2.900 Å
X-ray
2006-10-27
Name: | Elongation factor 2 |
---|---|
ID: | EF2_YEAST |
AC: | P32324 |
Organism: | Saccharomyces cerevisiae |
Reign: | Eukaryota |
TaxID: | 559292 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 38.305 |
---|---|
Number of residues: | 41 |
Including | |
Standard Amino Acids: | 41 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.201 | 627.750 |
% Hydrophobic | % Polar |
---|---|
55.91 | 44.09 |
According to VolSite |
HET Code: | MOU |
---|---|
Formula: | C37H52O12 |
Molecular weight: | 688.802 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 62.17 % |
Polar Surface area: | 180.77 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 12 |
H-Bond Donors: | 1 |
Rings: | 6 |
Aromatic rings: | 0 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 15 |
X | Y | Z |
---|---|---|
2.90057 | 15.1976 | 41.902 |
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 |
C2 | CB | PRO- 487 | 3.93 | 0 | Hydrophobic |
C41 | CG | GLN- 490 | 3.62 | 0 | Hydrophobic |
C43 | CG | GLN- 490 | 4.37 | 0 | Hydrophobic |
C2 | CD2 | LEU- 519 | 3.9 | 0 | Hydrophobic |
C36 | CD2 | LEU- 519 | 4.18 | 0 | Hydrophobic |
C31 | CD2 | LEU- 519 | 4.35 | 0 | Hydrophobic |
C22 | CE1 | TYR- 521 | 4.06 | 0 | Hydrophobic |
C26 | CE1 | TYR- 521 | 3.92 | 0 | Hydrophobic |
C28 | CZ | TYR- 521 | 3.94 | 0 | Hydrophobic |
C30 | CZ | TYR- 521 | 3.67 | 0 | Hydrophobic |
C34 | CG | TYR- 521 | 3.98 | 0 | Hydrophobic |
C22 | CB | SER- 523 | 4.38 | 0 | Hydrophobic |
C14 | CB | GLU- 524 | 4.21 | 0 | Hydrophobic |
O24 | N | GLU- 524 | 2.77 | 152.25 | H-Bond (Protein Donor) |
O25 | N | GLU- 524 | 3.36 | 146.49 | H-Bond (Protein Donor) |
C22 | CG1 | ILE- 529 | 3.99 | 0 | Hydrophobic |
C39 | CB | ALA- 531 | 4.49 | 0 | Hydrophobic |
C21 | CB | PRO- 559 | 4.03 | 0 | Hydrophobic |
C22 | CB | PRO- 559 | 4.27 | 0 | Hydrophobic |
C21 | CG2 | VAL- 561 | 4.3 | 0 | Hydrophobic |
O12 | N | ALA- 562 | 2.84 | 174.15 | H-Bond (Protein Donor) |
C7 | CB | PRO- 727 | 3.52 | 0 | Hydrophobic |
C6 | CE1 | PHE- 729 | 4.17 | 0 | Hydrophobic |
C32 | CE1 | PHE- 729 | 4.39 | 0 | Hydrophobic |
C21 | CG1 | VAL- 774 | 4.14 | 0 | Hydrophobic |
C7 | CG2 | VAL- 774 | 4.12 | 0 | Hydrophobic |
C43 | CB | SER- 777 | 4.47 | 0 | Hydrophobic |
C44 | CB | PHE- 780 | 4.4 | 0 | Hydrophobic |
C44 | CG2 | THR- 781 | 3.92 | 0 | Hydrophobic |
O46 | N | THR- 781 | 3.02 | 138.88 | H-Bond (Protein Donor) |
C38 | CG | MET- 796 | 4.34 | 0 | Hydrophobic |
C40 | CG | MET- 796 | 3.62 | 0 | Hydrophobic |
C6 | CB | PHE- 798 | 4.28 | 0 | Hydrophobic |
C7 | CD1 | PHE- 798 | 4 | 0 | Hydrophobic |
C13 | CB | PHE- 798 | 3.92 | 0 | Hydrophobic |
C17 | CE2 | PHE- 798 | 3.83 | 0 | Hydrophobic |
C18 | CZ | PHE- 798 | 4.28 | 0 | Hydrophobic |
C16 | CD2 | PHE- 798 | 3.64 | 0 | Hydrophobic |
O33 | N | PHE- 798 | 3.21 | 169.14 | H-Bond (Protein Donor) |
C18 | CZ2 | TRP- 801 | 3.46 | 0 | Hydrophobic |