 224 | 2.84 | 128.47 | H-Bond (Protein Donor) |
O3A | OG | SER- 224 | 3.09 | 158.71 | H-Bond (Protein Donor) |
C5' | CB | SER- 224 | 4.03 | 0 | Hydrophobic |
O2A | N | GLY- 226 | 2.77 | 155.32 | H-Bond (Protein Donor) |
O3' | O | GLY- 229 | 2.71 | 138.78 | H-Bond (Ligand Donor) |
C2' | CG | PRO- 243 | 4.48 | 0 | Hydrophobic |
C1' | CB | ALA- 254 | 4.21 | 0 | Hydrophobic |
C5' | CB | ALA- 254 | 4.02 | 0 | Hydrophobic |
O2G | N | GLY- 255 | 3.14 | 153.18 | H-Bond (Protein Donor) |
C5' | SD | MET- 258 | 3.96 | 0 | Hydrophobic |
C4' | CE | MET- 258 | 3.87 | 0 | Hydrophobic |
O2' | OG | SER- 284 | 3.04 | 159.04 | H-Bond (Ligand Donor) |
C1' | CB | SER- 284 | 4.28 | 0 | Hydrophobic |
N3 | OG | SER- 284 | 2.95 | 173.46 | H-Bond (Protein Donor) |
C1' | CG2 | THR- 287 | 4.47 | 0 | Hydrophobic |
O1G | MG | MG- 310 | 2.14 | 0 | Metal Acceptor |
O2B | MG | MG- 310 | 2.05 | 0 | Metal Acceptor |
O3G | MG | MG- 311 | 2.13 | 0 | Metal Acceptor |
O1B | MG | MG- 311 | 2.06 | 0 | Metal Acceptor |