1.800 Å
X-ray
2014-05-14
Name: | Actin, alpha skeletal muscle |
---|---|
ID: | ACTS_RABIT |
AC: | P68135 |
Organism: | Oryctolagus cuniculus |
Reign: | Eukaryota |
TaxID: | 9986 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 29.005 |
---|---|
Number of residues: | 46 |
Including | |
Standard Amino Acids: | 42 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 2 |
Cofactors: | |
Metals: | CA |
Ligandability | Volume (Å3) |
---|---|
0.357 | 840.375 |
% Hydrophobic | % Polar |
---|---|
36.55 | 63.45 |
According to VolSite |
HET Code: | ATP |
---|---|
Formula: | C10H12N5O13P3 |
Molecular weight: | 503.149 g/mol |
DrugBank ID: | DB00171 |
Buried Surface Area: | 72.32 % |
Polar Surface area: | 319.88 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
0.282194 | 0.787935 | -18.196 |
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 |
O1G | N | SER- 14 | 2.92 | 159.62 | H-Bond (Protein Donor) |
O1G | OG | SER- 14 | 2.79 | 153.65 | H-Bond (Protein Donor) |
O3B | N | SER- 14 | 3.46 | 135.87 | H-Bond (Protein Donor) |
O2B | N | GLY- 15 | 2.85 | 142.65 | H-Bond (Protein Donor) |
O2B | N | LEU- 16 | 2.72 | 149.63 | H-Bond (Protein Donor) |
C5' | CD1 | LEU- 16 | 4.07 | 0 | Hydrophobic |
O1B | NZ | LYS- 18 | 2.91 | 123.21 | H-Bond (Protein Donor) |
O2A | NZ | LYS- 18 | 2.9 | 172.72 | H-Bond (Protein Donor) |
O1B | NZ | LYS- 18 | 2.91 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 18 | 3.59 | 0 | Ionic (Protein Cationic) |
O2A | NZ | LYS- 18 | 2.9 | 0 | Ionic (Protein Cationic) |
O3B | N | ASP- 157 | 2.89 | 166.33 | H-Bond (Protein Donor) |
O3A | N | ASP- 157 | 3.1 | 126.71 | H-Bond (Protein Donor) |
O3' | OD1 | ASP- 157 | 2.62 | 159.76 | H-Bond (Ligand Donor) |
C4' | CB | ASP- 157 | 3.94 | 0 | Hydrophobic |
O2G | N | GLY- 158 | 2.82 | 162.77 | H-Bond (Protein Donor) |
O2G | N | VAL- 159 | 3 | 151.13 | H-Bond (Protein Donor) |
O3' | NZ | LYS- 213 | 3.22 | 133.33 | H-Bond (Protein Donor) |
O2' | NZ | LYS- 213 | 2.92 | 150.18 | H-Bond (Protein Donor) |
O2' | OE2 | GLU- 214 | 2.71 | 161.43 | H-Bond (Ligand Donor) |
O1A | N | GLY- 302 | 3.01 | 169.76 | H-Bond (Protein Donor) |
O5' | N | GLY- 302 | 3.38 | 129.1 | H-Bond (Protein Donor) |
O3G | CA | CA- 402 | 2.37 | 0 | Metal Acceptor |
O1B | CA | CA- 402 | 2.28 | 0 | Metal Acceptor |
N3 | O | HOH- 555 | 2.92 | 165.08 | H-Bond (Protein Donor) |