2.500 Å
X-ray
1999-06-04
Name: | Protein claret segregational |
---|---|
ID: | NCD_DROME |
AC: | P20480 |
Organism: | Drosophila melanogaster |
Reign: | Eukaryota |
TaxID: | 7227 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 13.292 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.182 | 256.500 |
% Hydrophobic | % Polar |
---|---|
64.47 | 35.53 |
According to VolSite |
HET Code: | ADP |
---|---|
Formula: | C10H12N5O10P2 |
Molecular weight: | 424.177 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 51.74 % |
Polar Surface area: | 260.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 14 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 3 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 6 |
X | Y | Z |
---|---|---|
6.19448 | 53.4542 | 43.9998 |
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 |
C1' | CD2 | LEU- 359 | 3.82 | 0 | Hydrophobic |
O1B | N | GLY- 437 | 2.6 | 153.75 | H-Bond (Protein Donor) |
O2B | OG | SER- 438 | 3.21 | 153.43 | H-Bond (Protein Donor) |
O2B | N | SER- 438 | 2.76 | 128.92 | H-Bond (Protein Donor) |
O2B | N | GLY- 439 | 3.34 | 162.8 | H-Bond (Protein Donor) |
O1B | NZ | LYS- 440 | 3.68 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 440 | 2.95 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 440 | 2.95 | 128.65 | H-Bond (Protein Donor) |
O2A | N | TYR- 442 | 3 | 169.54 | H-Bond (Protein Donor) |
C5' | CB | TYR- 442 | 3.67 | 0 | Hydrophobic |
C2' | CD2 | TYR- 442 | 3.7 | 0 | Hydrophobic |
DuAr | DuAr | TYR- 442 | 3.75 | 0 | Aromatic Face/Face |