0.920 Å
X-ray
2003-07-02
Name: | Aldose reductase |
---|---|
ID: | ALDR_HUMAN |
AC: | P15121 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 1.1.1.21 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 7.568 |
---|---|
Number of residues: | 25 |
Including | |
Standard Amino Acids: | 24 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | NAP |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.731 | 509.625 |
% Hydrophobic | % Polar |
---|---|
54.97 | 45.03 |
According to VolSite |
HET Code: | FID |
---|---|
Formula: | C12H10FN3O4 |
Molecular weight: | 279.224 g/mol |
DrugBank ID: | DB02021 |
Buried Surface Area: | 73.09 % |
Polar Surface area: | 110.52 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 4 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 1 |
X | Y | Z |
---|---|---|
16.8739 | -7.75985 | 16.7138 |
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 |
C8I | CH2 | TRP- 20 | 4.2 | 0 | Hydrophobic |
C15 | CG2 | VAL- 47 | 4.25 | 0 | Hydrophobic |
F17 | CG1 | VAL- 47 | 3.73 | 0 | Hydrophobic |
F17 | CD1 | TYR- 48 | 3.91 | 0 | Hydrophobic |
N4 | NE2 | HIS- 110 | 2.75 | 158.35 | H-Bond (Ligand Donor) |
O6I | NE1 | TRP- 111 | 2.79 | 156 | H-Bond (Protein Donor) |
C9 | CZ2 | TRP- 111 | 4.2 | 0 | Hydrophobic |
C8I | CH2 | TRP- 219 | 4.3 | 0 | Hydrophobic |
C8I | SG | CYS- 298 | 3.61 | 0 | Hydrophobic |
C9 | CD1 | LEU- 300 | 3.92 | 0 | Hydrophobic |
O20 | N | LEU- 300 | 2.95 | 143.5 | H-Bond (Protein Donor) |