2.530 Å
X-ray
2011-03-14
Name: | Beta-secretase 1 |
---|---|
ID: | BACE1_HUMAN |
AC: | P56817 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 3.4.23.46 |
Chain Name: | Percentage of Residues within binding site |
---|---|
E | 100 % |
B-Factor: | 21.029 |
---|---|
Number of residues: | 44 |
Including | |
Standard Amino Acids: | 44 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.886 | 914.625 |
% Hydrophobic | % Polar |
---|---|
27.31 | 72.69 |
According to VolSite |
HET Code: | PB0 |
---|---|
Formula: | C36H51F2N4O5 |
Molecular weight: | 657.811 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 59.74 % |
Polar Surface area: | 124.58 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 4 |
Rings: | 4 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 16 |
X | Y | Z |
---|---|---|
35.5327 | 18.2974 | 72.8584 |
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 |
C25 | CD1 | LEU- 30 | 3.95 | 0 | Hydrophobic |
F47 | CD2 | LEU- 30 | 3.35 | 0 | Hydrophobic |
O44 | OD1 | ASP- 32 | 3.2 | 175.24 | H-Bond (Ligand Donor) |
N37 | O | GLY- 34 | 2.96 | 162.41 | H-Bond (Ligand Donor) |
C30 | CB | SER- 35 | 4.38 | 0 | Hydrophobic |
C17 | CB | TYR- 71 | 4.07 | 0 | Hydrophobic |
C28 | CD1 | TYR- 71 | 3.67 | 0 | Hydrophobic |
C30 | CD1 | TYR- 71 | 4.22 | 0 | Hydrophobic |
C34 | CD1 | TYR- 71 | 4.33 | 0 | Hydrophobic |
F46 | CD2 | TYR- 71 | 3.78 | 0 | Hydrophobic |
C6 | CB | TYR- 71 | 3.34 | 0 | Hydrophobic |
C17 | CB | THR- 72 | 4.37 | 0 | Hydrophobic |
C31 | CB | THR- 72 | 4.01 | 0 | Hydrophobic |
C4 | CG2 | THR- 72 | 3.63 | 0 | Hydrophobic |
O43 | N | THR- 72 | 3.24 | 133.73 | H-Bond (Protein Donor) |
C31 | CB | GLN- 73 | 4.14 | 0 | Hydrophobic |
C5 | CB | GLN- 73 | 3.87 | 0 | Hydrophobic |
F46 | CD1 | PHE- 108 | 3.48 | 0 | Hydrophobic |
C26 | CG1 | ILE- 110 | 4.26 | 0 | Hydrophobic |
C35 | CD1 | ILE- 110 | 4.34 | 0 | Hydrophobic |
F47 | CD1 | ILE- 110 | 4.35 | 0 | Hydrophobic |
F47 | CH2 | TRP- 115 | 3.4 | 0 | Hydrophobic |
C28 | CD1 | ILE- 118 | 4.34 | 0 | Hydrophobic |
C24 | CD1 | ILE- 126 | 3.78 | 0 | Hydrophobic |
C20 | CE1 | TYR- 198 | 4.35 | 0 | Hydrophobic |
C24 | CE1 | TYR- 198 | 3.76 | 0 | Hydrophobic |
C32 | CE1 | TYR- 198 | 4.39 | 0 | Hydrophobic |
O45 | OH | TYR- 198 | 3.4 | 154.35 | H-Bond (Protein Donor) |
N37 | OD1 | ASP- 228 | 4 | 0 | Ionic (Ligand Cationic) |
N37 | OD2 | ASP- 228 | 2.79 | 0 | Ionic (Ligand Cationic) |
N37 | OD2 | ASP- 228 | 2.79 | 166.11 | H-Bond (Ligand Donor) |
N40 | O | GLY- 230 | 2.99 | 156.23 | H-Bond (Ligand Donor) |
C23 | CB | THR- 232 | 3.94 | 0 | Hydrophobic |
O41 | N | THR- 232 | 2.98 | 165.63 | H-Bond (Protein Donor) |
C4 | CD | ARG- 235 | 4.41 | 0 | Hydrophobic |