1.900 Å
X-ray
2009-09-07
Name: | FAD synthase |
---|---|
ID: | FAD1_YEAST |
AC: | P38913 |
Organism: | Saccharomyces cerevisiae |
Reign: | Eukaryota |
TaxID: | 559292 |
EC Number: | 2.7.7.2 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 20.256 |
---|---|
Number of residues: | 41 |
Including | |
Standard Amino Acids: | 39 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.663 | 884.250 |
% Hydrophobic | % Polar |
---|---|
37.02 | 62.98 |
According to VolSite |
HET Code: | FAD |
---|---|
Formula: | C27H31N9O15P2 |
Molecular weight: | 783.534 g/mol |
DrugBank ID: | DB03147 |
Buried Surface Area: | 56.98 % |
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 |
---|---|---|
24.8818 | 20.6499 | 23.8362 |
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 |
O2B | OG | SER- 59 | 3.14 | 169.86 | H-Bond (Ligand Donor) |
C1B | CB | SER- 59 | 4.29 | 0 | Hydrophobic |
N7A | ND2 | ASN- 61 | 3.29 | 134.8 | H-Bond (Protein Donor) |
C2B | CB | CYS- 66 | 4.19 | 0 | Hydrophobic |
N6A | O | ILE- 107 | 2.91 | 169.47 | H-Bond (Ligand Donor) |
N1A | N | ILE- 107 | 2.9 | 170.02 | H-Bond (Protein Donor) |
C8M | CE | MET- 144 | 3.87 | 0 | Hydrophobic |
C7M | CZ | PHE- 148 | 3.66 | 0 | Hydrophobic |
C8M | CE1 | PHE- 148 | 4.16 | 0 | Hydrophobic |
C7M | CG2 | ILE- 161 | 4.07 | 0 | Hydrophobic |
C1B | CG2 | ILE- 163 | 4.31 | 0 | Hydrophobic |
C8M | CG2 | ILE- 163 | 4.39 | 0 | Hydrophobic |
C4B | CG2 | ILE- 163 | 3.56 | 0 | Hydrophobic |
C7 | CD1 | ILE- 163 | 3.52 | 0 | Hydrophobic |
O3B | O | GLY- 164 | 3.38 | 136.57 | H-Bond (Ligand Donor) |
O2B | N | GLY- 164 | 2.96 | 176.98 | H-Bond (Protein Donor) |
C5B | CB | ILE- 165 | 4.23 | 0 | Hydrophobic |
C3' | CD1 | ILE- 165 | 3.86 | 0 | Hydrophobic |
N3 | OD2 | ASP- 182 | 2.63 | 141.18 | H-Bond (Ligand Donor) |
O4 | N | ASP- 182 | 2.82 | 166.39 | H-Bond (Protein Donor) |
C7M | CZ3 | TRP- 185 | 4.23 | 0 | Hydrophobic |
C1' | CZ2 | TRP- 185 | 3.99 | 0 | Hydrophobic |
DuAr | DuAr | TRP- 185 | 3.69 | 0 | Aromatic Face/Face |
C7M | CZ | PHE- 188 | 3.95 | 0 | Hydrophobic |
C6 | CD | ARG- 190 | 4.29 | 0 | Hydrophobic |
O1P | NH1 | ARG- 300 | 2.78 | 125.63 | H-Bond (Protein Donor) |
O1P | CZ | ARG- 300 | 3.58 | 0 | Ionic (Protein Cationic) |