2.400 Å
X-ray
1990-03-26
Name: | Glutathione reductase, mitochondrial |
---|---|
ID: | GSHR_HUMAN |
AC: | P00390 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 1.8.1.7 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 15.742 |
---|---|
Number of residues: | 68 |
Including | |
Standard Amino Acids: | 60 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 8 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.744 | 1782.000 |
% Hydrophobic | % Polar |
---|---|
46.40 | 53.60 |
According to VolSite |
HET Code: | FAD |
---|---|
Formula: | C27H31N9O15P2 |
Molecular weight: | 783.534 g/mol |
DrugBank ID: | DB03147 |
Buried Surface Area: | 72.49 % |
Polar Surface area: | 381.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 22 |
H-Bond Donors: | 7 |
Rings: | 6 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
60.6985 | 51.1368 | 19.1261 |
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 |
O1P | N | GLY- 31 | 2.69 | 164.43 | H-Bond (Protein Donor) |
O3B | OE1 | GLU- 50 | 2.8 | 175.61 | H-Bond (Ligand Donor) |
O3B | OE2 | GLU- 50 | 3.11 | 121.97 | H-Bond (Ligand Donor) |
O2B | OE2 | GLU- 50 | 2.54 | 161.66 | H-Bond (Ligand Donor) |
N3A | N | SER- 51 | 3.23 | 131.04 | H-Bond (Protein Donor) |
O1A | N | THR- 57 | 3.49 | 149.59 | H-Bond (Protein Donor) |
O1A | OG1 | THR- 57 | 2.94 | 162.05 | H-Bond (Protein Donor) |
O2A | N | THR- 57 | 3.06 | 140.48 | H-Bond (Protein Donor) |
C8M | CG2 | THR- 57 | 3.79 | 0 | Hydrophobic |
C2' | CB | CYS- 58 | 4.46 | 0 | Hydrophobic |
O4' | N | CYS- 58 | 3.5 | 124.39 | H-Bond (Protein Donor) |
C2' | SG | CYS- 63 | 4.28 | 0 | Hydrophobic |
N5 | NZ | LYS- 66 | 2.93 | 142.6 | H-Bond (Protein Donor) |
C6 | CB | LYS- 66 | 4.41 | 0 | Hydrophobic |
N6A | O | ALA- 130 | 2.96 | 164.73 | H-Bond (Ligand Donor) |
N1A | N | ALA- 130 | 2.82 | 177.38 | H-Bond (Protein Donor) |
C7M | CB | SER- 177 | 3.94 | 0 | Hydrophobic |
C7M | CE2 | PHE- 181 | 4.35 | 0 | Hydrophobic |
C8 | CD1 | ILE- 198 | 3.96 | 0 | Hydrophobic |
O3' | OD1 | ASP- 331 | 3.37 | 128.31 | H-Bond (Ligand Donor) |
O3' | OD2 | ASP- 331 | 2.74 | 169.03 | H-Bond (Ligand Donor) |
C5' | CB | ASP- 331 | 4.01 | 0 | Hydrophobic |
O2P | N | ASP- 331 | 2.96 | 143.8 | H-Bond (Protein Donor) |
O2 | N | THR- 339 | 3.21 | 159.55 | H-Bond (Protein Donor) |
C2' | CB | THR- 339 | 4.38 | 0 | Hydrophobic |
C4' | CB | THR- 339 | 4.45 | 0 | Hydrophobic |
O1P | O | HOH- 485 | 2.78 | 167.42 | H-Bond (Protein Donor) |
O1A | O | HOH- 491 | 3.19 | 179.98 | H-Bond (Protein Donor) |
O2A | O | HOH- 834 | 2.86 | 179.97 | H-Bond (Protein Donor) |