1.950 Å
X-ray
2006-10-12
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: | 11.352 |
---|---|
Number of residues: | 47 |
Including | |
Standard Amino Acids: | 45 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.931 | 1100.250 |
% Hydrophobic | % Polar |
---|---|
47.24 | 52.76 |
According to VolSite |
HET Code: | NAP |
---|---|
Formula: | C21H25N7O17P3 |
Molecular weight: | 740.381 g/mol |
DrugBank ID: | DB03461 |
Buried Surface Area: | 79.38 % |
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 |
---|---|---|
22.1499 | 26.8101 | 72.7659 |
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 | 3.35 | 146.34 | H-Bond (Protein Donor) |
O3D | N | TRP- 20 | 2.93 | 144.55 | H-Bond (Protein Donor) |
C5N | CE3 | TRP- 20 | 3.48 | 0 | Hydrophobic |
C3D | CB | TRP- 20 | 3.75 | 0 | Hydrophobic |
O1N | NZ | LYS- 21 | 2.86 | 159.84 | H-Bond (Protein Donor) |
O1N | NZ | LYS- 21 | 2.86 | 0 | Ionic (Protein Cationic) |
O2D | OD1 | ASP- 43 | 2.62 | 165.22 | H-Bond (Ligand Donor) |
C2D | CZ | TYR- 48 | 4.12 | 0 | Hydrophobic |
N7N | OG | SER- 159 | 2.9 | 142.19 | H-Bond (Ligand Donor) |
O7N | ND2 | ASN- 160 | 2.9 | 163.8 | H-Bond (Protein Donor) |
N7N | OE1 | GLN- 183 | 3 | 160.97 | H-Bond (Ligand Donor) |
C3N | CB | TYR- 209 | 4.41 | 0 | Hydrophobic |
DuAr | DuAr | TYR- 209 | 3.6 | 0 | Aromatic Face/Face |
O2N | OG | SER- 210 | 2.85 | 152.71 | H-Bond (Protein Donor) |
O5D | N | SER- 210 | 3.15 | 131.34 | H-Bond (Protein Donor) |
O1A | N | LEU- 212 | 3.01 | 146.34 | H-Bond (Protein Donor) |
C5B | CD1 | LEU- 212 | 4.47 | 0 | Hydrophobic |
C1B | CD1 | LEU- 212 | 4.31 | 0 | Hydrophobic |
O1A | N | SER- 214 | 3.11 | 141.84 | H-Bond (Protein Donor) |
O2N | OG | SER- 214 | 2.89 | 144.67 | H-Bond (Protein Donor) |
C4B | CG | PRO- 215 | 3.65 | 0 | Hydrophobic |
C1B | CG | PRO- 215 | 4.29 | 0 | Hydrophobic |
C3B | CB | ASP- 216 | 4.22 | 0 | Hydrophobic |
C4D | CG1 | ILE- 260 | 4.14 | 0 | Hydrophobic |
O2A | N | LYS- 262 | 2.84 | 174.71 | H-Bond (Protein Donor) |
O1X | NZ | LYS- 262 | 2.78 | 169.55 | H-Bond (Protein Donor) |
C5B | CD | LYS- 262 | 3.95 | 0 | Hydrophobic |
C3B | CD | LYS- 262 | 3.98 | 0 | Hydrophobic |
C5D | CB | LYS- 262 | 3.78 | 0 | Hydrophobic |
O1X | NZ | LYS- 262 | 2.78 | 0 | Ionic (Protein Cationic) |
O3X | OG | SER- 263 | 2.96 | 169.87 | H-Bond (Protein Donor) |
O1X | N | VAL- 264 | 3.21 | 144.09 | H-Bond (Protein Donor) |
O3X | OG1 | THR- 265 | 2.91 | 159.65 | H-Bond (Protein Donor) |
O2B | NH2 | ARG- 268 | 3.15 | 121.18 | H-Bond (Protein Donor) |
O3X | NH2 | ARG- 268 | 3.08 | 161.88 | H-Bond (Protein Donor) |
O3X | CZ | ARG- 268 | 3.97 | 0 | Ionic (Protein Cationic) |
N6A | OE1 | GLU- 271 | 3.03 | 165.06 | H-Bond (Ligand Donor) |
N7A | ND2 | ASN- 272 | 3.12 | 165.41 | H-Bond (Protein Donor) |
N6A | OD1 | ASN- 272 | 2.88 | 149.58 | H-Bond (Ligand Donor) |
C5N | SG | CYS- 298 | 3.87 | 0 | Hydrophobic |