1.760 Å
X-ray
1994-04-15
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: | 9.065 |
---|---|
Number of residues: | 47 |
Including | |
Standard Amino Acids: | 45 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.742 | 816.750 |
% Hydrophobic | % Polar |
---|---|
49.59 | 50.41 |
According to VolSite |
HET Code: | NAP |
---|---|
Formula: | C21H25N7O17P3 |
Molecular weight: | 740.381 g/mol |
DrugBank ID: | DB03461 |
Buried Surface Area: | 78.55 % |
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 |
---|---|---|
22.1515 | 26.9256 | 72.9159 |
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 |
O2D | N | THR- 19 | 3.32 | 146.85 | H-Bond (Protein Donor) |
O3D | N | TRP- 20 | 2.94 | 144.92 | H-Bond (Protein Donor) |
C3D | CB | TRP- 20 | 3.74 | 0 | Hydrophobic |
O1N | NZ | LYS- 21 | 2.84 | 149.44 | H-Bond (Protein Donor) |
O1N | NZ | LYS- 21 | 2.84 | 0 | Ionic (Protein Cationic) |
O2D | OD2 | ASP- 43 | 2.74 | 150.78 | H-Bond (Ligand Donor) |
C2D | CZ | TYR- 48 | 4.13 | 0 | Hydrophobic |
N7N | OG | SER- 159 | 2.89 | 140.85 | H-Bond (Ligand Donor) |
O7N | ND2 | ASN- 160 | 3.1 | 164.03 | H-Bond (Protein Donor) |
N7N | OE1 | GLN- 183 | 3.04 | 158.07 | H-Bond (Ligand Donor) |
C3N | CB | TYR- 209 | 4.3 | 0 | Hydrophobic |
DuAr | DuAr | TYR- 209 | 3.55 | 0 | Aromatic Face/Face |
O2N | OG | SER- 210 | 2.7 | 152.01 | H-Bond (Protein Donor) |
O5D | N | SER- 210 | 3.12 | 133.77 | H-Bond (Protein Donor) |
O1A | N | LEU- 212 | 3.11 | 142.4 | H-Bond (Protein Donor) |
C1B | CD1 | LEU- 212 | 4.29 | 0 | Hydrophobic |
O1A | N | SER- 214 | 3.06 | 142.97 | H-Bond (Protein Donor) |
O2N | OG | SER- 214 | 2.8 | 150.34 | H-Bond (Protein Donor) |
C4B | CG | PRO- 215 | 3.58 | 0 | Hydrophobic |
C1B | CG | PRO- 215 | 4.17 | 0 | Hydrophobic |
C3B | CB | ASP- 216 | 4.27 | 0 | Hydrophobic |
C4D | CG1 | ILE- 260 | 4.19 | 0 | Hydrophobic |
O2A | N | LYS- 262 | 2.88 | 172.32 | H-Bond (Protein Donor) |
O1X | NZ | LYS- 262 | 2.79 | 172.94 | H-Bond (Protein Donor) |
C5B | CD | LYS- 262 | 3.88 | 0 | Hydrophobic |
C3B | CD | LYS- 262 | 3.92 | 0 | Hydrophobic |
C5D | CB | LYS- 262 | 3.93 | 0 | Hydrophobic |
O1X | NZ | LYS- 262 | 2.79 | 0 | Ionic (Protein Cationic) |
O3X | OG | SER- 263 | 2.8 | 167.82 | H-Bond (Protein Donor) |
O1X | N | VAL- 264 | 3.07 | 155.22 | H-Bond (Protein Donor) |
O3X | OG1 | THR- 265 | 2.82 | 158.31 | H-Bond (Protein Donor) |
O3X | CZ | ARG- 268 | 3.85 | 0 | Ionic (Protein Cationic) |
N6A | OE2 | GLU- 271 | 3.07 | 167.03 | H-Bond (Ligand Donor) |
N7A | ND2 | ASN- 272 | 3.06 | 170.99 | H-Bond (Protein Donor) |
N6A | OD1 | ASN- 272 | 2.89 | 144.83 | H-Bond (Ligand Donor) |
C4N | SG | CYS- 298 | 4.14 | 0 | Hydrophobic |
N1A | O | HOH- 917 | 2.93 | 179.94 | H-Bond (Protein Donor) |