2.050 Å
X-ray
2013-09-06
Name: | SADH |
---|---|
ID: | O42703_CANPA |
AC: | O42703 |
Organism: | Candida parapsilosis |
Reign: | Eukaryota |
TaxID: | 5480 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 4 % |
B | 96 % |
B-Factor: | 32.334 |
---|---|
Number of residues: | 55 |
Including | |
Standard Amino Acids: | 49 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 4 |
Cofactors: | |
Metals: | ZN ZN |
Ligandability | Volume (Å3) |
---|---|
1.523 | 1302.750 |
% Hydrophobic | % Polar |
---|---|
56.99 | 43.01 |
According to VolSite |
HET Code: | NAD |
---|---|
Formula: | C21H26N7O14P2 |
Molecular weight: | 662.417 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 66.72 % |
Polar Surface area: | 343.54 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 18 |
H-Bond Donors: | 6 |
Rings: | 5 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 1 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 11 |
X | Y | Z |
---|---|---|
-38.4241 | -4.77518 | 4.70095 |
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 |
C5N | SG | CYS- 44 | 4 | 0 | Hydrophobic |
C3D | CB | HIS- 45 | 4.07 | 0 | Hydrophobic |
O2D | OG | SER- 46 | 2.92 | 163.96 | H-Bond (Ligand Donor) |
O3D | NE2 | HIS- 49 | 3.38 | 165.02 | H-Bond (Protein Donor) |
O2D | NE2 | HIS- 49 | 2.83 | 122.36 | H-Bond (Protein Donor) |
C4N | CG2 | THR- 158 | 3.66 | 0 | Hydrophobic |
O2A | N | GLY- 181 | 2.88 | 166.84 | H-Bond (Protein Donor) |
O2N | N | LEU- 182 | 2.74 | 178.84 | H-Bond (Protein Donor) |
C5N | CD2 | LEU- 182 | 3.78 | 0 | Hydrophobic |
O3B | OD2 | ASP- 201 | 2.72 | 161.48 | H-Bond (Ligand Donor) |
O2B | OD1 | ASP- 201 | 2.63 | 144.52 | H-Bond (Ligand Donor) |
N3A | N | LYS- 202 | 3.34 | 148.07 | H-Bond (Protein Donor) |
C1B | CG2 | VAL- 238 | 4.35 | 0 | Hydrophobic |
N7N | O | VAL- 260 | 2.96 | 167.56 | H-Bond (Ligand Donor) |
O3D | N | LEU- 262 | 3.08 | 164.1 | H-Bond (Protein Donor) |
C3N | CD1 | LEU- 262 | 4.36 | 0 | Hydrophobic |
N7N | O | SER- 284 | 3.3 | 163.23 | H-Bond (Ligand Donor) |
O7N | N | TRP- 286 | 2.74 | 148.17 | H-Bond (Protein Donor) |
O2B | ND2 | ASN- 326 | 3.07 | 159.18 | H-Bond (Protein Donor) |
O1N | NH1 | ARG- 331 | 2.7 | 175.2 | H-Bond (Protein Donor) |
O1N | NH2 | ARG- 331 | 3.41 | 130.52 | H-Bond (Protein Donor) |
O1N | CZ | ARG- 331 | 3.51 | 0 | Ionic (Protein Cationic) |
O2N | O | HOH- 2055 | 2.81 | 179.95 | H-Bond (Protein Donor) |