1.040 Å
X-ray
2005-03-14
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: | 11.192 |
---|---|
Number of residues: | 34 |
Including | |
Standard Amino Acids: | 32 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | NDP |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.798 | 394.875 |
% Hydrophobic | % Polar |
---|---|
63.25 | 36.75 |
According to VolSite |
HET Code: | 3NA |
---|---|
Formula: | C18H10F3N2O2S |
Molecular weight: | 375.344 g/mol |
DrugBank ID: | DB07063 |
Buried Surface Area: | 75.55 % |
Polar Surface area: | 86.19 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 3 |
H-Bond Donors: | 0 |
Rings: | 4 |
Aromatic rings: | 4 |
Anionic atoms: | 1 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 4 |
X | Y | Z |
---|---|---|
16.9437 | -6.25973 | 14.3405 |
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 |
C20 | CE2 | TRP- 20 | 3.52 | 0 | Hydrophobic |
C20 | CE1 | TYR- 48 | 4.1 | 0 | Hydrophobic |
O33 | OH | TYR- 48 | 2.72 | 161.12 | H-Bond (Protein Donor) |
S14 | CH2 | TRP- 79 | 4.3 | 0 | Hydrophobic |
F19 | CH2 | TRP- 79 | 3.4 | 0 | Hydrophobic |
F19 | SG | CYS- 80 | 3.5 | 0 | Hydrophobic |
O33 | NE2 | HIS- 110 | 2.69 | 152.57 | H-Bond (Protein Donor) |
S14 | CZ2 | TRP- 111 | 3.63 | 0 | Hydrophobic |
C17 | CZ2 | TRP- 111 | 4.35 | 0 | Hydrophobic |
F19 | CD2 | TRP- 111 | 3.88 | 0 | Hydrophobic |
F22 | CZ3 | TRP- 111 | 3.65 | 0 | Hydrophobic |
F23 | CE3 | TRP- 111 | 3.91 | 0 | Hydrophobic |
C25 | CB | TRP- 111 | 4.06 | 0 | Hydrophobic |
O34 | NE1 | TRP- 111 | 2.95 | 161.16 | H-Bond (Protein Donor) |
DuAr | DuAr | TRP- 111 | 3.51 | 0 | Aromatic Face/Face |
F23 | CG2 | THR- 113 | 3.76 | 0 | Hydrophobic |
C25 | CG2 | THR- 113 | 4.46 | 0 | Hydrophobic |
F19 | CZ | PHE- 115 | 3.52 | 0 | Hydrophobic |
S14 | CZ | PHE- 122 | 3.96 | 0 | Hydrophobic |
F19 | CE2 | PHE- 122 | 3.96 | 0 | Hydrophobic |
C17 | CH2 | TRP- 219 | 3.77 | 0 | Hydrophobic |
C17 | SG | CYS- 298 | 4.25 | 0 | Hydrophobic |
F22 | CB | ALA- 299 | 4.15 | 0 | Hydrophobic |
C3 | CD1 | LEU- 300 | 3.97 | 0 | Hydrophobic |
C17 | CG | LEU- 300 | 3.74 | 0 | Hydrophobic |
S14 | CD1 | LEU- 300 | 3.88 | 0 | Hydrophobic |
F22 | CB | LEU- 300 | 4.34 | 0 | Hydrophobic |
C26 | CB | CYS- 303 | 4.06 | 0 | Hydrophobic |
F23 | CB | CYS- 303 | 3.49 | 0 | Hydrophobic |
C25 | SG | CYS- 303 | 3.74 | 0 | Hydrophobic |
F22 | CE1 | TYR- 309 | 3.4 | 0 | Hydrophobic |
F23 | CD1 | TYR- 309 | 3.39 | 0 | Hydrophobic |
F22 | CE2 | PHE- 311 | 4.2 | 0 | Hydrophobic |
C20 | C4N | NDP- 318 | 3.78 | 0 | Hydrophobic |