2.100 Å
X-ray
2002-02-01
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: | 25.680 |
---|---|
Number of residues: | 47 |
Including | |
Standard Amino Acids: | 44 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 2 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.364 | 847.125 |
% Hydrophobic | % Polar |
---|---|
44.62 | 55.38 |
According to VolSite |
HET Code: | ATP |
---|---|
Formula: | C10H12N5O13P3 |
Molecular weight: | 503.149 g/mol |
DrugBank ID: | DB00171 |
Buried Surface Area: | 69.78 % |
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 |
---|---|---|
-4.65765 | -13.5187 | 74.2569 |
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 |
O3G | N | SER- 14 | 2.85 | 156.56 | H-Bond (Protein Donor) |
O3G | OG | SER- 14 | 2.68 | 152.48 | H-Bond (Protein Donor) |
O3B | N | SER- 14 | 3.16 | 128.22 | H-Bond (Protein Donor) |
O2B | N | GLY- 15 | 2.89 | 142.83 | H-Bond (Protein Donor) |
O2B | N | LEU- 16 | 2.73 | 169.4 | H-Bond (Protein Donor) |
C5' | CD1 | LEU- 16 | 4.33 | 0 | Hydrophobic |
O1B | NZ | LYS- 18 | 2.76 | 132.87 | H-Bond (Protein Donor) |
O2A | NZ | LYS- 18 | 2.95 | 160.68 | H-Bond (Protein Donor) |
O1B | NZ | LYS- 18 | 2.76 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 18 | 3.33 | 0 | Ionic (Protein Cationic) |
O2A | NZ | LYS- 18 | 2.95 | 0 | Ionic (Protein Cationic) |
O3B | N | ASP- 157 | 3.31 | 172.59 | H-Bond (Protein Donor) |
O3A | N | ASP- 157 | 3.12 | 121.21 | H-Bond (Protein Donor) |
C3' | CB | ASP- 157 | 3.94 | 0 | Hydrophobic |
C4' | CB | ASP- 157 | 3.79 | 0 | Hydrophobic |
O3' | OD1 | ASP- 157 | 2.61 | 168.55 | H-Bond (Ligand Donor) |
O1G | N | GLY- 158 | 2.94 | 157.27 | H-Bond (Protein Donor) |
O1G | N | VAL- 159 | 3.15 | 154.85 | H-Bond (Protein Donor) |
O3' | NZ | LYS- 213 | 3.39 | 131.35 | H-Bond (Protein Donor) |
O2' | NZ | LYS- 213 | 2.91 | 155.21 | H-Bond (Protein Donor) |
O2' | OE2 | GLU- 214 | 2.59 | 157.91 | H-Bond (Ligand Donor) |
O1A | N | GLY- 302 | 2.93 | 176.78 | H-Bond (Protein Donor) |
O5' | N | GLY- 302 | 3.43 | 122.07 | H-Bond (Protein Donor) |
O2G | MG | MG- 395 | 2.36 | 0 | Metal Acceptor |
O1B | MG | MG- 395 | 2.26 | 0 | Metal Acceptor |
O3G | O | HOH- 432 | 2.88 | 154.8 | H-Bond (Protein Donor) |