2.400 Å
X-ray
2004-07-22
Name: | NTPase P4 |
---|---|
ID: | Q94M05_9VIRU |
AC: | Q94M05 |
Organism: | Pseudomonas phage phi12 |
Reign: | Viruses |
TaxID: | 161736 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 33 % |
C | 67 % |
B-Factor: | 32.606 |
---|---|
Number of residues: | 41 |
Including | |
Standard Amino Acids: | 35 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 5 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.287 | 594.000 |
% Hydrophobic | % Polar |
---|---|
38.07 | 61.93 |
According to VolSite |
HET Code: | APC |
---|---|
Formula: | C11H14N5O12P3 |
Molecular weight: | 501.176 g/mol |
DrugBank ID: | DB02596 |
Buried Surface Area: | 58.13 % |
Polar Surface area: | 310.64 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 16 |
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 |
---|---|---|
31.898 | 52.6313 | 27.1415 |
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 |
O2B | N | THR- 137 | 2.79 | 145.42 | H-Bond (Protein Donor) |
C3A | CB | THR- 137 | 3.39 | 0 | Hydrophobic |
C5' | CG | PRO- 138 | 4.29 | 0 | Hydrophobic |
O1G | NZ | LYS- 192 | 2.83 | 125.19 | H-Bond (Protein Donor) |
O1G | NZ | LYS- 192 | 2.83 | 0 | Ionic (Protein Cationic) |
O1A | N | GLY- 276 | 3.48 | 138.53 | H-Bond (Protein Donor) |
C2' | CG | GLN- 278 | 4.23 | 0 | Hydrophobic |
C1' | CZ | TYR- 288 | 4.21 | 0 | Hydrophobic |
DuAr | DuAr | TYR- 288 | 3.53 | 0 | Aromatic Face/Face |
N7 | OG | SER- 292 | 2.59 | 160.74 | H-Bond (Protein Donor) |
O2G | NZ | LYS- 310 | 3.95 | 0 | Ionic (Protein Cationic) |
O1B | NZ | LYS- 310 | 3.42 | 0 | Ionic (Protein Cationic) |
O2A | NZ | LYS- 310 | 2.74 | 0 | Ionic (Protein Cationic) |
O1B | NZ | LYS- 310 | 3.42 | 129.92 | H-Bond (Protein Donor) |
O2A | NZ | LYS- 310 | 2.74 | 155.96 | H-Bond (Protein Donor) |
C3' | CD | LYS- 310 | 4.31 | 0 | Hydrophobic |
O3B | MG | MG- 701 | 2.7 | 0 | Metal Acceptor |
O1A | O | HOH- 2165 | 2.99 | 156.1 | H-Bond (Protein Donor) |
O2' | O | HOH- 2183 | 2.51 | 152.61 | H-Bond (Protein Donor) |