2.300 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: | 41.523 |
---|---|
Number of residues: | 47 |
Including | |
Standard Amino Acids: | 43 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 2 |
Cofactors: | |
Metals: | CA |
Ligandability | Volume (Å3) |
---|---|
0.450 | 769.500 |
% Hydrophobic | % Polar |
---|---|
44.30 | 55.70 |
According to VolSite |
HET Code: | ATP |
---|---|
Formula: | C10H12N5O13P3 |
Molecular weight: | 503.149 g/mol |
DrugBank ID: | DB00171 |
Buried Surface Area: | 72.14 % |
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 |
---|---|---|
5.03016 | 4.552 | -21.6795 |
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 | OG | SER- 14 | 2.76 | 154.37 | H-Bond (Protein Donor) |
O1G | N | SER- 14 | 2.86 | 163.25 | H-Bond (Protein Donor) |
O3B | N | SER- 14 | 3.38 | 128.63 | H-Bond (Protein Donor) |
O1B | N | GLY- 15 | 2.86 | 154.47 | H-Bond (Protein Donor) |
O1B | N | LEU- 16 | 2.81 | 153.46 | H-Bond (Protein Donor) |
C5' | CD1 | LEU- 16 | 3.75 | 0 | Hydrophobic |
O1B | NZ | LYS- 18 | 3.6 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 18 | 2.88 | 0 | Ionic (Protein Cationic) |
O2A | NZ | LYS- 18 | 2.8 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 18 | 2.88 | 122.17 | H-Bond (Protein Donor) |
O2A | NZ | LYS- 18 | 2.8 | 169.04 | H-Bond (Protein Donor) |
O3B | N | ASP- 157 | 2.96 | 172.81 | H-Bond (Protein Donor) |
O3A | N | ASP- 157 | 3.15 | 122.36 | H-Bond (Protein Donor) |
O3' | OD1 | ASP- 157 | 2.58 | 159.76 | H-Bond (Ligand Donor) |
C4' | CB | ASP- 157 | 3.97 | 0 | Hydrophobic |
O2G | N | GLY- 158 | 2.71 | 148.58 | H-Bond (Protein Donor) |
O2G | N | VAL- 159 | 2.9 | 157.19 | H-Bond (Protein Donor) |
O2' | NZ | LYS- 213 | 3.12 | 157.28 | H-Bond (Protein Donor) |
O2' | OE2 | GLU- 214 | 2.74 | 165.97 | H-Bond (Ligand Donor) |
O1A | N | GLY- 302 | 3.02 | 166.08 | H-Bond (Protein Donor) |
O5' | N | GLY- 302 | 3.45 | 129.13 | H-Bond (Protein Donor) |
O3G | CA | CA- 402 | 2.37 | 0 | Metal Acceptor |
O2B | CA | CA- 402 | 2.26 | 0 | Metal Acceptor |