1.990 Å
X-ray
2011-06-17
Name: | Serine-pyruvate aminotransferase (AgxT) |
---|---|
ID: | Q97VM5_SULSO |
AC: | Q97VM5 |
Organism: | Sulfolobus solfataricus |
Reign: | Archaea |
TaxID: | 273057 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 82 % |
B | 18 % |
B-Factor: | 33.286 |
---|---|
Number of residues: | 39 |
Including | |
Standard Amino Acids: | 38 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.059 | 594.000 |
% Hydrophobic | % Polar |
---|---|
65.34 | 34.66 |
According to VolSite |
HET Code: | PXG |
---|---|
Formula: | C15H14N2O7P |
Molecular weight: | 365.255 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 73.19 % |
Polar Surface area: | 167.51 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 9 |
H-Bond Donors: | 2 |
Rings: | 2 |
Aromatic rings: | 2 |
Anionic atoms: | 3 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
-22.0526 | -19.8464 | -16.774 |
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 |
C13 | CG1 | VAL- 8 | 4 | 0 | Hydrophobic |
C12 | CE1 | PHE- 28 | 3.35 | 0 | Hydrophobic |
OP1 | N | GLY- 63 | 2.87 | 146.67 | H-Bond (Protein Donor) |
OP3 | OG1 | THR- 64 | 2.51 | 149.3 | H-Bond (Protein Donor) |
OP3 | N | THR- 64 | 2.64 | 148.23 | H-Bond (Protein Donor) |
C2A | CB | PHE- 88 | 3.76 | 0 | Hydrophobic |
C3 | CB | PHE- 88 | 4.32 | 0 | Hydrophobic |
C5A | CE1 | PHE- 88 | 3.88 | 0 | Hydrophobic |
C4A | CE1 | PHE- 88 | 3.7 | 0 | Hydrophobic |
DuAr | DuAr | PHE- 88 | 3.77 | 0 | Aromatic Face/Face |
C2A | CG2 | THR- 134 | 4.19 | 0 | Hydrophobic |
C2A | CB | THR- 138 | 4.38 | 0 | Hydrophobic |
C3 | CB | THR- 138 | 4.45 | 0 | Hydrophobic |
C9 | CG2 | THR- 138 | 3.94 | 0 | Hydrophobic |
O3 | OG1 | THR- 138 | 2.54 | 141.69 | H-Bond (Ligand Donor) |
N1 | OD2 | ASP- 163 | 2.59 | 172.18 | H-Bond (Ligand Donor) |
C2A | CB | VAL- 165 | 3.96 | 0 | Hydrophobic |
C4A | CG1 | VAL- 165 | 4.1 | 0 | Hydrophobic |
C3 | CG1 | VAL- 165 | 3.47 | 0 | Hydrophobic |
O3 | OG | SER- 166 | 3.43 | 126.31 | H-Bond (Ligand Donor) |
OP1 | NE2 | GLN- 188 | 2.97 | 154.22 | H-Bond (Protein Donor) |
OP2 | OH | TYR- 240 | 2.76 | 174.44 | H-Bond (Protein Donor) |
C12 | CE1 | TYR- 240 | 3.31 | 0 | Hydrophobic |
OP2 | N | THR- 243 | 2.84 | 152.15 | H-Bond (Protein Donor) |
OP2 | OG1 | THR- 243 | 2.73 | 152.47 | H-Bond (Protein Donor) |
O2 | NH2 | ARG- 337 | 3.26 | 139.13 | H-Bond (Protein Donor) |
O8 | NH2 | ARG- 337 | 2.88 | 156.25 | H-Bond (Protein Donor) |
O8 | NH1 | ARG- 337 | 3.17 | 138.69 | H-Bond (Protein Donor) |
O8 | CZ | ARG- 337 | 3.45 | 0 | Ionic (Protein Cationic) |