2.310 Å
X-ray
2015-05-19
Name: | Ornithine aminotransferase, mitochondrial, putative |
---|---|
ID: | S8EY38_TOXGM |
AC: | S8EY38 |
Organism: | Toxoplasma gondii |
Reign: | Eukaryota |
TaxID: | 508771 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 80 % |
B | 20 % |
B-Factor: | 27.112 |
---|---|
Number of residues: | 33 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.537 | 826.875 |
% Hydrophobic | % Polar |
---|---|
36.33 | 63.67 |
According to VolSite |
HET Code: | PLP |
---|---|
Formula: | C8H8NO6P |
Molecular weight: | 245.126 g/mol |
DrugBank ID: | DB00114 |
Buried Surface Area: | 70.23 % |
Polar Surface area: | 132.42 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 1 |
Rings: | 1 |
Aromatic rings: | 1 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 4 |
X | Y | Z |
---|---|---|
27.1337 | 1.84733 | 58.4643 |
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 |
O3P | N | GLY- 136 | 3.07 | 156.23 | H-Bond (Protein Donor) |
O2P | N | ALA- 137 | 3.09 | 156.3 | H-Bond (Protein Donor) |
C4A | CE1 | TYR- 171 | 3.5 | 0 | Hydrophobic |
C5A | CE1 | TYR- 171 | 4.39 | 0 | Hydrophobic |
C2A | CG | GLU- 224 | 4.42 | 0 | Hydrophobic |
N1 | OD2 | ASP- 257 | 2.8 | 162.43 | H-Bond (Ligand Donor) |
C2A | CB | ILE- 259 | 4.36 | 0 | Hydrophobic |
C5 | CG2 | ILE- 259 | 4.01 | 0 | Hydrophobic |
C2A | CB | GLN- 260 | 4.22 | 0 | Hydrophobic |
O1P | OG1 | THR- 316 | 2.54 | 157.61 | H-Bond (Protein Donor) |
O1P | N | THR- 316 | 2.93 | 150.18 | H-Bond (Protein Donor) |
O3 | O | HOH- 653 | 2.89 | 153.91 | H-Bond (Protein Donor) |