2.000 Å
X-ray
2013-01-17
Name: | Mitochondrial FAD-linked sulfhydryl oxidase ERV1 |
---|---|
ID: | ERV1_YEAST |
AC: | P27882 |
Organism: | Saccharomyces cerevisiae |
Reign: | Eukaryota |
TaxID: | 559292 |
EC Number: | 1.8.3.2 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 13 % |
B | 87 % |
B-Factor: | 11.201 |
---|---|
Number of residues: | 48 |
Including | |
Standard Amino Acids: | 46 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | FAD |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.094 | 1005.750 |
% Hydrophobic | % Polar |
---|---|
56.04 | 43.96 |
According to VolSite |
HET Code: | FAD |
---|---|
Formula: | C27H31N9O15P2 |
Molecular weight: | 783.534 g/mol |
DrugBank ID: | DB03147 |
Buried Surface Area: | 68.05 % |
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 |
---|---|---|
-2.808 | 10.5522 | 37.58 |
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 |
C5' | CG | GLU- 88 | 3.77 | 0 | Hydrophobic |
C5' | CB | ARG- 92 | 4.46 | 0 | Hydrophobic |
O2P | NH2 | ARG- 92 | 3.02 | 146.69 | H-Bond (Protein Donor) |
O2P | NE | ARG- 92 | 3.2 | 141.17 | H-Bond (Protein Donor) |
O2P | CZ | ARG- 92 | 3.55 | 0 | Ionic (Protein Cationic) |
C8M | CB | SER- 94 | 3.87 | 0 | Hydrophobic |
C7M | CH2 | TRP- 95 | 3.85 | 0 | Hydrophobic |
C8M | CE2 | TRP- 95 | 3.23 | 0 | Hydrophobic |
C8 | CZ2 | TRP- 95 | 3.41 | 0 | Hydrophobic |
O2' | NE1 | TRP- 95 | 2.87 | 175.71 | H-Bond (Protein Donor) |
C7M | CD1 | LEU- 98 | 4.47 | 0 | Hydrophobic |
C8M | CD1 | LEU- 98 | 4.11 | 0 | Hydrophobic |
C7M | CE1 | PHE- 124 | 4.27 | 0 | Hydrophobic |
C8M | CZ | TYR- 128 | 3.93 | 0 | Hydrophobic |
C6 | CB | CYS- 133 | 3.92 | 0 | Hydrophobic |
C9A | SG | CYS- 133 | 4.2 | 0 | Hydrophobic |
C7M | CG | PHE- 137 | 3.84 | 0 | Hydrophobic |
N6A | O | CYS- 159 | 2.89 | 157 | H-Bond (Ligand Donor) |
O1A | NE2 | HIS- 162 | 2.96 | 170.79 | H-Bond (Protein Donor) |
DuAr | DuAr | HIS- 162 | 3.94 | 0 | Aromatic Face/Face |
N6A | OD1 | ASN- 163 | 3 | 126.05 | H-Bond (Ligand Donor) |
C6 | CG2 | VAL- 165 | 4.12 | 0 | Hydrophobic |
C9A | CG1 | VAL- 165 | 4.23 | 0 | Hydrophobic |
C2' | CG1 | VAL- 165 | 4.16 | 0 | Hydrophobic |
N7A | ND2 | ASN- 166 | 3.13 | 167.02 | H-Bond (Protein Donor) |
O4 | NZ | LYS- 168 | 3.46 | 157.06 | H-Bond (Protein Donor) |
C2' | CD1 | LEU- 169 | 3.76 | 0 | Hydrophobic |
O1P | NZ | LYS- 171 | 2.85 | 155.75 | H-Bond (Protein Donor) |
O1P | NZ | LYS- 171 | 2.85 | 0 | Ionic (Protein Cationic) |
DuAr | DuAr | PHE- 174 | 3.79 | 0 | Aromatic Face/Face |
C2B | CE1 | PHE- 174 | 4 | 0 | Hydrophobic |
O2B | NE | ARG- 182 | 2.83 | 155.41 | H-Bond (Protein Donor) |
C4B | CZ2 | TRP- 183 | 4.42 | 0 | Hydrophobic |
C1B | CZ2 | TRP- 183 | 4.04 | 0 | Hydrophobic |
N3A | NE1 | TRP- 183 | 2.97 | 165.5 | H-Bond (Protein Donor) |
O4' | O | HOH- 312 | 2.67 | 138.76 | H-Bond (Ligand Donor) |