2.300 Å
X-ray
2012-06-14
Name: | Aminotransferase ALD1, chloroplastic |
---|---|
ID: | ALD1_ARATH |
AC: | Q9ZQI7 |
Organism: | Arabidopsis thaliana |
Reign: | Eukaryota |
TaxID: | 3702 |
EC Number: | 2.6.1 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 94 % |
B | 6 % |
B-Factor: | 26.090 |
---|---|
Number of residues: | 33 |
Including | |
Standard Amino Acids: | 32 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.045 | 1049.625 |
% Hydrophobic | % Polar |
---|---|
48.23 | 51.77 |
According to VolSite |
HET Code: | PLP |
---|---|
Formula: | C8H8NO6P |
Molecular weight: | 245.126 g/mol |
DrugBank ID: | DB00114 |
Buried Surface Area: | 74.64 % |
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 |
---|---|---|
16.4322 | -69.5942 | 202.141 |
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 | ALA- 142 | 2.76 | 163.43 | H-Bond (Protein Donor) |
C5A | CB | ALA- 142 | 3.77 | 0 | Hydrophobic |
O2P | N | GLN- 143 | 2.97 | 166.35 | H-Bond (Protein Donor) |
C2A | CZ | PHE- 166 | 3.5 | 0 | Hydrophobic |
C2A | SG | CYS- 219 | 3.64 | 0 | Hydrophobic |
C2A | CB | ASN- 223 | 3.76 | 0 | Hydrophobic |
O3 | ND2 | ASN- 223 | 2.92 | 154.07 | H-Bond (Protein Donor) |
N1 | OD2 | ASP- 251 | 2.71 | 169.77 | H-Bond (Ligand Donor) |
N1 | OD1 | ASP- 251 | 3.41 | 132.39 | H-Bond (Ligand Donor) |
C5 | CB | ALA- 253 | 3.99 | 0 | Hydrophobic |
C2A | CE2 | TYR- 254 | 3.93 | 0 | Hydrophobic |
O3 | OH | TYR- 254 | 2.69 | 155.97 | H-Bond (Protein Donor) |
C5A | CB | SER- 281 | 4.03 | 0 | Hydrophobic |
O3P | OG | SER- 281 | 2.65 | 164.04 | H-Bond (Protein Donor) |
C5A | CB | SER- 283 | 4.42 | 0 | Hydrophobic |
O1P | OG | SER- 283 | 2.79 | 166.11 | H-Bond (Protein Donor) |
O1P | CZ | ARG- 292 | 3.88 | 0 | Ionic (Protein Cationic) |
O2P | CZ | ARG- 292 | 3.72 | 0 | Ionic (Protein Cationic) |
O1P | NH1 | ARG- 292 | 3.06 | 170.81 | H-Bond (Protein Donor) |
O2P | NH2 | ARG- 292 | 2.78 | 171.09 | H-Bond (Protein Donor) |
O2P | ND2 | ASN- 323 | 3.12 | 157.63 | H-Bond (Protein Donor) |