2.870 Å
X-ray
2013-07-11
Name: | Glutamine synthetase |
---|---|
ID: | GLNA_BACSU |
AC: | P12425 |
Organism: | Bacillus subtilis |
Reign: | Bacteria |
TaxID: | 224308 |
EC Number: | 6.3.1.2 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 17 % |
F | 83 % |
B-Factor: | 70.976 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 29 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.127 | 840.375 |
% Hydrophobic | % Polar |
---|---|
31.73 | 68.27 |
According to VolSite |
HET Code: | ADP |
---|---|
Formula: | C10H12N5O10P2 |
Molecular weight: | 424.177 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 54.78 % |
Polar Surface area: | 260.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 14 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 3 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 6 |
X | Y | Z |
---|---|---|
46.1397 | 54.2029 | 18.3717 |
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 | NZ | LYS- 44 | 3.85 | 0 | Ionic (Protein Cationic) |
O1A | NZ | LYS- 44 | 2.87 | 0 | Ionic (Protein Cationic) |
O2A | NZ | LYS- 44 | 3.85 | 0 | Ionic (Protein Cationic) |
O2' | O | PHE- 199 | 3.08 | 173.32 | H-Bond (Ligand Donor) |
C1' | CB | ASN- 247 | 3.93 | 0 | Hydrophobic |
N1 | OG | SER- 249 | 2.65 | 169.15 | H-Bond (Protein Donor) |
O3B | OG | SER- 325 | 3.25 | 154.59 | H-Bond (Protein Donor) |
O1B | OG | SER- 329 | 2.62 | 120.11 | H-Bond (Protein Donor) |
C1' | CD | ARG- 331 | 4 | 0 | Hydrophobic |