1.750 Å
X-ray
2003-09-09
Name: | Endoplasmin |
---|---|
ID: | ENPL_CANLF |
AC: | P41148 |
Organism: | Canis lupus familiaris |
Reign: | Eukaryota |
TaxID: | 9615 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 24.986 |
---|---|
Number of residues: | 36 |
Including | |
Standard Amino Acids: | 33 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.201 | 529.875 |
% Hydrophobic | % Polar |
---|---|
43.31 | 56.69 |
According to VolSite |
HET Code: | NEC |
---|---|
Formula: | C12H16N6O4 |
Molecular weight: | 308.293 g/mol |
DrugBank ID: | DB03719 |
Buried Surface Area: | 54.96 % |
Polar Surface area: | 148.41 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 8 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 3 |
X | Y | Z |
---|---|---|
18.973 | -17.6053 | 53.961 |
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 |
C52 | CE | MET- 85 | 4.49 | 0 | Hydrophobic |
N6 | OD2 | ASP- 149 | 2.87 | 161.49 | H-Bond (Ligand Donor) |
C1' | SD | MET- 154 | 3.55 | 0 | Hydrophobic |
N5' | O | ASN- 162 | 3.02 | 129.33 | H-Bond (Ligand Donor) |
O2' | OD1 | ASN- 162 | 3.06 | 144.58 | H-Bond (Ligand Donor) |
C4' | CB | ASN- 162 | 4.06 | 0 | Hydrophobic |
C1' | CB | ASN- 162 | 4.25 | 0 | Hydrophobic |
C4' | CD2 | LEU- 163 | 4.38 | 0 | Hydrophobic |
C52 | CB | VAL- 197 | 3.86 | 0 | Hydrophobic |
C52 | CE2 | TYR- 200 | 3.36 | 0 | Hydrophobic |
N1 | O | HOH- 402 | 2.73 | 155.22 | H-Bond (Protein Donor) |
O5' | O | HOH- 403 | 2.59 | 179.97 | H-Bond (Protein Donor) |