2.100 Å
X-ray
2007-05-31
Name: | Uncharacterized protein At5g02240 |
---|---|
ID: | Y5224_ARATH |
AC: | Q94EG6 |
Organism: | Arabidopsis thaliana |
Reign: | Eukaryota |
TaxID: | 3702 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 27.889 |
---|---|
Number of residues: | 53 |
Including | |
Standard Amino Acids: | 47 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 6 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.963 | 789.750 |
% Hydrophobic | % Polar |
---|---|
48.72 | 51.28 |
According to VolSite |
HET Code: | NAP |
---|---|
Formula: | C21H25N7O17P3 |
Molecular weight: | 740.381 g/mol |
DrugBank ID: | DB03461 |
Buried Surface Area: | 61.46 % |
Polar Surface area: | 405.54 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 21 |
H-Bond Donors: | 5 |
Rings: | 5 |
Aromatic rings: | 3 |
Anionic atoms: | 4 |
Cationic atoms: | 1 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
61.1657 | 20.0729 | 63.9302 |
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 |
O1A | CZ | ARG- 15 | 3.65 | 0 | Ionic (Protein Cationic) |
O1N | CZ | ARG- 15 | 3.76 | 0 | Ionic (Protein Cationic) |
O1A | NH2 | ARG- 15 | 2.64 | 159.09 | H-Bond (Protein Donor) |
O2N | N | THR- 16 | 3.01 | 150 | H-Bond (Protein Donor) |
O2N | OG1 | THR- 16 | 2.79 | 157.25 | H-Bond (Protein Donor) |
N6A | OD1 | ASP- 56 | 2.63 | 131.08 | H-Bond (Ligand Donor) |
N1A | N | ILE- 57 | 2.91 | 158.01 | H-Bond (Protein Donor) |
C5D | CD2 | LEU- 76 | 3.55 | 0 | Hydrophobic |
C1B | CG2 | THR- 77 | 4.25 | 0 | Hydrophobic |
O3D | O | THR- 77 | 3.2 | 130.89 | H-Bond (Ligand Donor) |
C5B | CB | SER- 78 | 3.97 | 0 | Hydrophobic |
C3D | CB | SER- 78 | 3.23 | 0 | Hydrophobic |
O4B | N | SER- 78 | 3.17 | 144.69 | H-Bond (Protein Donor) |
O2D | OG | SER- 78 | 2.63 | 165.52 | H-Bond (Ligand Donor) |
N6A | OE1 | GLN- 103 | 3.08 | 151.5 | H-Bond (Ligand Donor) |
C4D | CG1 | VAL- 131 | 4.07 | 0 | Hydrophobic |
C5N | CB | SER- 133 | 3.4 | 0 | Hydrophobic |
O2D | NZ | LYS- 155 | 3.42 | 124.12 | H-Bond (Protein Donor) |
C5N | CB | ALA- 174 | 3.76 | 0 | Hydrophobic |
C5D | CD1 | LEU- 177 | 4.23 | 0 | Hydrophobic |
C3N | CG | LEU- 177 | 3.39 | 0 | Hydrophobic |
O7N | N | LEU- 177 | 3 | 175.83 | H-Bond (Protein Donor) |
O1N | CZ | ARG- 205 | 3.69 | 0 | Ionic (Protein Cationic) |
O2N | CZ | ARG- 205 | 3.64 | 0 | Ionic (Protein Cationic) |
O2N | NE | ARG- 205 | 3.44 | 133.2 | H-Bond (Protein Donor) |
O2N | NH2 | ARG- 205 | 3.01 | 141.59 | H-Bond (Protein Donor) |
O2X | O | HOH- 403 | 3.43 | 179.97 | H-Bond (Protein Donor) |
O2N | O | HOH- 405 | 3.34 | 179.98 | H-Bond (Protein Donor) |
O1X | O | HOH- 507 | 2.93 | 140.3 | H-Bond (Protein Donor) |